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Conserved domains on  [gi|22326858|ref|NP_197195|]
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AAA-type ATPase family protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ATAD3_N pfam12037
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ...
64-333 8.91e-134

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: 392.81  E-value: 8.91e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858    64 AGEESDAPPRIRNNNPRTTSAGFDPEALERGAKALKGINNSAHAKKVFESIKTREETRQAEFTAKAQEFKAMQSQAEAER 143
Cdd:pfam12037   1 GGPGSDKDPKKSNDKPRTAYSGFDPEALERAAKAARELESSPHAKKALELMKKQEQTRQAELQAKIKEYEAAQEQLKIER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   144 QRVIYEEQKKLAQHQAQTKSQMARYEDELARKRMQAENEAQRTRNQELVKMQEESAIRREVARrateeeIQAQRRQTERE 223
Cdd:pfam12037  81 QRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEELLRKQEESVAKQEAMR------IQAQRRQTEEH 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   224 KAEIERETIRVKAMAEAEGRARESKLSEDVNRRMLVDRANAEREKWVSAINTTFDHIGGGLRTILTDQNKLIVAVGGLTA 303
Cdd:pfam12037 155 EAELRRETERAKAEAEAEARAKEERENEDLNLEQLREKANEERETVLESINTAGSHIGGGLRALLTDWDKLVAAVGGLTA 234
                         250       260       270
                  ....*....|....*....|....*....|
gi 22326858   304 LAAGIYTTREGAKVIWSYVDRILGQPSLIR 333
Cdd:pfam12037 235 LAAGVYTAKEGTGVAWRYIEARLGKPSLVR 264
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
377-526 4.77e-83

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member cd19512:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 150  Bit Score: 257.84  E-value: 4.77e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 377 LEKRIEQLANATANTKAHQAPFRNILFYGPPGTGKTMAARELARRSGLDYALMTGGDVAPLGAQAVTKIHQLFDWSKKSK 456
Cdd:cd19512   1 LEARVRDIAIATRNTKKNKGLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAIHKVFDWANTSR 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 457 RGLLLFIDEADAFLCERNKTYMSEAQRSALNALLFRTGDQSKDIVLALATNRPGDLDSAVADRIDETLEF 526
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 ...
64-333 8.91e-134

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: 392.81  E-value: 8.91e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858    64 AGEESDAPPRIRNNNPRTTSAGFDPEALERGAKALKGINNSAHAKKVFESIKTREETRQAEFTAKAQEFKAMQSQAEAER 143
Cdd:pfam12037   1 GGPGSDKDPKKSNDKPRTAYSGFDPEALERAAKAARELESSPHAKKALELMKKQEQTRQAELQAKIKEYEAAQEQLKIER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   144 QRVIYEEQKKLAQHQAQTKSQMARYEDELARKRMQAENEAQRTRNQELVKMQEESAIRREVARrateeeIQAQRRQTERE 223
Cdd:pfam12037  81 QRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEELLRKQEESVAKQEAMR------IQAQRRQTEEH 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   224 KAEIERETIRVKAMAEAEGRARESKLSEDVNRRMLVDRANAEREKWVSAINTTFDHIGGGLRTILTDQNKLIVAVGGLTA 303
Cdd:pfam12037 155 EAELRRETERAKAEAEAEARAKEERENEDLNLEQLREKANEERETVLESINTAGSHIGGGLRALLTDWDKLVAAVGGLTA 234
                         250       260       270
                  ....*....|....*....|....*....|
gi 22326858   304 LAAGIYTTREGAKVIWSYVDRILGQPSLIR 333
Cdd:pfam12037 235 LAAGVYTAKEGTGVAWRYIEARLGKPSLVR 264
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
377-526 4.77e-83

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: 257.84  E-value: 4.77e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 377 LEKRIEQLANATANTKAHQAPFRNILFYGPPGTGKTMAARELARRSGLDYALMTGGDVAPLGAQAVTKIHQLFDWSKKSK 456
Cdd:cd19512   1 LEARVRDIAIATRNTKKNKGLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAIHKVFDWANTSR 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 457 RGLLLFIDEADAFLCERNKTYMSEAQRSALNALLFRTGDQSKDIVLALATNRPGDLDSAVADRIDETLEF 526
Cdd:cd19512  81 RGLLLFVDEADAFLRKRSTEKISEDLRAALNAFLYRTGEQSNKFMLVLASNQPEQFDWAINDRIDEMVEF 150
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
368-636 8.90e-35

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 132.32  E-value: 8.90e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 368 FGDVILRPALEKRIEQLA---NATANTKAH-QAPFRNILFYGPPGTGKTMAARELARRSGLDYALMTGGDV--APLGaQA 441
Cdd:COG1223   1 LDDVVGQEEAKKKLKLIIkelRRRENLRKFgLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLigSYLG-ET 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 442 VTKIHQLFDWSKKskRGLLLFIDEADAFLCER-NKTYMSEAQRsALNALL-FRTGDQSKDIVLAlATNRPGDLDSAVADR 519
Cdd:COG1223  80 ARNLRKLFDFARR--APCVIFFDEFDAIAKDRgDQNDVGEVKR-VVNALLqELDGLPSGSVVIA-ATNHPELLDSALWRR 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 520 IDETLEFPLPGEEERFKLLNLYLEKYISKTNLkkpgllqslfkkeqqtieikgvtedLLKEAAAKTKGFSGREIAKLM-A 598
Cdd:COG1223 156 FDEVIEFPLPDKEERKEILELNLKKFPLPFEL-------------------------DLKKLAKKLEGLSGADIEKVLkT 210
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 22326858 599 SVQAAVYGSANCLLdanlfREVIDYKVAEHQQRKKLAG 636
Cdd:COG1223 211 ALKKAILEDREKVT-----KEDLEEALKQRKERKKEPK 243
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
215-603 2.67e-33

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: 131.96  E-value: 2.67e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 215 AQRRQTEREKAEIERETIRVKAMAEAEGRARESKLSEDVNRRMLVDRANAEREKWVSAINTTFDHIGGGLRTILTDQNKL 294
Cdd:COG0464   2 AELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLAL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 295 IVAVGGLTALAAGIYTTREGAKVIWSYVDRILGQPSLIRESSRGKYPWSGSASRVLSTLRGGGKESTSKTGK-GFGDVIL 373
Cdd:COG0464  82 LAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREaILDDLGG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 374 RPALEKRIEQLANA-TANTKAHQA----PFRNILFYGPPGTGKTMAARELARRSGLDYALMTGGDVA--PLGaQAVTKIH 446
Cdd:COG0464 162 LEEVKEELRELVALpLKRPELREEyglpPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVskYVG-ETEKNLR 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 447 QLFDWSKKSKRGLLlFIDEADAFLCERNKTyMSEAQRSALNALLFRTGDQSKDIVLALATNRPGDLDSAVADRIDETLEF 526
Cdd:COG0464 241 EVFDKARGLAPCVL-FIDEADALAGKRGEV-GDGVGRRVVNTLLTEMEELRSDVVVIAATNRPDLLDPALLRRFDEIIFF 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 527 PLPGEEERFKLLNLYLEKYisktnlkkpgllqslfkkeqqtieikGVTEDL-LKEAAAKTKGFSGREIAKLM--ASVQAA 603
Cdd:COG0464 319 PLPDAEERLEIFRIHLRKR--------------------------PLDEDVdLEELAEATEGLSGADIRNVVrrAALQAL 372
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
401-528 6.88e-27

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: 105.75  E-value: 6.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   401 ILFYGPPGTGKTMAARELARRSGLDYALMTGGDVAPLGA-QAVTKIHQLFDWSKKSKRGlLLFIDEADAFLCERNKTYMS 479
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVgESEKRLRELFEAAKKLAPC-VIFIDEIDALAGSRGSGGDS 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 22326858   480 EAQRsALNALLFR----TGDQSKDIVLAlATNRPGDLDSAVADRIDETLEFPL 528
Cdd:pfam00004  80 ESRR-VVNQLLTEldgfTSSNSKVIVIA-ATNRPDKLDPALLGRFDRIIEFPL 130
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
397-596 1.58e-12

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: 70.71  E-value: 1.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   397 PFRNILFYGPPGTGKTMAARELARRSGLDYALMTGGDV-APLGAQAVTKIHQLFDWSKKSKRGLLlFIDEADAFLCERNK 475
Cdd:TIGR01243 486 PPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEIlSKWVGESEKAIREIFRKARQAAPAII-FFDEIDAIAPARGA 564
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   476 TYMSEAQRSALNALLFRTG--DQSKDIVLALATNRPGDLDSAV--ADRIDETLEFPLPGEEERFKLLNLYLEKYisktnl 551
Cdd:TIGR01243 565 RFDTSVTDRIVNQLLTEMDgiQELSNVVVIAATNRPDILDPALlrPGRFDRLILVPPPDEEARKEIFKIHTRSM------ 638
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 22326858   552 kkpgllqslfkkeqqtieikGVTEDL-LKEAAAKTKGFSGREIAKL 596
Cdd:TIGR01243 639 --------------------PLAEDVdLEELAEMTEGYTGADIEAV 664
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
397-551 8.58e-12

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 67.48  E-value: 8.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858  397 PFRNILFYGPPGTGKTMAARELARRSGLDYALMTGGD-VAPLGAQAVTKIHQLFDWSKKSKRGlLLFIDEADAFLCERNK 475
Cdd:PTZ00454 178 PPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEfVQKYLGEGPRMVRDVFRLARENAPS-IIFIDEVDSIATKRFD 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858  476 TYMS---EAQRSALNALLFRTG-DQSKDIVLALATNRPGDLDSAV--ADRIDETLEFPLPGEEERfkllNLYLEKYISKT 549
Cdd:PTZ00454 257 AQTGadrEVQRILLELLNQMDGfDQTTNVKVIMATNRADTLDPALlrPGRLDRKIEFPLPDRRQK----RLIFQTITSKM 332

                 ..
gi 22326858  550 NL 551
Cdd:PTZ00454 333 NL 334
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
397-529 1.83e-09

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 56.61  E-value: 1.83e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858    397 PFRNILFYGPPGTGKTMAARELARRSG------------------LDYALMTGGDVAPLGAQAVTKIHQLFDWSKKSKRG 458
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGppgggviyidgedileevLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22326858    459 lLLFIDEADAFLceRNKTYMSEAQRSALNALLFRTGDQSKDIVlaLATNRPGDLDSA-VADRIDETLEFPLP 529
Cdd:smart00382  81 -VLILDEITSLL--DAEQEALLLLLEELRLLLLLKSEKNLTVI--LTTNDEKDLGPAlLRRRFDRRIVLLLI 147
PTZ00121 PTZ00121
MAEBL; Provisional
92-268 6.82e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.38  E-value: 6.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858    92 ERGAKALKGINNSAHAKKVFESIKTREETRQAEFTAKAQEFKAMQSQAEAERQRVIYEEQK--KLAQHQAQTKSQMARYE 169
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKaeELKKAEEKKKAEEAKKA 1572
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   170 DE---LARKRMQAENEAQRTRNQELVKM-QEESAIRREVARRATEEEIQA-QRRQTEREKAEIERETirvKAMAEAEGRA 244
Cdd:PTZ00121 1573 EEdknMALRKAEEAKKAEEARIEEVMKLyEEEKKMKAEEAKKAEEAKIKAeELKKAEEEKKKVEQLK---KKEAEEKKKA 1649
                         170       180
                  ....*....|....*....|....*
gi 22326858   245 RESKLSEDVNR-RMLVDRANAEREK 268
Cdd:PTZ00121 1650 EELKKAEEENKiKAAEEAKKAEEDK 1674
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
101-197 6.43e-05

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: 43.34  E-value: 6.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858    101 INNSAHAKKVFESIKTREETRQAEFTAKAQEFKAMQSQAEAERQRVIYEEQKKLAQhqaqtksQMARYEDELARKRMQAE 180
Cdd:smart00935  10 LQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEAAREKKEK-------ELQKKVQEFQRKQQKLQ 82
                           90
                   ....*....|....*..
gi 22326858    181 NEAQRTRNQELVKMQEE 197
Cdd:smart00935  83 QDLQKRQQEELQKILDK 99
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
118-266 1.23e-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: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   118 EETRQAEFTAKAQEFKAMQsqaEAERQRVIYEEQKKLAQHQAQTKSQMARYEDELARKRMQAENEAQRTRNQELVKMQEE 197
Cdd:TIGR02794  87 EQARQKELEQRAAAEKAAK---QAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAE 163
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22326858   198 SAIRREVARRATEEEIQAQ---RRQTEREKAEIERETIRVKAMAEAEGRARESKlsedvnrrMLVDRANAER 266
Cdd:TIGR02794 164 AKKKAEEAKKKAEAEAKAKaeaEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEA--------AAAAAAEAER 227
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
140-250 7.77e-03

Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.


