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Conserved domains on  [gi|489114781|ref|WP_003024632|]
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MULTISPECIES: flotillin family protein [Citrobacter]

Protein Classification

flotillin family protein( domain architecture ID 11455184)

flotillin family protein may act as a scaffolding protein within caveolar membranes, functionally participating in the formation of caveolae or caveolae-like vesicles

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
29-535 5.22e-84

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


:

Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 268.28  E-value: 5.22e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  29 FARLYRRASAEQAFVRTG-LGGQKVVMSGGAIVMPIFHEIIPINMNTLKLEVSRStvDSLITKDRMRVDVVVAFFVRVKP 107
Cdd:COG2268   24 LARFYRKVPPNEALVITGrGGGYKVVTGGGAFVLPVLHRAERMSLSTMTIEVERT--EGLITKDGIRVDVDAVFYVKVNS 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 108 SVEGIATAAQTLGQRTlsPEDLRVLIEDKFVDALRATASQMTMHELQDTRENFVQGVQNTVAEDLSKNGLELESVSLTNF 187
Cdd:COG2268  102 DPEDIANAAERFLGRD--PEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDL 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 188 NQtekvhfnPNNAFDAEGLTKLTQETERRRRERNEVEQDVEVAVREKNRdalsrkleieqQEAFMTLEQEQQVKTRT-AE 266
Cdd:COG2268  180 ED-------ENNYLDALGRRKIAEIIRDARIAEAEAERETEIAIAQANR-----------EAEEAELEQEREIETARiAE 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 267 QNAKIAAFEAERHREAEQTRILAERQIQETEIEREQAVrsrkveaerevrikeieqQQATEIANQTKSIAIAAKSEQQSQ 346
Cdd:COG2268  242 AEAELAKKKAEERREAETARAEAEAAYEIAEANAEREV------------------QRQLEIAEREREIELQEKEAEREE 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 347 AEARAndalaeavraqqnvettrqtaeadrakqvaliaaaqdaetqavELTVRAKAEKEAAELQAAAIvelAEATRKKGL 426
Cdd:COG2268  304 AELEA-------------------------------------------DVRKPAEAEKQAAEAEAEAE---AEAIRAKGL 337

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 427 AEAEAQRALNDAINVLSDEQtslkFKLALLQSLPAVIEKSVEPMKSIDGIKIIQvDGLNRGGAvgevtagnvtGGNLAEQ 506
Cdd:COG2268  338 AEAEGKRALAEAWNKLGDAA----ILLMLIEKLPEIAEAAAKPLEKIDKITIID-GGNGGNGA----------GSAVAEA 402

                        490       500
                 ....*....|....*....|....*....
gi 489114781 507 AlsaalayrtqAPLIDSLLNEIGLSGGSL 535
Cdd:COG2268  403 L----------APLLESLLEETGLDLPGL 421
HflC super family cl33838
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 353-435 5.91e-03

Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];


The actual alignment was detected with superfamily member COG0330:

Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 38.67  E-value: 5.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 353 DALAEAVRAQQNVETTRQTAEADRAKQVALI-----AAAQDAETQAVELTVRAKAEKEAAELQAAAIVELAEATRKKGLa 427
Cdd:COG0330  171 DAMEDRMKAEREREAAILEAEGYREAAIIRAegeaqRAIIEAEAYREAQILRAEGEAEAFRIVAEAYSAAPFVLFYRSL- 249


                 ....*...
gi 489114781 428 eaEAQRAL 435
Cdd:COG0330  250 --EALEEV 255
 
Name Accession Description Interval E-value
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
29-535 5.22e-84

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 268.28  E-value: 5.22e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  29 FARLYRRASAEQAFVRTG-LGGQKVVMSGGAIVMPIFHEIIPINMNTLKLEVSRStvDSLITKDRMRVDVVVAFFVRVKP 107
Cdd:COG2268   24 LARFYRKVPPNEALVITGrGGGYKVVTGGGAFVLPVLHRAERMSLSTMTIEVERT--EGLITKDGIRVDVDAVFYVKVNS 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 108 SVEGIATAAQTLGQRTlsPEDLRVLIEDKFVDALRATASQMTMHELQDTRENFVQGVQNTVAEDLSKNGLELESVSLTNF 187
Cdd:COG2268  102 DPEDIANAAERFLGRD--PEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDL 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 188 NQtekvhfnPNNAFDAEGLTKLTQETERRRRERNEVEQDVEVAVREKNRdalsrkleieqQEAFMTLEQEQQVKTRT-AE 266
Cdd:COG2268  180 ED-------ENNYLDALGRRKIAEIIRDARIAEAEAERETEIAIAQANR-----------EAEEAELEQEREIETARiAE 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 267 QNAKIAAFEAERHREAEQTRILAERQIQETEIEREQAVrsrkveaerevrikeieqQQATEIANQTKSIAIAAKSEQQSQ 346
Cdd:COG2268  242 AEAELAKKKAEERREAETARAEAEAAYEIAEANAEREV------------------QRQLEIAEREREIELQEKEAEREE 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 347 AEARAndalaeavraqqnvettrqtaeadrakqvaliaaaqdaetqavELTVRAKAEKEAAELQAAAIvelAEATRKKGL 426
Cdd:COG2268  304 AELEA-------------------------------------------DVRKPAEAEKQAAEAEAEAE---AEAIRAKGL 337