Pssm-ID: 259804 [Multi-domain]  Cd Length: 293  Bit Score: 38.82  E-value: 7.77e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 140 EAERQRV-IYEEQKKLAQHQAQTKsqmaryedelaRKR--MQAENEAQ--RTRNQELVkMQEESAIRRevarrateEEIQ 214
Cdd:cd03406 172 EAEKTKLlIAEQHQKVVEKEAETE-----------RKRavIEAEKDAEvaKIQMQQKI-MEKEAEKKI--------SEIE 231
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 22326858 215 AQRRqTEREKAEIERETIRVKAMAEAEgrarESKLS 250
Cdd:cd03406 232 DEMH-LAREKARADAEYYRALREAEAN----KLKLT 262
 
Name Accession Description Interval E-value
ATAD3_N pfam12037
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ...
64-333 8.91e-134

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: 392.81  E-value: 8.91e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858    64 AGEESDAPPRIRNNNPRTTSAGFDPEALERGAKALKGINNSAHAKKVFESIKTREETRQAEFTAKAQEFKAMQSQAEAER 143
Cdd:pfam12037   1 GGPGSDKDPKKSNDKPRTAYSGFDPEALERAAKAARELESSPHAKKALELMKKQEQTRQAELQAKIKEYEAAQEQLKIER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   144 QRVIYEEQKKLAQHQAQTKSQMARYEDELARKRMQAENEAQRTRNQELVKMQEESAIRREVARrateeeIQAQRRQTERE 223
Cdd:pfam12037  81 QRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEELLRKQEESVAKQEAMR------IQAQRRQTEEH 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   224 KAEIERETIRVKAMAEAEGRARESKLSEDVNRRMLVDRANAEREKWVSAINTTFDHIGGGLRTILTDQNKLIVAVGGLTA 303
Cdd:pfam12037 155 EAELRRETERAKAEAEAEARAKEERENEDLNLEQLREKANEERETVLESINTAGSHIGGGLRALLTDWDKLVAAVGGLTA 234
                         250       260       270
                  ....*....|....*....|....*....|
gi 22326858   304 LAAGIYTTREGAKVIWSYVDRILGQPSLIR 333
Cdd:pfam12037 235 LAAGVYTAKEGTGVAWRYIEARLGKPSLVR 264
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
377-526 4.77e-83

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: 257.84  E-value: 4.77e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 377 LEKRIEQLANATANTKAHQAPFRNILFYGPPGTGKTMAARELARRSGLDYALMTGGDVAPLGAQAVTKIHQLFDWSKKSK 456
Cdd:cd19512   1 LEARVRDIAIATRNTKKNKGLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAIHKVFDWANTSR 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 457 RGLLLFIDEADAFLCERNKTYMSEAQRSALNALLFRTGDQSKDIVLALATNRPGDLDSAVADRIDETLEF 526
Cdd:cd19512  81 RGLLLFVDEADAFLRKRSTEKISEDLRAALNAFLYRTGEQSNKFMLVLASNQPEQFDWAINDRIDEMVEF 150
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
368-636 8.90e-35

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 132.32  E-value: 8.90e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 368 FGDVILRPALEKRIEQLA---NATANTKAH-QAPFRNILFYGPPGTGKTMAARELARRSGLDYALMTGGDV--APLGaQA 441
Cdd:COG1223   1 LDDVVGQEEAKKKLKLIIkelRRRENLRKFgLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLigSYLG-ET 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 442 VTKIHQLFDWSKKskRGLLLFIDEADAFLCER-NKTYMSEAQRsALNALL-FRTGDQSKDIVLAlATNRPGDLDSAVADR 519
Cdd:COG1223  80 ARNLRKLFDFARR--APCVIFFDEFDAIAKDRgDQNDVGEVKR-VVNALLqELDGLPSGSVVIA-ATNHPELLDSALWRR 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 520 IDETLEFPLPGEEERFKLLNLYLEKYISKTNLkkpgllqslfkkeqqtieikgvtedLLKEAAAKTKGFSGREIAKLM-A 598
Cdd:COG1223 156 FDEVIEFPLPDKEERKEILELNLKKFPLPFEL-------------------------DLKKLAKKLEGLSGADIEKVLkT 210
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 22326858 599 SVQAAVYGSANCLLdanlfREVIDYKVAEHQQRKKLAG 636
Cdd:COG1223 211 ALKKAILEDREKVT-----KEDLEEALKQRKERKKEPK 243
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
215-603 2.67e-33

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: 131.96  E-value: 2.67e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 215 AQRRQTEREKAEIERETIRVKAMAEAEGRARESKLSEDVNRRMLVDRANAEREKWVSAINTTFDHIGGGLRTILTDQNKL 294
Cdd:COG0464   2 AELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLAL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 295 IVAVGGLTALAAGIYTTREGAKVIWSYVDRILGQPSLIRESSRGKYPWSGSASRVLSTLRGGGKESTSKTGK-GFGDVIL 373
Cdd:COG0464  82 LAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREaILDDLGG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 374 RPALEKRIEQLANA-TANTKAHQA----PFRNILFYGPPGTGKTMAARELARRSGLDYALMTGGDVA--PLGaQAVTKIH 446
Cdd:COG0464 162 LEEVKEELRELVALpLKRPELREEyglpPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVskYVG-ETEKNLR 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 447 QLFDWSKKSKRGLLlFIDEADAFLCERNKTyMSEAQRSALNALLFRTGDQSKDIVLALATNRPGDLDSAVADRIDETLEF 526
Cdd:COG0464 241 EVFDKARGLAPCVL-FIDEADALAGKRGEV-GDGVGRRVVNTLLTEMEELRSDVVVIAATNRPDLLDPALLRRFDEIIFF 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 527 PLPGEEERFKLLNLYLEKYisktnlkkpgllqslfkkeqqtieikGVTEDL-LKEAAAKTKGFSGREIAKLM--ASVQAA 603
Cdd:COG0464 319 PLPDAEERLEIFRIHLRKR--------------------------PLDEDVdLEELAEATEGLSGADIRNVVrrAALQAL 372
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
377-526 2.03e-27

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: 108.52  E-value: 2.03e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 377 LEKRIEQLANATANTKAHQAPFRNILFYGPPGTGKTMAARELARRSGLDYALMTGGDVA-PLGAQAVTKIHQLFDWSKKS 455
Cdd:cd19481   5 LREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLsKYVGESEKNLRKIFERARRL 84
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22326858 456 KRGlLLFIDEADAFLCERNKTYMSEAQRSALNALLFRTGD--QSKDIVLALATNRPGDLDSAVAD--RIDETLEF 526
Cdd:cd19481  85 APC-ILFIDEIDAIGRKRDSSGESGELRRVLNQLLTELDGvnSRSKVLVIAATNRPDLLDPALLRpgRFDEVIEF 158
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
401-528 6.88e-27

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: 105.75  E-value: 6.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   401 ILFYGPPGTGKTMAARELARRSGLDYALMTGGDVAPLGA-QAVTKIHQLFDWSKKSKRGlLLFIDEADAFLCERNKTYMS 479
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVgESEKRLRELFEAAKKLAPC-VIFIDEIDALAGSRGSGGDS 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 22326858   480 EAQRsALNALLFR----TGDQSKDIVLAlATNRPGDLDSAVADRIDETLEFPL 528
Cdd:pfam00004  80 ESRR-VVNQLLTEldgfTSSNSKVIVIA-ATNRPDKLDPALLGRFDRIIEFPL 130
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
401-596 2.68e-24

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 104.32  E-value: 2.68e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 401 ILFYGPPGTGKTMAARELARRSGLDYALMTGGDVAP--LGAQAvTKIHQLFDWSKKSKRGlLLFIDEADAFLCERNKTYM 478
Cdd:COG1222 115 VLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSkyIGEGA-RNVREVFELAREKAPS-IIFIDEIDAIAARRTDDGT 192
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 479 S-EAQRSaLNALL-----FrtgDQSKDIVLALATNRPGDLDSAV--ADRIDETLEFPLPGEEERFKLLNLYLEKYIsktn 550
Cdd:COG1222 193 SgEVQRT-VNQLLaeldgF---ESRGDVLIIAATNRPDLLDPALlrPGRFDRVIEVPLPDEEAREEILKIHLRDMP---- 264
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 22326858 551 lkkpgllqslfkkeqqtieikgVTEDL-LKEAAAKTKGFSGREIAKL 596
Cdd:COG1222 265 ----------------------LADDVdLDKLAKLTEGFSGADLKAI 289
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
375-528 5.10e-16

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: 75.65  E-value: 5.10e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 375 PALEKRIEQLANAtantkAHQAPFRNILFYGPPGTGKTMAARELARRSG--------LDYALMTGGDVAPLGAQAVTKIH 446
Cdd:cd00009   1 VGQEEAIEALREA-----LELPPPKNLLLYGPPGTGKTTLARAIANELFrpgapflyLNASDLLEGLVVAELFGHFLVRL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 447 QLFDwsKKSKRGLLLFIDEADAFLCErnktyMSEAQRSALNALLFRTGDQSKDIVLAlATNRP--GDLDSAVADRIDETL 524
Cdd:cd00009  76 LFEL--AEKAKPGVLFIDEIDSLSRG-----AQNALLRVLETLNDLRIDRENVRVIG-ATNRPllGDLDRALYDRLDIRI 147

                ....
gi 22326858 525 EFPL 528
Cdd:cd00009 148 VIPL 151
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
396-526 4.22e-15

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: 73.48  E-value: 4.22e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 396 APFRNILFYGPPGTGKTMAARELARRSGLDYALMTGGDV--APLGaQAVTKIHQLFDWSKKSKRGlLLFIDEADAfLCER 473
Cdd:cd19503  32 KPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIvsKYLG-ESEKNLREIFEEARSHAPS-IIFIDEIDA-LAPK 108
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 22326858 474 NKTYMSEAQRSALNAL--LFRTGDQSKDIVLALATNRPGDLDSAV--ADRIDETLEF 526
Cdd:cd19503 109 REEDQREVERRVVAQLltLMDGMSSRGKVVVIAATNRPDAIDPALrrPGRFDREVEI 165
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
389-520 1.98e-14

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: 71.30  E-value: 1.98e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 389 ANTKAHQAPfRNILFYGPPGTGKTMAARELARRSG-----LDYALMTG---GDVAPLgAQAVTKIHQLFDWSkkskrglL 460
Cdd:cd19520  27 DNSRLLQPP-KGVLLYGPPGCGKTMLAKATAKEAGarfinLQVSSLTDkwyGESQKL-VAAVFSLASKLQPS-------I 97
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22326858 461 LFIDEADAFLCERNKT-YMSEAQRSALNALL---FRTGDQSKDIVLAlATNRPGDLDSAVADRI 520
Cdd:cd19520  98 IFIDEIDSFLRQRSSTdHEATAMMKAEFMSLwdgLSTDGNCRVIVMG-ATNRPQDLDEAILRRM 160
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
397-524 1.15e-13

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: 68.85  E-value: 1.15e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 397 PFRNILFYGPPGTGKTMAARELARRSGLDYALMTGGDV-APLGAQAVTKIHQLFDWSKKSKRGlLLFIDEADAFLCERNK 475
Cdd:cd19511  26 PPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELfSKYVGESERAVREIFQKARQAAPC-IIFFDEIDSLAPRRGQ 104
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 22326858 476 TYMSEAQRSALNALLFRTG--DQSKDIVLALATNRPGDLDSAV--ADRIDETL 524
Cdd:cd19511 105 SDSSGVTDRVVSQLLTELDgiESLKGVVVIAATNRPDMIDPALlrPGRLDKLI 157
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
396-526 4.95e-13

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: 67.36  E-value: 4.95e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 396 APFRNILFYGPPGTGKTMAARELARRSGLDYALMTGGDVAPL----GAQAVTKIHQLfdwsKKSKRGLLLFIDEADAFLC 471
Cdd:cd19502  35 EPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKyigeGARLVRELFEM----AREKAPSIIFIDEIDAIGA 110
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22326858 472 ER---NKTYMSEAQRSALNALLFRTG-DQSKDIVLALATNRPGDLDSAV--ADRIDETLEF 526
Cdd:cd19502 111 KRfdsGTGGDREVQRTMLELLNQLDGfDPRGNIKVIMATNRPDILDPALlrPGRFDRKIEF 171
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
399-516 1.01e-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: 66.49  E-value: 1.01e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 399 RNILFYGPPGTGKTMAARELARRSGLDYALMTGGDVAP----LGAQavtKIHQLFDWSKKSKRgLLLFIDEADAFLCERN 474
Cdd:cd19501  38 KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEmfvgVGAS---RVRDLFEQAKKNAP-CIVFIDEIDAVGRKRG 113
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 22326858 475 KTYM--SEAQRSALNALL-----FRTGDQSkdIVLAlATNRPGDLDSAV 516
Cdd:cd19501 114 AGLGggHDEREQTLNQLLvemdgFESNTGV--IVIA-ATNRPDVLDPAL 159
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
397-596 1.58e-12

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: 70.71  E-value: 1.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   397 PFRNILFYGPPGTGKTMAARELARRSGLDYALMTGGDV-APLGAQAVTKIHQLFDWSKKSKRGLLlFIDEADAFLCERNK 475
Cdd:TIGR01243 486 PPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEIlSKWVGESEKAIREIFRKARQAAPAII-FFDEIDAIAPARGA 564
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   476 TYMSEAQRSALNALLFRTG--DQSKDIVLALATNRPGDLDSAV--ADRIDETLEFPLPGEEERFKLLNLYLEKYisktnl 551
Cdd:TIGR01243 565 RFDTSVTDRIVNQLLTEMDgiQELSNVVVIAATNRPDILDPALlrPGRFDRLILVPPPDEEARKEIFKIHTRSM------ 638
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 22326858   552 kkpgllqslfkkeqqtieikGVTEDL-LKEAAAKTKGFSGREIAKL 596
Cdd:TIGR01243 639 --------------------PLAEDVdLEELAEMTEGYTGADIEAV 664
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
396-519 2.39e-12

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


Pssm-ID: 410917 [Multi-domain]  Cd Length: 163  Bit Score: 65.45  E-value: 2.39e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 396 APFRNILFYGPPGTGKTMAARELARRSGLDYALMTGGDVA--PLGAqAVTKIHQLFDWSKKSKRGlLLFIDEADAFLCER 473
Cdd:cd19509  30 GPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVskWVGE-SEKIVRALFALARELQPS-IIFIDEIDSLLSER 107
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 22326858 474 NKTyMSEAQRSALNALLFR----TGDQSKDIVLALATNRPGDLDSAVADR 519
Cdd:cd19509 108 GSG-EHEASRRVKTEFLVQmdgvLNKPEDRVLVLGATNRPWELDEAFLRR 156
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
397-551 8.58e-12

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 67.48  E-value: 8.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858  397 PFRNILFYGPPGTGKTMAARELARRSGLDYALMTGGD-VAPLGAQAVTKIHQLFDWSKKSKRGlLLFIDEADAFLCERNK 475
Cdd:PTZ00454 178 PPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEfVQKYLGEGPRMVRDVFRLARENAPS-IIFIDEVDSIATKRFD 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858  476 TYMS---EAQRSALNALLFRTG-DQSKDIVLALATNRPGDLDSAV--ADRIDETLEFPLPGEEERfkllNLYLEKYISKT 549
Cdd:PTZ00454 257 AQTGadrEVQRILLELLNQMDGfDQTTNVKVIMATNRADTLDPALlrPGRLDRKIEFPLPDRRQK----RLIFQTITSKM 332

                 ..
gi 22326858  550 NL 551
Cdd:PTZ00454 333 NL 334
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
397-516 7.10e-11

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: 61.30  E-value: 7.10e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 397 PFRNILFYGPPGTGKTMAARELARRSGLDYALMTGGDV-APLGAQAVTKIHQLFDWSKKSKRGlLLFIDEADAFLCERNK 475
Cdd:cd19519  33 PPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEImSKLAGESESNLRKAFEEAEKNAPA-IIFIDEIDAIAPKREK 111
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 22326858 476 TYmSEAQR---SALNALLFRTGDQSKDIVLAlATNRPGDLDSAV 516
Cdd:cd19519 112 TH-GEVERrivSQLLTLMDGLKQRAHVIVMA-ATNRPNSIDPAL 153
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
391-521 1.13e-10

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: 60.59  E-value: 1.13e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 391 TKAHQAPFRNILFYGPPGTGKTMAARELARRSGLDYALMTGGDVAPLGAQAVTK-IHQLFdwsKKSKRG--LLLFIDEAD 467
Cdd:cd19529  20 KRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKaIREIF---RKARQVapCVIFFDEID 96
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 22326858 468 AFLCERNKTYMSEAQRSALNALLFRTG--DQSKDIVLALATNRPGDLDSAV--ADRID 521
Cdd:cd19529  97 SIAPRRGTTGDSGVTERVVNQLLTELDglEEMNGVVVIAATNRPDIIDPALlrAGRFD 154
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
397-522 1.18e-10

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: 60.65  E-value: 1.18e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 397 PFRNILFYGPPGTGKTMAARELARRSGLDYALMTGGD-VAPLGAQAVTKIHQLFDWSKKSKRGlLLFIDEADAfLCERNK 475
Cdd:cd19521  39 PWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDlVSKWMGESEKLVKQLFAMARENKPS-IIFIDEVDS-LCGTRG 116
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 22326858 476 TYMSEAQRSALNALLFR---TGDQSKDIVLALATNRPGDLDSAVADRIDE 522
Cdd:cd19521 117 EGESEASRRIKTELLVQmngVGNDSQGVLVLGATNIPWQLDSAIRRRFEK 166
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
397-594 1.54e-10

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 63.31  E-value: 1.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858  397 PFRNILFYGPPGTGKTMAARELARRSGLDYALMTG--------GDvaplGAQAVtkiHQLFDWSKKsKRGLLLFIDEADA 468
Cdd:PRK03992 164 PPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGselvqkfiGE----GARLV---RELFELARE-KAPSIIFIDEIDA 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858  469 FLCERNKTYMS---EAQRSaLNALL-----FrtgDQSKDIVLALATNRPGDLDSAV--ADRIDETLEFPLPGEEERFKLL 538
Cdd:PRK03992 236 IAAKRTDSGTSgdrEVQRT-LMQLLaemdgF---DPRGNVKIIAATNRIDILDPAIlrPGRFDRIIEVPLPDEEGRLEIL 311
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 22326858  539 NLYLEkyisKTNLKkpgllqslfkkeqqtieikgvtEDL-LKEAAAKTKGFSGREIA 594
Cdd:PRK03992 312 KIHTR----KMNLA----------------------DDVdLEELAELTEGASGADLK 342
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
397-516 3.26e-10

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: 59.06  E-value: 3.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 397 PFRNILFYGPPGTGKTMAARELARRSGLDYALMTGGDVAPLG-AQAVTKIHQLFDWSKKSKRgLLLFIDEADAFLCERNK 475
Cdd:cd19528  26 PSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWfGESEANVRDIFDKARAAAP-CVLFFDELDSIAKARGG 104
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 22326858 476 TY--MSEAQRSALNALLFRTG--DQSKDIVLALATNRPGDLDSAV 516
Cdd:cd19528 105 NIgdAGGAADRVINQILTEMDgmNTKKNVFIIGATNRPDIIDPAI 149
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
115-260 3.48e-10

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 62.58  E-value: 3.48e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 115 KTREETRQAEFTAKAQEFKAMQSQAEAERQRViyEEQKKLAQHQAQTKSQMArYEDELARKRMQAENEAQRTRNQELVKM 194
Cdd:COG2268 218 QANREAEEAELEQEREIETARIAEAEAELAKK--KAEERREAETARAEAEAA-YEIAEANAEREVQRQLEIAEREREIEL 294
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 195 QEESAIRREVARRATEEEIQAQRRQTEREKAEIERETIRVKAMAEAEGRARES----KLSEDVNRRMLVD 260
Cdd:COG2268 295 QEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAeawnKLGDAAILLMLIE 364
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
392-522 3.54e-10

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: 59.23  E-value: 3.54e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 392 KAHQAPFRNILFYGPPGTGKTMAARELARRSGLDYALMTGGDVAP-LGAQAVTKIHQLFDWSKKSKRGlLLFIDEADAFL 470
Cdd:cd19522  27 KGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSkYRGESEKLVRLLFEMARFYAPT-TIFIDEIDSIC 105
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22326858 471 CERNKTYMSEAQRSALNALLFR--------TGDQSKDIVLAL-ATNRPGDLDSAVADRIDE 522
Cdd:cd19522 106 SRRGTSEEHEASRRVKSELLVQmdgvggasENDDPSKMVMVLaATNFPWDIDEALRRRLEK 166
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
395-520 8.74e-10

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: 57.94  E-value: 8.74e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 395 QAPFRNILFYGPPGTGKTMAARELARRSGLDYALMTGGDVAPLGAQAVTKIHQLFDWSKKSKRGLLLFIDEADAFLCERn 474
Cdd:cd19524  30 RAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLSER- 108
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 22326858 475 KTYMSEAQRSALNALLF-----RTGDQSKDIVLAlATNRPGDLDSAVADRI 520
Cdd:cd19524 109 SEGEHEASRRLKTEFLIefdgvQSNGDDRVLVMG-ATNRPQELDDAVLRRF 158
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
395-524 1.45e-09

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: 57.69  E-value: 1.45e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 395 QAPFRNILFYGPPGTGKTMAARELARRSGLDYALMTGGDVAPLGAQAVTKIHQLFDWSKKSKRGLLLFIDEADAFLCERN 474
Cdd:cd19525  52 RGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRG 131
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 22326858 475 KTYMSEAQRSALNALLFRTG--DQSKDIVLAL-ATNRPGDLDSAVADRIDETL 524
Cdd:cd19525 132 EGEHESSRRIKTEFLVQLDGatTSSEDRILVVgATNRPQEIDEAARRRLVKRL 184
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
397-544 1.71e-09

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 60.56  E-value: 1.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858  397 PFRNILFYGPPGTGKTMAARELARRSGLDYALMTG--------GDvaplGAQAVTKIHQLFDWSKKSkrglLLFIDEADA 468
Cdd:PTZ00361 216 PPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGseliqkylGD----GPKLVRELFRVAEENAPS----IVFIDEIDA 287
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858  469 FLCERNKTYMS---EAQRSALNALLFRTG-DQSKDIVLALATNRPGDLDSAV--ADRIDETLEFPLPGEEERFKLLNLYL 542
Cdd:PTZ00361 288 IGTKRYDATSGgekEIQRTMLELLNQLDGfDSRGDVKVIMATNRIESLDPALirPGRIDRKIEFPNPDEKTKRRIFEIHT 367

                 ..
gi 22326858  543 EK 544
Cdd:PTZ00361 368 SK 369
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
397-529 1.83e-09

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 56.61  E-value: 1.83e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858    397 PFRNILFYGPPGTGKTMAARELARRSG------------------LDYALMTGGDVAPLGAQAVTKIHQLFDWSKKSKRG 458
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGppgggviyidgedileevLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22326858    459 lLLFIDEADAFLceRNKTYMSEAQRSALNALLFRTGDQSKDIVlaLATNRPGDLDSA-VADRIDETLEFPLP 529
Cdd:smart00382  81 -VLILDEITSLL--DAEQEALLLLLEELRLLLLLKSEKNLTVI--LTTNDEKDLGPAlLRRRFDRRIVLLLI 147
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
397-521 3.27e-09

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: 56.26  E-value: 3.27e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 397 PFRNILFYGPPGTGKTMAARELARRSGLD-YALMTGGDVAPLGAQAVTKIHQLFDwSKKSKRGLLLFIDEADAFLCERnK 475
Cdd:cd19518  33 PPRGVLLHGPPGCGKTMLANAIAGELKVPfLKISATEIVSGVSGESEEKIRELFD-QAISNAPCIVFIDEIDAITPKR-E 110
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 22326858 476 TYMSEAQR-------SALNALLFRTGDQSKDIVLAlATNRPGDLDSAV--ADRID 521
Cdd:cd19518 111 SAQREMERrivsqllTCMDELNNEKTAGGPVLVIG-ATNRPDSLDPALrrAGRFD 164
PTZ00121 PTZ00121
MAEBL; Provisional
92-268 6.82e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.38  E-value: 6.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858    92 ERGAKALKGINNSAHAKKVFESIKTREETRQAEFTAKAQEFKAMQSQAEAERQRVIYEEQK--KLAQHQAQTKSQMARYE 169
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKaeELKKAEEKKKAEEAKKA 1572
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   170 DE---LARKRMQAENEAQRTRNQELVKM-QEESAIRREVARRATEEEIQA-QRRQTEREKAEIERETirvKAMAEAEGRA 244
Cdd:PTZ00121 1573 EEdknMALRKAEEAKKAEEARIEEVMKLyEEEKKMKAEEAKKAEEAKIKAeELKKAEEEKKKVEQLK---KKEAEEKKKA 1649
                         170       180
                  ....*....|....*....|....*
gi 22326858   245 RESKLSEDVNR-RMLVDRANAEREK 268
Cdd:PTZ00121 1650 EELKKAEEENKiKAAEEAKKAEEDK 1674
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
399-544 9.18e-09

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 58.51  E-value: 9.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858  399 RNILFYGPPGTGKTMAARELARRSGLDYALMTGGD-VAPLGAQAVTKIHQLFDWSKKSKRgLLLFIDEADAFLCERNKTY 477
Cdd:PRK10733 186 KGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDfVEMFVGVGASRVRDMFEQAKKAAP-CIIFIDEIDAVGRQRGAGL 264
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22326858  478 MS--EAQRSALNALLFRTG--DQSKDIVLALATNRPGDLDSAV--ADRIDETLEFPLPGEEERFKLLNLYLEK 544
Cdd:PRK10733 265 GGghDEREQTLNQMLVEMDgfEGNEGIIVIAATNRPDVLDPALlrPGRFDRQVVVGLPDVRGREQILKVHMRR 337
PTZ00121 PTZ00121
MAEBL; Provisional
89-267 1.77e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.84  E-value: 1.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858    89 EALERGAKALKGINNSAHAKKVFESIKTREETRQA-EFTAKAQEF-KAMQSQAEAERQRVIYEEQKKLAQ----HQAQTK 162
Cdd:PTZ00121 1399 KAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAdEAKKKAEEAkKADEAKKKAEEAKKAEEAKKKAEEakkaDEAKKK 1478
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   163 SQMARYEDELARKRMQAENEAQRTRNQELVKMQEESAIRREVARRATE-EEIQAQRRQTEREKAEIERETIRVKAMAEA- 240
Cdd:PTZ00121 1479 AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEaKKAEEAKKADEAKKAEEKKKADELKKAEELk 1558
                         170       180       190
                  ....*....|....*....|....*....|
gi 22326858   241 ---EGRARESKLSEDVNRRMLVDRANAERE 267
Cdd:PTZ00121 1559 kaeEKKKAEEAKKAEEDKNMALRKAEEAKK 1588
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
397-541 1.81e-08

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 57.61  E-value: 1.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   397 PFRNILFYGPPGTGKTMAARELARRSGLDYALMTGGDV-APLGAQAVTKIHQLFDWSKKSKRGlLLFIDEADAFLCERNK 475
Cdd:TIGR01243 211 PPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEImSKYYGESEERLREIFKEAEENAPS-IIFIDEIDAIAPKREE 289
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22326858   476 TYMSEAQRSALNALLFRTGDQSKDIVLAL-ATNRPGDLDSAV--ADRIDETLEFPLPGEEERFKLLNLY 541
Cdd:TIGR01243 290 VTGEVEKRVVAQLLTLMDGLKGRGRVIVIgATNRPDALDPALrrPGRFDREIVIRVPDKRARKEILKVH 358
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
105-268 2.04e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.64  E-value: 2.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 105 AHAKKVFESIKTREETRQAEFTAKAQEFKAMQSQAEAERqrviyeEQKKLAQHQAQTKSQMARYEDELARKRmQAENEAQ 184
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAEL------EELRLELEELELELEEAQAEEYELLAE-LARLEQD 303
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 185 RTRNQELVKMQEESAIRREVARRATEEEIQAQRRQTEREKAEIERETIRVKAMAEAEGRARESKLSEDVNRRMLVDRANA 264
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383

                ....
gi 22326858 265 EREK 268
Cdd:COG1196 384 LAEE 387
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
392-526 2.50e-08

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: 54.05  E-value: 2.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 392 KAHQAPFRNILFYGPPGTGKTMAARELA---RRSG--LDYALMTGGDV-APLGAQAVTKIHQLFDWSKKSkRGLLLFIDE 465
Cdd:cd19517  28 KFKITPPRGVLFHGPPGTGKTLMARALAaecSKGGqkVSFFMRKGADClSKWVGEAERQLRLLFEEAYRM-QPSIIFFDE 106
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22326858 466 ADAFLCERNkTYMSEAQRSALNALL-FRTG-DQSKDIVLALATNRPGDLDSAV--ADRIDETLEF 526
Cdd:cd19517 107 IDGLAPVRS-SKQEQIHASIVSTLLaLMDGlDNRGQVVVIGATNRPDALDPALrrPGRFDREFYF 170
PTZ00121 PTZ00121
MAEBL; Provisional
89-268 2.55e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.46  E-value: 2.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858    89 EALERGAKALKGINNSAHAKKVFESIKTREETRQAEFTAKAQEFKAMQSQAEAERQRViyEEQKKLAQhQAQTKSQMARY 168
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK--EEAKKKAD-AAKKKAEEKKK 1392
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   169 EDELARKRMQAENEAQRTRNQELVKMQEESAIRR-EVARRATEEEIQAQRRQTERE---KAEIERETIRVKAMAEAEGRA 244
Cdd:PTZ00121 1393 ADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKaEEKKKADEAKKKAEEAKKADEakkKAEEAKKAEEAKKKAEEAKKA 1472
                         170       180
                  ....*....|....*....|....
gi 22326858   245 RESKLSEDVNRRMLVDRANAEREK 268
Cdd:PTZ00121 1473 DEAKKKAEEAKKADEAKKKAEEAK 1496
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
372-524 4.45e-08

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: 52.88  E-value: 4.45e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 372 ILRPAleKRIEQLANATANTKAhqapfrNILFYGPPGTGKTMAARELARRSGLDYALMTGGDVAPLG-AQAVTKIHQLFD 450
Cdd:cd19530  12 ILRPI--KRPDIYKALGIDLPT------GVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYvGESERAVRQVFQ 83
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22326858 451 WSKKSKRgLLLFIDEADAfLCERNKTYMSEAQRSALNALLFRT--GDQSKDIVLALATNRPGDLDSAV--ADRIDETL 524
Cdd:cd19530  84 RARASAP-CVIFFDEVDA-LVPKRGDGGSWASERVVNQLLTEMdgLEERSNVFVIAATNRPDIIDPAMlrPGRLDKTL 159
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
128-268 5.81e-08

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 55.90  E-value: 5.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   128 KAQEFKAMQSQAEAERQRVIYEEQKKLAQHQAQTKSQMARYEDELARKRMQAENEAQRTRNQELVKmQEESAIRREVAR- 206
Cdd:pfam17380 387 RQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVR-LEEQERQQQVERl 465
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22326858   207 RATEEEIQAQRRQTEREKAEIERETIRVKAMAEAEGRARESKLSEDVNRRMLVDRANAEREK 268
Cdd:pfam17380 466 RQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQK 527
PTZ00121 PTZ00121
MAEBL; Provisional
105-268 7.66e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.92  E-value: 7.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   105 AHAKKVFESIKTREETRQAEFTAKAQEFKAMQSQAEAERQRViYEEQKKLAQHQAQTKSQ---------MARYEDELARK 175
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKK-AEEDKNMALRKAEEAKKaeearieevMKLYEEEKKMK 1608
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   176 RMQAEN-EAQRTRNQELVKMQEESAIRREVARRATEEEIQAQRRQTEREKAEIERETIRVKAmAEAEGRARESKLSEDVN 254
Cdd:PTZ00121 1609 AEEAKKaEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA-EEDKKKAEEAKKAEEDE 1687
                         170
                  ....*....|....
gi 22326858   255 RRMLVDRANAEREK 268
Cdd:PTZ00121 1688 KKAAEALKKEAEEA 1701
PTZ00121 PTZ00121
MAEBL; Provisional
55-277 9.32e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.53  E-value: 9.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858    55 SESGKEPSVAGEESDAPPRIRNNNPRTTSAGFDPEALERGAKALKGINNSAHAKKVFESIKTREETRQAEFTAKAQEFKA 134
Cdd:PTZ00121 1068 QDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARK 1147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   135 MQSQAEAERQRVIYEEQkklaqhqaqtKSQMARYEDElaRKRMQAENEAQRTRNQELVKMQEEsAIRREVARRATEEeiq 214
Cdd:PTZ00121 1148 AEDAKRVEIARKAEDAR----------KAEEARKAED--AKKAEAARKAEEVRKAEELRKAED-ARKAEAARKAEEE--- 1211
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22326858   215 aqRRQTEREKAEIERETIRVKAMAEAEGRARESKLSEDVnrrmlvdRANAEREKWVSAINTTF 277
Cdd:PTZ00121 1212 --RKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEE-------RNNEEIRKFEEARMAHF 1265
ftsH CHL00176
cell division protein; Validated
397-597 9.58e-08

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 55.06  E-value: 9.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858  397 PFRNILFYGPPGTGKTMAARELARRSGLDYALMTGGD-VAPLGAQAVTKIHQLFdwsKKSKRG--LLLFIDEADAFLCER 473
Cdd:CHL00176 215 IPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEfVEMFVGVGAARVRDLF---KKAKENspCIVFIDEIDAVGRQR 291
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858  474 NKTYM--SEAQRSALNALL-----FRtgdQSKDIVLALATNRPGDLDSAV--ADRIDETLEFPLPGEEERFKLLNLYLEK 544
Cdd:CHL00176 292 GAGIGggNDEREQTLNQLLtemdgFK---GNKGVIVIAATNRVDILDAALlrPGRFDRQITVSLPDREGRLDILKVHARN 368
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 22326858  545 yisktnlkkpgllqslfKKEQQTIeikgvtedLLKEAAAKTKGFSGREIAKLM 597
Cdd:CHL00176 369 -----------------KKLSPDV--------SLELIARRTPGFSGADLANLL 396
PTZ00121 PTZ00121
MAEBL; Provisional
112-268 1.17e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.15  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   112 ESIKTREETRQAEFTAKAQEFKAMQS-QAEAERQRVIYEEQKKLAQHQAQTKSQMARYEDELARK--RMQAENEAQRTRN 188
Cdd:PTZ00121 1584 EEAKKAEEARIEEVMKLYEEEKKMKAeEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKaeELKKAEEENKIKA 1663
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   189 QELVKMQEESAIRREVARRATEEEIQAQRRQTEREKAEIERETIRvKAMAEAEGRARESKLSEDVNrRMLVDRANAEREK 268
Cdd:PTZ00121 1664 AEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELK-KKEAEEKKKAEELKKAEEEN-KIKAEEAKKEAEE 1741
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
114-252 2.32e-07

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: 53.80  E-value: 2.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   114 IKTREETRQAEFTAKAQefKAMQSQAEAERQRVIYEEQKKLAQHQAQTKSQMaRYEDELARKRMQAENEAQRTRNQELVK 193
Cdd:pfam15709 325 LEKREQEKASRDRLRAE--RAEMRRLEVERKRREQEEQRRLQQEQLERAEKM-REELELEQQRRFEEIRLRKQRLEEERQ 401
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22326858   194 MQEESAIR--------REVARRATEE------EIQAQRRQTEREKAEIERETIRVKAMAEAEGRARESKLSED 252
Cdd:pfam15709 402 RQEEEERKqrlqlqaaQERARQQQEEfrrklqELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEE 474
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
89-268 2.38e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 2.38e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858  89 EALERGAKALKGINNSAHAKKVFESIKTREETRQAEFTAKAQEFKAMQSQAEAERQRVIyEEQKKLAQHQAQTKSQMARY 168
Cdd:COG1196 285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE-EELEEAEEELEEAEAELAEA 363
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 169 EDELARKRmQAENEAQRTRNQELVKMQEESAIRREVARRATEEEIQAQRRQTEREKAEIERETIRVKAMAEAEGRARESK 248
Cdd:COG1196 364 EEALLEAE-AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
                       170       180
                ....*....|....*....|
gi 22326858 249 LSEDVNRRMLVDRANAEREK 268
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALL 462
PTZ00121 PTZ00121
MAEBL; Provisional
89-268 4.58e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.22  E-value: 4.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858    89 EALERGAKALKGINNSAHAKKVFESIKTREETRQAE-FTAKAQEF-KAMQSQAEAERQRVIYEEQKKLAqhQAQTKSQMA 166
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADaAKKKAEEKkKADEAKKKAEEDKKKADELKKAA--AAKKKADEA 1423
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   167 RYEDELARKRMQAENEAQRTRNQELVKMQEESAIRREVARRATEEeiqAQRRQTEREKAEIERETIRVKAMA-EAEGRAR 245
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEE---AKKADEAKKKAEEAKKADEAKKKAeEAKKKAD 1500
                         170       180
                  ....*....|....*....|...
gi 22326858   246 ESKLSEDVNRRMLVDRANAEREK 268
Cdd:PTZ00121 1501 EAKKAAEAKKKADEAKKAEEAKK 1523
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
107-294 5.80e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 5.80e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 107 AKKvFESIKTREETRQAEFTAKAQEFKAMQSQAEAERQRVIYEEQKKLAQHQAQTKSQMARYEDELARKRMQAENEAQRT 186
Cdd:COG1196 212 AER-YRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 187 RNQELVKMQEESAIRREVARR----ATEEEIQAQRRQTEREKAEIERETIRVKAMAEAEGRARESKLSEDVNRRMLVDRA 262
Cdd:COG1196 291 YELLAELARLEQDIARLEERRreleERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
                       170       180       190
                ....*....|....*....|....*....|..
gi 22326858 263 NAEREKWVSAINTTFDHIGGGLRTILTDQNKL 294
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQL 402
PTZ00121 PTZ00121
MAEBL; Provisional
89-261 6.06e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.84  E-value: 6.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858    89 EALERGAKALKGINNSAHAKKVFESIKTREET---RQAEFTAKAQEFKAMQSQAEAErqrviyEEQKKLAQHQAQTKSQM 165
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEnkiKAAEEAKKAEEDKKKAEEAKKA------EEDEKKAAEALKKEAEE 1700
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   166 ARYEDELARKRmqaenEAQRTRNQELVKMQEESAIRREVARRATEEEIQA--QRRQTEREKAEIERETIRVKAMAEAEGR 243
Cdd:PTZ00121 1701 AKKAEELKKKE-----AEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKaeEAKKDEEEKKKIAHLKKEEEKKAEEIRK 1775
                         170       180
                  ....*....|....*....|...
gi 22326858   244 ARESKLSE-----DVNRRMLVDR 261
Cdd:PTZ00121 1776 EKEAVIEEeldeeDEKRRMEVDK 1798
PTZ00121 PTZ00121
MAEBL; Provisional
66-268 7.01e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.84  E-value: 7.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858    66 EESDAPPRIRNNNPRTTSAGFDPEALERGAKALKginnsAHAKKVFESIKTREETRQAEFTAKAQEF-KAMQSQAEAERQ 144
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIRKFEEARMAHFARRQAAIK-----AEEARKADELKKAEEKKKADEAKKAEEKkKADEAKKKAEEA 1314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   145 RVIYEEQKKLAQHQ-----AQTKSQMARYEDELARKRMQA---ENEAQRTRNQELVKMQEESAIRREVARRATEEEIQAQ 216
Cdd:PTZ00121 1315 KKADEAKKKAEEAKkkadaAKKKAEEAKKAAEAAKAEAEAaadEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAD 1394
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 22326858   217 RRQTEREkaEIERETIRVKAMAEAEGRARESKLSEDVNRRMLVDRANAEREK 268
Cdd:PTZ00121 1395 EAKKKAE--EDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAK 1444
PTZ00121 PTZ00121
MAEBL; Provisional
89-267 8.74e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.45  E-value: 8.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858    89 EALERGAKALKGINNSAHAKKVFESIKTREETRQAEFTAKAQEFKAMQSQAEAERQRVIYEEQKKLAQHQAQTKSQMARY 168
Cdd:PTZ00121 1353 EAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK 1432
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   169 EDEL------ARKRMQAENEAQRTRNQELVKMQEESAIRREVARRATEEEIQAQRRQTEREKAEIERETIRVKamAEAEG 242
Cdd:PTZ00121 1433 ADEAkkkaeeAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA--AEAKK 1510
                         170       180
                  ....*....|....*....|....*
gi 22326858   243 RARESKLSEDVNRRMLVDRANAERE 267
Cdd:PTZ00121 1511 KADEAKKAEEAKKADEAKKAEEAKK 1535
PTZ00121 PTZ00121
MAEBL; Provisional
59-267 1.43e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.68  E-value: 1.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858    59 KEPSVAGEESDAPPRIRNNNPRTTSAGFDPEALERGA----KALKGINNSAHAKKVFESIKTREETRQA--EFTAKAQEF 132
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAeekkKADEAKKKAEEDKKKADELKKAAAAKKKadEAKKKAEEK 1430
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   133 -KAMQSQAEAERQRVIYEEQKKLAQHQaqtKSQMARYEDELARKRMQAENEAQRTRN-QELVKMQEESAIRREVARRATE 210
Cdd:PTZ00121 1431 kKADEAKKKAEEAKKADEAKKKAEEAK---KAEEAKKKAEEAKKADEAKKKAEEAKKaDEAKKKAEEAKKKADEAKKAAE 1507
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 22326858   211 EEIQAQ--RRQTEREKAEIERETIRVKAMAEAEgRARESKLSEDVNRRMLVDRANAERE 267
Cdd:PTZ00121 1508 AKKKADeaKKAEEAKKADEAKKAEEAKKADEAK-KAEEKKKADELKKAEELKKAEEKKK 1565
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
105-268 1.94e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 1.94e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 105 AHAKKVFESIKTREETRQAEFTAKAQEFKAMQSQAEAERQRVIY---------EEQKKLAQHQAQTKSQMARYEDELARK 175
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREleerleeleEELAELEEELEELEEELEELEEELEEA 349
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 176 RMQAEN-EAQRTRNQELVKMQEESAIRREVARRATEEEIQAQRRQTEREKAEIERETIRVKAMAEAEGRARESKLSEDVN 254
Cdd:COG1196 350 EEELEEaEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
                       170
                ....*....|....
gi 22326858 255 RRMLVDRANAEREK 268
Cdd:COG1196 430 LAELEEEEEEEEEA 443
PTZ00491 PTZ00491
major vault protein; Provisional
151-241 2.22e-06

major vault protein; Provisional


Pssm-ID: 240439 [Multi-domain]  Cd Length: 850  Bit Score: 50.79  E-value: 2.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858  151 QKKLAQHQAQTKSQMARyeDELARKRM--QAENEAQRTrnqELVKMQEES-AIRREVARRAtEEEIQAQRRQTEREkAEI 227
Cdd:PTZ00491 664 QEAAARHQAELLEQEAR--GRLERQKMhdKAKAEEQRT---KLLELQAESaAVESSGQSRA-EALAEAEARLIEAE-AEV 736
                         90
                 ....*....|....*..
gi 22326858  228 ERETIRVKA---MAEAE 241
Cdd:PTZ00491 737 EQAELRAKAlriEAEAE 753
PTZ00121 PTZ00121
MAEBL; Provisional
92-268 2.27e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 2.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858    92 ERGAKALKGINNSAHAKKVFESIKTREETRQA-EFTAKAQEF--KAMQSQAEAERQRVIYEEQKKLAQHQAQT--KSQMA 166
Cdd:PTZ00121 1454 EEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAdEAKKKAEEAkkKADEAKKAAEAKKKADEAKKAEEAKKADEakKAEEA 1533
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   167 RYEDELarKRMQAENEAQRTRNQELVKMQEESAiRREVARRATEEEIQAQRRQTEREKAEIER---------ETIRVKA- 236
Cdd:PTZ00121 1534 KKADEA--KKAEEKKKADELKKAEELKKAEEKK-KAEEAKKAEEDKNMALRKAEEAKKAEEARieevmklyeEEKKMKAe 1610
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 22326858   237 ----MAEAEGRARESKLSEDVNRRMLVDRANAEREK 268
Cdd:PTZ00121 1611 eakkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEK 1646
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
105-268 2.89e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 2.89e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 105 AHAKKVFESIKTREETRQAEFTAKAQEFKAMQSQAEAERQRVIYEEQKKLAQHQAQtksqmaryeDELARKRMQAENEAQ 184
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL---------EELAEELLEALRAAA 396
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 185 RTRNQELVKMQEESAIRREVARRATEEEiqaqRRQTEREKAEIERETIRVKAMAEAEGRARESKLSEDVNRRMLVDRANA 264
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELE----ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472

                ....
gi 22326858 265 EREK 268
Cdd:COG1196 473 ALLE 476
PTZ00121 PTZ00121
MAEBL; Provisional
105-268 2.93e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 2.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   105 AHAKKVFESIKTREE-----TRQAEFTAKAQEFKAMQSQAEAERQRVIYEEQKKLAQhQAQTKSQMARYEDELARKRMQ- 178
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEdknmaLRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE-EAKIKAEELKKAEEEKKKVEQl 1638
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   179 -AENEAQRTRNQELVKMQEESAIRREVARRATEEEiqaQRRQTEREKAEIEREtirvKAMAEAEGRARESKLSEDVNRRM 257
Cdd:PTZ00121 1639 kKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED---KKKAEEAKKAEEDEK----KAAEALKKEAEEAKKAEELKKKE 1711
                         170
                  ....*....|.
gi 22326858   258 LVDRANAEREK 268
Cdd:PTZ00121 1712 AEEKKKAEELK 1722
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
401-516 3.08e-06

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


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 47.51  E-value: 3.08e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 401 ILFYGPPGTGKTMAARELARRSGLDYALMTGGDVAPLG-AQAVTKIHQLFDwSKKSKRGLLLFIDEADAFLCERNKTYMS 479
Cdd:cd19527  29 ILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYiGESEANVREVFQ-KARDAKPCVIFFDELDSLAPSRGNSGDS 107
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 22326858 480 ----EAQRSALNALLFRTGDQSKDIVLALATNRPGDLDSAV 516
Cdd:cd19527 108 ggvmDRVVSQLLAELDGMSSSGQDVFVIGATNRPDLLDPAL 148
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
108-245 4.71e-06

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 49.49  E-value: 4.71e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 108 KKVFESIKTRE-ETRQAEFTAKAQEFKAMQSQAEAERQRVIYEEQKKLAQHQAQTKSQMARYEDELARKRMQAENEA--Q 184
Cdd:COG2268 192 RKIAEIIRDARiAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYeiA 271
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22326858 185 RTRNQELVKMQEESAIRR---EVARRATEEEIQAQRRqTEREKAEIEREtirvKAMAEAEGRAR 245
Cdd:COG2268 272 EANAEREVQRQLEIAEREreiELQEKEAEREEAELEA-DVRKPAEAEKQ----AAEAEAEAEAE 330
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
108-268 8.37e-06

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 48.97  E-value: 8.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   108 KKVFESIKTREETRQAEFTAKAQEFKAMQSQAEAERQRVIYEEQKKlaQHQAQtksqmaryedelarkRMQAENEAQRTR 187
Cdd:pfam17380 413 RKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQER--QQQVE---------------RLRQQEEERKRK 475
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   188 NQELVKMQEESAIRREVARRATEEEIQaqrrqtEREKAEIEREtiRVKAMAEAEGRARESKLSEDVNRRmlvdRANAERE 267
Cdd:pfam17380 476 KLELEKEKRDRKRAEEQRRKILEKELE------ERKQAMIEEE--RKRKLLEKEMEERQKAIYEEERRR----EAEEERR 543

                  .
gi 22326858   268 K 268
Cdd:pfam17380 544 K 544
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
112-267 8.94e-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: 8.94e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 112 ESIKTREETRQAEF-TAKAQEFKAMQSQAEAERQRviyEEQKKLAQHQAQTKSQMARYEDELARKRMQAENEAQRTRNQE 190
Cdd:COG1196 326 AELEEELEELEEELeELEEELEEAEEELEEAEAEL---AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22326858 191 LVKMQEESAIRREVARRATEEEIQAQRRQTEREKAEIERETIRVKAMAEAEGRARESKLSEDVNRRMLVDRANAERE 267
Cdd:COG1196 403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
PTZ00121 PTZ00121
MAEBL; Provisional
89-268 9.38e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 9.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858    89 EALERGAKALKGINNSAHAKKV--FESIKTREETRQAEFTA-----------KAQEFKAMQSQAEAERQRViYEEQKKLa 155
Cdd:PTZ00121 1227 EAVKKAEEAKKDAEEAKKAEEErnNEEIRKFEEARMAHFARrqaaikaeearKADELKKAEEKKKADEAKK-AEEKKKA- 1304
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   156 qHQAQTKSQMARYEDELARKRMQAENEAqrtrnQELVKMQEESAIRREVARRATEEEIQAQRRQTEREKAEIERETIRVK 235
Cdd:PTZ00121 1305 -DEAKKKAEEAKKADEAKKKAEEAKKKA-----DAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKK 1378
                         170       180       190
                  ....*....|....*....|....*....|...
gi 22326858   236 AMAEAEGRARESKLSEDVNRRMLVDRANAEREK 268
Cdd:PTZ00121 1379 KADAAKKKAEEKKKADEAKKKAEEDKKKADELK 1411
PTZ00121 PTZ00121
MAEBL; Provisional
105-252 1.21e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   105 AHAKKVFESIKTREETRQAEFTAKAQEFKAMQS---QAE----AERQRVIYEEQK-------KLAQHQAQTKSQMARYED 170
Cdd:PTZ00121 1202 AEAARKAEEERKAEEARKAEDAKKAEAVKKAEEakkDAEeakkAEEERNNEEIRKfeearmaHFARRQAAIKAEEARKAD 1281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   171 ELarKRMQAENEAQRTRNQELVKMQEESAIRREVARRATEEEIQAQRRQTEREKAEIERETIRVK---AMAEAEGRARES 247
Cdd:PTZ00121 1282 EL--KKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAaeaAKAEAEAAADEA 1359

                  ....*
gi 22326858   248 KLSED 252
Cdd:PTZ00121 1360 EAAEE 1364
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
108-246 1.27e-05

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: 48.41  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   108 KKVFESIKTREETRQAEFTAKAQE--FKAMQSQAEAERQRVIYEEQKKLAQhQAQTKSQMARYEDELARKRMQAENEAQR 185
Cdd:pfam15709 383 QRRFEEIRLRKQRLEEERQRQEEEerKQRLQLQAAQERARQQQEEFRRKLQ-ELQRKKQQEEAERAEAEKQRQKELEMQL 461
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22326858   186 TRNQE-LVKMQEESaiRREVARRATEEEIQAQ-----RRQTEREKAEIEREtirvKAMAEAEGRARE 246
Cdd:pfam15709 462 AEEQKrLMEMAEEE--RLEYQRQKQEAEEKARleaeeRRQKEEEAARLALE----EAMKQAQEQARQ 522
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
112-280 1.44e-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: 48.20  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   112 ESIKTREETRQAEFTAKAQEFKAMQSQAEAERQRVIYEEQKKLAQHQAQTKSQMAryeDELARKRMQAENEAQR------ 185
Cdd:pfam17380 435 REVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRA---EEQRRKILEKELEERKqamiee 511
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   186 TRNQELV--KMQE-ESAIRREVARRATEEEiqaQRRQTEREkaeiERETIRVKAMAEAEGRAR-ESKLSEDVNRRMLVDR 261
Cdd:pfam17380 512 ERKRKLLekEMEErQKAIYEEERRREAEEE---RRKQQEME----ERRRIQEQMRKATEERSRlEAMEREREMMRQIVES 584
                         170
                  ....*....|....*....
gi 22326858   262 ANAEREKWVSAINTTFDHI 280
Cdd:pfam17380 585 EKARAEYEATTPITTIKPI 603
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
396-516 1.78e-05

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


Pssm-ID: 410931 [Multi-domain]  Cd Length: 163  Bit Score: 45.26  E-value: 1.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 396 APFRNILFYGPPGTGKTMAARELARRSGLDYALMTGGDVAPLGAQAVTKIHQLFDWSKKSKRGLLLFIDEADAFLCER-- 473
Cdd:cd19523  31 RLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEKILQASFLAARCRQPSVLFISDLDALLSSQdd 110
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 22326858 474 NKTYMSEAQRSALNALLFRTGDQSKDIVLALATNRPGDLDSAV 516
Cdd:cd19523 111 EASPVGRLQVELLAQLDGVLGSGEDGVLVVCTTSKPEEIDESL 153
PTZ00121 PTZ00121
MAEBL; Provisional
112-268 2.41e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 2.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   112 ESIKTREETRQAEFTAKAQEFKAMQSQAEAERQRVIYEEQKKLAQHQAQTK---SQMARYED----------ELARKRMQ 178
Cdd:PTZ00121 1161 EDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEErkaEEARKAEDakkaeavkkaEEAKKDAE 1240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   179 AENEAQRTRNQELVKMQEESAI----RREVARRAtEEEIQAQ--RRQTEREKAEIERETIRVKAMAEAEGRARESKLSED 252
Cdd:PTZ00121 1241 EAKKAEEERNNEEIRKFEEARMahfaRRQAAIKA-EEARKADelKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADE 1319
                         170
                  ....*....|....*.
gi 22326858   253 VNRRMLVDRANAEREK 268
Cdd:PTZ00121 1320 AKKKAEEAKKKADAAK 1335
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
392-470 2.45e-05

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 47.00  E-value: 2.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858  392 KAHQAPfrNILFYGPPGTGKTMAARELARRSGLDY----ALMTGgdvaplgaqaVTKIHQLFD---WSKKSKRGLLLFID 464
Cdd:PRK13342  32 EAGRLS--SMILWGPPGTGKTTLARIIAGATDAPFealsAVTSG----------VKDLREVIEearQRRSAGRRTILFID 99
                         90
                 ....*....|....
gi 22326858  465 E--------ADAFL 470
Cdd:PRK13342 100 EihrfnkaqQDALL 113
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
112-268 3.14e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 3.14e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 112 ESIKTREETRQAEFTAKAQEFKAMQSQAEAERQRVIYEEQKKlaQHQAQTKSQMARYEDELARKRMQAENEAQRTRNQEL 191
Cdd:COG1196 263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI--ARLEERRRELEERLEELEEELAELEEELEELEEELE 340
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22326858 192 VKMQEESAIRREVARRATEEEIQAQRRQ-TEREKAEIERETIRVKAMAEAEGRARESKLSEDVNRRMLVDRANAEREK 268
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEAEEALLeAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
101-197 3.40e-05

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: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 44.10  E-value: 3.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   101 INNSAHAKKVFESIKTREETRQAEFTAKAQEFKAMqsQAEAERQRVIYEEQKKLAQHQAQTKSQmaryedELARKRMQAE 180
Cdd:pfam03938  11 LEESPEGKAAQAQLEKKFKKRQAELEAKQKELQKL--YEELQKDGALLEEEREEKEQELQKKEQ------ELQQLQQKAQ 82
                          90
                  ....*....|....*..
gi 22326858   181 NEAQRTRNQELVKMQEE 197
Cdd:pfam03938  83 QELQKKQQELLQPIQDK 99
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
395-525 6.37e-05

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: 43.57  E-value: 6.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 395 QAPFR---NILFYGPPGTGKTMAARELARRSGLDYALMTGGDVAP--LGA--QAVtkiHQLFDwSKKSKRGLLLFIDEAD 467
Cdd:cd19526  21 SSPLRlrsGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNkyIGAseQNV---RDLFS-RAQSAKPCILFFDEFD 96
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22326858 468 AFLCERNKTYMSEAQRsALNALLFRT-GDQSKDIVLALA-TNRPGDLDSAV--ADRIDETLE 525
Cdd:cd19526  97 SIAPKRGHDSTGVTDR-VVNQLLTQLdGVEGLDGVYVLAaTSRPDLIDPALlrPGRLDKLVY 157
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
101-197 6.43e-05

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: 43.34  E-value: 6.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858    101 INNSAHAKKVFESIKTREETRQAEFTAKAQEFKAMQSQAEAERQRVIYEEQKKLAQhqaqtksQMARYEDELARKRMQAE 180
Cdd:smart00935  10 LQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEAAREKKEK-------ELQKKVQEFQRKQQKLQ 82
                           90
                   ....*....|....*..
gi 22326858    181 NEAQRTRNQELVKMQEE 197
Cdd:smart00935  83 QDLQKRQQEELQKILDK 99
PRK07353 PRK07353
F0F1 ATP synthase subunit B'; Validated
149-240 6.61e-05

F0F1 ATP synthase subunit B'; Validated


Pssm-ID: 235999 [Multi-domain]  Cd Length: 140  Bit Score: 43.07  E-value: 6.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858  149 EEQKKLAQHQAQTksqmARYEDELARKRMQ-------AENEAQRTRNQELVKMQEESAIRREVARRATEEEIQAQRRQTE 221
Cdd:PRK07353  47 EAKERLAEAEKLE----AQYEQQLASARKQaqaviaeAEAEADKLAAEALAEAQAEAQASKEKARREIEQQKQAALAQLE 122
                         90
                 ....*....|....*....
gi 22326858  222 REKAEIEReTIRVKAMAEA 240
Cdd:PRK07353 123 QQVDALSR-QILEKLLAAK 140
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
381-420 1.18e-04

DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];


Pssm-ID: 442061 [Multi-domain]  Cd Length: 340  Bit Score: 44.80  E-value: 1.18e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 22326858 381 IEQLANATANTKAHQApfrnILFYGPPGTGKTMAARELAR 420
Cdd:COG2812  19 VRTLKNALASGRLAHA----YLFTGPRGVGKTTLARILAK 54
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
118-266 1.23e-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: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   118 EETRQAEFTAKAQEFKAMQsqaEAERQRVIYEEQKKLAQHQAQTKSQMARYEDELARKRMQAENEAQRTRNQELVKMQEE 197
Cdd:TIGR02794  87 EQARQKELEQRAAAEKAAK---QAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAE 163
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22326858   198 SAIRREVARRATEEEIQAQ---RRQTEREKAEIERETIRVKAMAEAEGRARESKlsedvnrrMLVDRANAER 266
Cdd:TIGR02794 164 AKKKAEEAKKKAEAEAKAKaeaEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEA--------AAAAAAEAER 227
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
128-267 1.35e-04

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 44.86  E-value: 1.35e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 128 KAQEFKAMQSQAEAERQRviyEEQKKLAQHQAQTKSQMARYEDELARKRmQAENEAqrtrnqELVKMQEESAIRREVARR 207
Cdd:COG2268 193 KIAEIIRDARIAEAEAER---ETEIAIAQANREAEEAELEQEREIETAR-IAEAEA------ELAKKKAEERREAETARA 262
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22326858 208 ATEE--EIQAQRRQTEREKAEIERETIRVKAMAEAEGRARESKLSEDVNRRMLVDRANAERE 267
Cdd:COG2268 263 EAEAayEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAE 324
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
400-470 1.47e-04

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 44.66  E-value: 1.47e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 400 NILFYGPPGTGKTMAARELARRSGLDY----ALMTGgdVAPLgAQAVTKIHQLfdwsKKSKRGLLLFIDE--------AD 467
Cdd:COG2256  51 SMILWGPPGTGKTTLARLIANATDAEFvalsAVTSG--VKDI-REVIEEARER----RAYGRRTILFVDEihrfnkaqQD 123

                ...
gi 22326858 468 AFL 470
Cdd:COG2256 124 ALL 126
44 PHA02544
clamp loader, small subunit; Provisional
400-537 1.84e-04

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 43.83  E-value: 1.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858  400 NILFYGP-PGTGKTMAARELARRSGLDYALMTGGD--------VAPLGAQAVTkihqlfdwskKSKRGLLLFIDEADafl 470
Cdd:PHA02544  44 NMLLHSPsPGTGKTTVAKALCNEVGAEVLFVNGSDcridfvrnRLTRFASTVS----------LTGGGKVIIIDEFD--- 110
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858  471 cernKTYMSEAQ---RSALNALlfrtgdqSKDIVLALATNRPGDLDSAVADRIDEtLEFPLPGEEERFKL 537
Cdd:PHA02544 111 ----RLGLADAQrhlRSFMEAY-------SKNCSFIITANNKNGIIEPLRSRCRV-IDFGVPTKEEQIEM 168
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
197-420 2.11e-04

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 44.38  E-value: 2.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 197 ESAIRREVARRATEEEIQAQRRQTEREKAEIERETIRVKAMAEAEGRARESKLSEDVNRRMLVDRANAEREKWVSAINTT 276
Cdd:COG1401  19 PLESEDAVRELGIRADDLRGAAELATRLAERLSEELLRADRAARATELVEELSAALEVVVLLLDLEKVELNEKLALSEAA 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 277 FDHIGGGLRTILTDQNKLIVAVGGLTALAAGIYTTREGAKV--IWSYVDRILGQPSLIRESSRGKYPWSGSASRVLSTLR 354
Cdd:COG1401  99 VAIEELYELEADSEIEAVGLLLELAERSDALEALERARLLLelADLEERAALETEVLEALEAELEELLAAPEDLSADALA 178
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22326858 355 GGGKESTSKTGKGFGDVILRPALEKRIEQLANATANTKAHQAPfRNILFYGPPGTGKTMAARELAR 420
Cdd:COG1401 179 AELSAAEELYSEDLESEDDYLKDLLREKFEETLEAFLAALKTK-KNVILAGPPGTGKTYLARRLAE 243
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
399-516 2.78e-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: 42.09  E-value: 2.78e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 399 RNILFYGPPGTGKTMAARELARR-SGLDYALMTGGDV-APLGAQAVTKIHQLFDWSKKSKR------GLLLFI-DEADAF 469
Cdd:cd19504  36 KGILLYGPPGTGKTLMARQIGKMlNAREPKIVNGPEIlNKYVGESEANIRKLFADAEEEQRrlgansGLHIIIfDEIDAI 115
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 22326858 470 LCERNKTYMSEA-QRSALNALLFRTG--DQSKDIVLALATNRPGDLDSAV 516
Cdd:cd19504 116 CKQRGSMAGSTGvHDTVVNQLLSKIDgvEQLNNILVIGMTNRKDLIDEAL 165
PTZ00121 PTZ00121
MAEBL; Provisional
105-268 2.89e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 2.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   105 AHAKKVFESIKTREETR--QAEFTAKAQE--FKAMQSQAEAERQRVIYEEQKKLAQHQAQTKSQMARYEDELARKRMQAE 180
Cdd:PTZ00121 1589 AEEARIEEVMKLYEEEKkmKAEEAKKAEEakIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK 1668
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   181 NEAQRTRNQELVKMQEESAIRREVARRATEEEIQAQRRQTEREKAEIERETIRVKAMAEAEGRARESKLSEDVNRRMLVD 260
Cdd:PTZ00121 1669 KAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748

                  ....*...
gi 22326858   261 RANAEREK 268
Cdd:PTZ00121 1749 AKKDEEEK 1756
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
122-244 3.57e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 43.26  E-value: 3.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858  122 QAEFTAKAQEFKAMQSQAeAERQRVIYEEQKKLAQHQAQTKSQMARYEDELARKrmQAENEAQRTRNQELVKMQEESAIR 201
Cdd:PRK09510  80 QRKKKEQQQAEELQQKQA-AEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQK--QAEEAAAKAAAAAKAKAEAEAKRA 156
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 22326858  202 REVARRATEE-----EIQAQRRQTEREKAEIERETiRVKAMAEAEGRA 244
Cdd:PRK09510 157 AAAAKKAAAEakkkaEAEAAKKAAAEAKKKAEAEA-AAKAAAEAKKKA 203
PRK11578 PRK11578
macrolide transporter subunit MacA; Provisional
123-189 3.68e-04

macrolide transporter subunit MacA; Provisional


Pssm-ID: 183211 [Multi-domain]  Cd Length: 370  Bit Score: 43.22  E-value: 3.68e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858  123 AEFTAKAQEFKAMQSQAEAERQ--RVIYEEQKKLAQHQAQTKSQMARYEDELARKRMQAEN-EAQRTRNQ 189
Cdd:PRK11578 102 KEVEATLMELRAQRQQAEAELKlaRVTLSRQQRLAKTQAVSQQDLDTAATELAVKQAQIGTiDAQIKRNQ 171
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
114-268 5.49e-04

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.60  E-value: 5.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   114 IKTREETRQAEFTAKAQEFKAMQSQAEAERQRVIYEEQKKLAQhQAQTKSQMARYEDELARKR--MQAENEAQRTRNQEL 191
Cdd:pfam13868  82 IEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEK-QRQLREEIDEFNEEQAEWKelEKEEEREEDERILEY 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   192 VKMQEESAIRREVARRAT----EEEIQAQRRQTEREKAEI-ERETIRVK-AMAEAEGRARESKLSEDVNRRMLVDRANAE 265
Cdd:pfam13868 161 LKEKAEREEEREAEREEIeeekEREIARLRAQQEKAQDEKaERDELRAKlYQEEQERKERQKEREEAEKKARQRQELQQA 240

                  ...
gi 22326858   266 REK 268
Cdd:pfam13868 241 REE 243
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
400-421 5.90e-04

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


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 42.72  E-value: 5.90e-04
                        10        20
                ....*....|....*....|..
gi 22326858 400 NILFYGPPGTGKTMaareLARR 421
Cdd:COG0606 213 NLLMIGPPGSGKTM----LARR 230
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
89-308 1.05e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 1.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858  89 EALERGAKALKGInnSAHAKKVFESIKTREETRQAEFTAKAQEFKAMQSQAEAERQRVIYEEQKKLAQHQAQTKSQMARY 168
Cdd:COG4717  71 KELKELEEELKEA--EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERL 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 169 ED---------ELARKRMQAENEAQRTRNQELVKMQEESAIRREVARRATE--EEIQAQRRQTEREKAEIEREtirVKAM 237
Cdd:COG4717 149 EEleerleelrELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEelEELQQRLAELEEELEEAQEE---LEEL 225
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22326858 238 AEAEGRARESKLSEDVNRRmlvdranAEREKWVSAINTTFDHIGGGLRTILTdqnkLIVAVGGLTALAAGI 308
Cdd:COG4717 226 EEELEQLENELEAAALEER-------LKEARLLLLIAAALLALLGLGGSLLS----LILTIAGVLFLVLGL 285
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
396-418 1.18e-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: 40.60  E-value: 1.18e-03
                          10        20
                  ....*....|....*....|...
gi 22326858   396 APFRNILFYGPPGTGKTMAAREL 418
Cdd:pfam01078  20 AGGHNLLMIGPPGSGKTMLAKRL 42
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
112-246 1.26e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 41.72  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858  112 ESIKTREETRQAEFTAKAQEfKAMQSQAEAERQRVIYEEQKKLA---QHQAQTKSQMARYEDELARKRMQAENEAQRTRN 188
Cdd:PRK09510  78 EEQRKKKEQQQAEELQQKQA-AEQERLKQLEKERLAAQEQKKQAeeaAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRA 156
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 22326858  189 QELVKMQEESAIRREVARRATEEEIQAQRRQTEREKAEIERETiRVKAMAEAEGRARE 246
Cdd:PRK09510 157 AAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEA-KKKAEAEAKKKAAA 213
PRK12704 PRK12704
phosphodiesterase; Provisional
121-265 1.34e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858  121 RQAEFTAKAQEFKAMQSQAEAERQRviyEEQKKLAQHQAQTKSQMAR--YEDELARKRMQ-AENEAQRTRNQELVKMQEE 197
Cdd:PRK12704  27 KIAEAKIKEAEEEAKRILEEAKKEA---EAIKKEALLEAKEEIHKLRneFEKELRERRNElQKLEKRLLQKEENLDRKLE 103
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22326858  198 SAIRREVARRATEEEIQAQRRQTEREKAEIERetIRVKAMAEAEgraRESKLSEDVNRRMLVDRANAE 265
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEE--LIEEQLQELE---RISGLTAEEAKEILLEKVEEE 166
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
377-533 1.39e-03

DNA polymerase III, delta prime subunit [Replication, recombination and repair];


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 41.11  E-value: 1.39e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 377 LEKRIEQLANATANTKAHQApfrnILFYGPPGTGKTMAARELARR---------------SGLDYALMTGGDVAPLGAQA 441
Cdd:COG0470   1 QEEAWEQLLAAAESGRLPHA----LLLHGPPGIGKTTLALALARDllcenpeggkacgqcHSRLMAAGNHPDLLELNPEE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 442 VTK------IHQLFDW-SKKSKRG--LLLFIDEADAflcernktyMSEAqrsALNALLfRT-GDQSKDIVLALATNRPGD 511
Cdd:COG0470  77 KSDqigidqIRELGEFlSLTPLEGgrKVVIIDEADA---------MNEA---AANALL-KTlEEPPKNTPFILIANDPSR 143
                       170       180
                ....*....|....*....|..
gi 22326858 512 LDSAVADRIdETLEFPLPGEEE 533
Cdd:COG0470 144 LLPTIRSRC-QVIRFRPPSEEE 164
PRK04195 PRK04195
replication factor C large subunit; Provisional
378-467 1.41e-03

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 41.44  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858  378 EKRIEQLAnATANTKAHQAPFRNILFYGPPGTGKTMAARELARRSGLDYALMTGGD---------VAplGAQAVTKIhqL 448
Cdd:PRK04195  20 EKAKEQLR-EWIESWLKGKPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDqrtadvierVA--GEAATSGS--L 94
                         90
                 ....*....|....*....
gi 22326858  449 FDWSKKskrglLLFIDEAD 467
Cdd:PRK04195  95 FGARRK-----LILLDEVD 108
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
130-265 1.62e-03

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 41.66  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   130 QEFKAMQSQAEAERQRVIyEEQKKLAQHQAQTKSQMARYEDEL--ARKRMQAENEAQRTRNQELVKMQE--ESAIRREVA 205
Cdd:pfam07111 506 QEVGRAREQGEAERQQLS-EVAQQLEQELQRAQESLASVGQQLevARQGQQESTEEAASLRQELTQQQEiyGQALQEKVA 584
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22326858   206 RraTEEEIQAQRRQTEREKAEIERETIR-VKAMAEAEGRA-RESKLSEDVNRrmLVDRANAE 265
Cdd:pfam07111 585 E--VETRLREQLSDTKRRLNEARREQAKaVVSLRQIQHRAtQEKERNQELRR--LQDEARKE 642
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
373-465 1.81e-03

Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the RuvABC revolvasome which catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. Branch migration is catalyzed by the RuvB protein that is targeted to the Holliday junction by the structure specific RuvA protein. This family contains the N-terminal region of the protein.


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 39.41  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   373 LRPAL-------EKRIEQLANATANTKAHQAPFRNILFYGPPGTGKTMAARELARRSGLDYALMTG------GDVAPLga 439
Cdd:pfam05496   1 LRPRTldeyigqEKVKENLKIFIEAAKQRGEALDHVLLYGPPGLGKTTLANIIANEMGVNIRITSGpaierpGDLAAI-- 78
                          90       100
                  ....*....|....*....|....*.
gi 22326858   440 qaVTKIhqlfdwskksKRGLLLFIDE 465
Cdd:pfam05496  79 --LTNL----------EPGDVLFIDE 92
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
399-426 1.92e-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: 40.54  E-value: 1.92e-03
                        10        20
                ....*....|....*....|....*...
gi 22326858 399 RNILFYGPPGTGKTMAARELARRSGLDY 426
Cdd:COG0714  32 GHLLLEGVPGVGKTTLAKALARALGLPF 59
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
133-255 1.92e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 41.58  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   133 KAMQSQAEAERQRVIYEEQKKLAQHQAQTKSQMARYEDELA-------------RKRMQAENEAQRTRNQELV------- 192
Cdd:PRK10929  121 KSRQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRLQtlgtpntplaqaqLTALQAESAALKALVDELElaqlsan 200
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22326858   193 KMQEESAIRREVARRATEE---EIQAQRRQ--TEREKaEIERETIRVKAMAEAEGRARESKLSE-DVNR 255
Cdd:PRK10929  201 NRQELARLRSELAKKRSQQldaYLQALRNQlnSQRQR-EAERALESTELLAEQSGDLPKSIVAQfKINR 268
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
117-272 2.64e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 2.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 117 REETRQAEFTAKAQEFKAMQSQAEAERQRVIYEEQKKLAQHQAQTKSQmaryEDELARKRMQAENEAQRTRNqelvkmQE 196
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE----EEEEEEALEEAAEEEAELEE------EE 458
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22326858 197 ESAIRREVARRATEEEIQAQRRQTEREKAEIE-RETIRVKAMAEAEGRARESKLSEDVNRRMLVDRANAEREKWVSA 272
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAaRLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAA 535
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
405-466 3.05e-03

ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];


Pssm-ID: 440273 [Multi-domain]  Cd Length: 514  Bit Score: 40.73  E-value: 3.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 405 GPPGTGKT---MAARELARRSGLDYALmtggdVAP-----------LGAQAVTkIHQLFDWSKKSKRGL----------- 459
Cdd:COG0507 147 GGAGTGKTttlRALLAALEALGLRVAL-----AAPtgkaakrlsesTGIEART-IHRLLGLRPDSGRFRhnrdnpltpad 220

                ....*..
gi 22326858 460 LLFIDEA 466
Cdd:COG0507 221 LLVVDEA 227
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
112-244 3.80e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.17  E-value: 3.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858  112 ESIKTREETRQAEftAKAQEFKAMQSQAEaERQRVIYEEQKKLAQHQAQTKSQMARYEDELARKRMQAenEAQRTRNQEL 191
Cdd:PRK09510 109 ERLAAQEQKKQAE--EAAKQAALKQKQAE-EAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEA--EAAKKAAAEA 183
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 22326858  192 VKMQEESAIRR--EVARRATEEEIQAQRRQTEREKAEIERETIRVKAMAEAEGRA 244
Cdd:PRK09510 184 KKKAEAEAAAKaaAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAA 238
rfc PRK00440
replication factor C small subunit; Reviewed
400-420 4.60e-03

replication factor C small subunit; Reviewed


Pssm-ID: 234763 [Multi-domain]  Cd Length: 319  Bit Score: 39.47  E-value: 4.60e-03
                         10        20
                 ....*....|....*....|.
gi 22326858  400 NILFYGPPGTGKTMAARELAR 420
Cdd:PRK00440  40 HLLFAGPPGTGKTTAALALAR 60
COG2842 COG2842
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ...
402-467 4.93e-03

Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons];


Pssm-ID: 442090 [Multi-domain]  Cd Length: 254  Bit Score: 39.16  E-value: 4.93e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 402 LFYGPPGTGKTMAARELARRSGlDYALMTGGD-----------VAPLGAQAVT-KIHQLFD--WSKKSKRGLLLFIDEAD 467
Cdd:COG2842  54 VVYGESGVGKTTAAREYANRNP-NVIYVTASPswtskelleelAEELGIPAPPgTIADLRDriLERLAGTGRLLIIDEAD 132
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
401-421 5.01e-03

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


Pssm-ID: 459992  Cd Length: 102  Bit Score: 36.81  E-value: 5.01e-03
                          10        20
                  ....*....|....*....|.
gi 22326858   401 ILFYGPPGTGKTMAARELARR 421
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARA 21
PTZ00121 PTZ00121
MAEBL; Provisional
93-268 5.01e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 5.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858    93 RGAKALKGINNSAHAKKVFESIKTREETRQAEFTAKAQE---FKAMQSQAEAERQRVI-------------------YEE 150
Cdd:PTZ00121 1647 KKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEdekKAAEALKKEAEEAKKAeelkkkeaeekkkaeelkkAEE 1726
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   151 QKKLAQHQAQTKSQMARYEDELARKRMQAENEAQRTRNQELVKMQEESAIRREVARRATEEEIQAQRRQTEREKAEI-ER 229
Cdd:PTZ00121 1727 ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIfDN 1806
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 22326858   230 ETIRVKAMAEAEGRARESKLSEDVNRRMLVDRANAEREK 268
Cdd:PTZ00121 1807 FANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEE 1845
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
117-268 5.08e-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: 5.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   117 REETRQAEFTAKAQEFKAMQSQAEAERQRVIYEEQKKLAQHQAQTKSQMARYEDELARKRMQAENEAQRTRnQELVKMQE 196
Cdd:pfam13868  59 EEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLR-EEIDEFNE 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   197 ESAIRREVARRATEEE---IQAQRRQTEREKAEIERETIRVKAMAEAEGRARESKLSEDVNRR-----MLVDRANAEREK 268
Cdd:pfam13868 138 EQAEWKELEKEEEREEderILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKaerdeLRAKLYQEEQER 217
PRK12402 PRK12402
replication factor C small subunit 2; Reviewed
400-421 5.56e-03

replication factor C small subunit 2; Reviewed


Pssm-ID: 237090 [Multi-domain]  Cd Length: 337  Bit Score: 39.59  E-value: 5.56e-03
                         10        20
                 ....*....|....*....|..
gi 22326858  400 NILFYGPPGTGKTMAARELARR 421
Cdd:PRK12402  38 HLLVQGPPGSGKTAAVRALARE 59
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
378-421 5.76e-03

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 38.25  E-value: 5.76e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 22326858   378 EKRIEQLANATANTKAHQapFRNILFYGPPGTGKTMAARELARR 421
Cdd:pfam13191   6 EEELEQLLDALDRVRSGR--PPSVLLTGEAGTGKTTLLRELLRA 47
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
114-240 5.88e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 38.75  E-value: 5.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 114 IKTREETRQAEFTAKAQEFKAMQSQAEAERQRV--IYEEQKKLAQHQAQTKSQMARYEDELARKR-------MQAENEAQ 184
Cdd:COG1579  22 LEHRLKELPAELAELEDELAALEARLEAAKTELedLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeyeaLQKEIESL 101
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22326858 185 RTRNQ-----ELVKMQEESAIRREVA-----RRATEEEIQAQRRQTEREKAEIERETIRVKAMAEA 240
Cdd:COG1579 102 KRRISdledeILELMERIEELEEELAeleaeLAELEAELEEKKAELDEELAELEAELEELEAEREE 167
AAA_18 pfam13238
AAA domain;
401-436 6.30e-03

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 37.41  E-value: 6.30e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 22326858   401 ILFYGPPGTGKTMAARELARRSGLDYALmtgGDVAP 436
Cdd:pfam13238   1 ILITGTPGVGKTTLAKELSKRLGFGDNV---RDLAL 33
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
114-229 6.46e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 6.46e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 114 IKTREETRQAEFTAKAQEFKAMQSQAEAERQRVIYEEQKKLAQHQAQTKSQMARYEDELARKRMQAENEAQRTRNQELVK 193
Cdd:COG1196 648 EVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALE 727
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 22326858 194 MQEESAIRREVARRATEEE---------------IQAQRRQTEREKAEIER 229
Cdd:COG1196 728 EQLEAEREELLEELLEEEElleeealeelpeppdLEELERELERLEREIEA 778
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
164-269 6.54e-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: 39.13  E-value: 6.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   164 QMARYEDELARKRMQAENEAQRTRNQELVKMQEEsaiRREVARRATEEEIQAQ------RRQTEREKAEIERETIR--VK 235
Cdd:pfam13868  32 KRIKAEEKEEERRLDEMMEEERERALEEEEEKEE---ERKEERKRYRQELEEQieereqKRQEEYEEKLQEREQMDeiVE 108
                          90       100       110
                  ....*....|....*....|....*....|....
gi 22326858   236 AMAEAEGRARESKLSEDVNRRMLVDRANAEREKW 269
Cdd:pfam13868 109 RIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEW 142
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
118-222 7.54e-03

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: 37.71  E-value: 7.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   118 EETRQAEFTAKAQEFKAMQSQAEAERQRvIYEEQKKLAQHQAQTKSQMARYEDELARKRMQAENEAQRTRNQElvKMQEE 197
Cdd:pfam05672  31 EQERLEKEEEERLRKEELRRRAEEERAR-REEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQKQ--KEEAE 107
                          90       100
                  ....*....|....*....|....*
gi 22326858   198 SAIRREVARRATEEEIQAQRRQTER 222
Cdd:pfam05672 108 AKAREEAERQRQEREKIMQQEEQER 132
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
140-250 7.77e-03

Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.


Pssm-ID: 259804 [Multi-domain]  Cd Length: 293  Bit Score: 38.82  E-value: 7.77e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858 140 EAERQRV-IYEEQKKLAQHQAQTKsqmaryedelaRKR--MQAENEAQ--RTRNQELVkMQEESAIRRevarrateEEIQ 214
Cdd:cd03406 172 EAEKTKLlIAEQHQKVVEKEAETE-----------RKRavIEAEKDAEvaKIQMQQKI-MEKEAEKKI--------SEIE 231
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 22326858 215 AQRRqTEREKAEIERETIRVKAMAEAEgrarESKLS 250
Cdd:cd03406 232 DEMH-LAREKARADAEYYRALREAEAN----KLKLT 262
DEXXQc_Helz-like cd18038
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ...
382-413 7.87e-03

DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and similar proteins. Helicase with zinc finger (HELZ) acts as a helicase that plays a role in RNA metabolism during development. Moloney leukemia virus 10-like protein 1 (Mov10L1) binds Piwi-interacting RNA (piRNA) precursors to initiate piRNA processing. All are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350796 [Multi-domain]  Cd Length: 229  Bit Score: 38.37  E-value: 7.87e-03
                        10        20        30
                ....*....|....*....|....*....|....
gi 22326858 382 EQLA--NATANTKAHQAPFrniLFYGPPGTGKTM 413
Cdd:cd18038   5 EQKLavRNIVTGTSRPPPY---IIFGPPGTGKTV 35
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
112-246 9.04e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 38.75  E-value: 9.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   112 ESIKTREETRQAEFTAKAQEFKAMQSQAEAERQRVIYEEQKKLAQHQAQTKSQMARYE------DELARKRMQAENEAQR 185
Cdd:pfam13868 140 AEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQdekaerDELRAKLYQEEQERKE 219
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22326858   186 tRNQELVKMQEESAIRREVAR-RATEEEIQAQRRQTEREKAEIERETIRVKAMAEAEGRARE 246
Cdd:pfam13868 220 -RQKEREEAEKKARQRQELQQaREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEE 280
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
117-335 9.56e-03

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


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 38.83  E-value: 9.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   117 REETRQAEFTAKAQEFKAMQSQAEAERQRVIYEEqkklAQHQAQTKSQMARYEDELARKRMQAENEAQRTRNQELVKMQE 196
Cdd:pfam05262 219 KEELDKKQIDADKAQQKADFAQDNADKQRDEVRQ----KQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQIEIKKND 294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326858   197 ESAIRR------EVARRATEEEIQAQRRQTE--REKAEIERETIRVKAMAEAEGRARESKLSEDVN---RRMLVDRANAE 265
Cdd:pfam05262 295 EEALKAkdhkafDLKQESKASEKEAEDKELEaqKKREPVAEDLQKTKPQVEAQPTSLNEDAIDSSNpvyGLKVVDPITNL 374
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22326858   266 REKWVSAINTTFDHIGGGLRTI----LTDQNKLIVAVGGLT--ALAAGIYTTREGAKVIWSYVDRILGQPSLIRES 335
Cdd:pfam05262 375 SELVLIDLKTEVRLRESAQQTIrrrgLYEREKDLVAIAITSgnAKLQLVDIDLKNLEVIKESNFEIAKNSSLYVDS 450
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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