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 427 AEAEAQRALNDAINVLSDEQtslkFKLALLQSLPAVIEKSVEPMKSIDGIKIIQvDGLNRGGAvgevtagnvtGGNLAEQ 506
Cdd:COG2268  338 AEAEGKRALAEAWNKLGDAA----ILLMLIEKLPEIAEAAAKPLEKIDKITIID-GGNGGNGA----------GSAVAEA 402

                        490       500
                 ....*....|....*....|....*....
gi 489114781 507 AlsaalayrtqAPLIDSLLNEIGLSGGSL 535
Cdd:COG2268  403 L----------APLLESLLEETGLDLPGL 421
Flot pfam15975
Flotillin; Flotillin is a family of lipid-membrane-associated proteins found in bacteria, ...
 406-527 9.31e-38

Flotillin; Flotillin is a family of lipid-membrane-associated proteins found in bacteria, archaea and eukaryotes. The family is found in association with pfam01145, another integral membrane-associated domain. Flotillins in vertebrates are associated with sphingolipids and cholesterol-enriched membrane microdomains known as lipid-rafts. These rafts along with other membrane components are important in cell-signalling. Flotillins in other organizms have roles in viral pathogenesis, endocytosis, and membrane shaping.


Pssm-ID: 435047 [Multi-domain]  Cd Length: 121  Bit Score: 135.14  E-value: 9.31e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  406 AAELQAAAIVELAEATRKKGLAEAEAQRALNDAINVLSDEQTSLKFKLALLQSLPAVIEKSVEPMKSIDGIKIIQVDGLN 485
Cdd:pfam15975   1 EAEAEADAIKLRAEAKRKKALAEAEGIRALNEAENALSDEQIALQVKLALLEALPEIIAESVKPLEKIDGIKILQVDGLG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 489114781  486 rGGAVGEVTAGNVTGGNLAEQALSAALAYRTQAPLIDSLLNE 527
Cdd:pfam15975  81 -GGAAGGGGGGGGGGGSLAEQAVDSALGYRAQAPLIDSLLKE 121
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 59-209 2.47e-35

Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; The flotillin (reggie) like proteins are lipid raft-associated. Individual proteins of this SPFH family may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. In addition, microdomains formed from flotillin proteins may be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and interact with a variety of proteins. They may play a role 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.


Pssm-ID: 259798 [Multi-domain]  Cd Length: 145  Bit Score: 129.55  E-value: 2.47e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  59 IVMPIFHEIIPINMNTLKLEVSRSTVdslITKDRMRVDVVVAFFVRVKPSVEGIATAA-QTLGQRTlspEDLRVLIEDKF 137
Cdd:cd03399    1 FVIPFLQRVQRLSLETMTIDVKVEEV---LTKDGIPVDVTAVAQVKVGSDPEEIAAAAeRFLGKST---EEIRELVKETL 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489114781 138 VDALRATASQMTMHELQDTRENFVQGVQNTVAEDLSKNGLELESVSLTNFNQTEKvHFNPNNAFDAEGLTKL 209
Cdd:cd03399   75 EGHLRAIVGTMTVEEIYQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDISDDNG-YLESLGRKQAAEVKKD 145
PHB smart00244
prohibitin homologues; prohibitin homologues
 30-188 7.49e-15

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 72.31  E-value: 7.49e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781    30 ARLYRRASAEQAFVRTGLGGQKVVMSGGAIVMPIFHEIIPINMNTLKLEVSRSTVdslITKDRmrVDVVVAFFVRVKpSV 109
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQET---ITKDN--VKVSVDAVVYYR-VL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781   110 EGIATAAQTLGQRtlspedlRVLIEDKFVDALRATASQMTMHELQ-DTRENFVQGVQNTVAEDLSKNGLELESVSLTNFN 188
Cdd:smart00244  75 DPLRAVYRVLDAD-------YAVIEQLAQTTLRSVIGKRTLDELLtDQREKISENIREELNEAAEAWGIKVEDVEIKDIR 147
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 255-434 4.48e-10

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 61.75  E-value: 4.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 255 EQEQQVKTRTAEQNAKiaaFEAERHREAEQTRILAERQ-IQETEIEREQAVRSRKvEAEREVRIKEIEQQQATEIANQTK 333
Cdd:PRK09510  67 QQQQQKSAKRAEEQRK---KKEQQQAEELQQKQAAEQErLKQLEKERLAAQEQKK-QAEEAAKQAALKQKQAEEAAAKAA 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 334 SIAIAAKSEQQSQAEARANDALAEAVRAQQNVETTRQTAEadrAKQVALIAAAQDAETQAveltvRAKAEKEAAELQAAA 413
Cdd:PRK09510 143 AAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE---AKKKAEAEAAAKAAAEA-----KKKAEAEAKKKAAAE 214

                        170       180
                 ....*....|....*....|.
gi 489114781 414 IVELAEATRKKGLAEAEAQRA 434
Cdd:PRK09510 215 AKKKAAAEAKAAAAKAAAEAK 235
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 245-465 1.45e-08

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: 56.78  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  245 IEQQEAFMTLEQEQQVKTRTAEQNAKIAAFEAERHREAEQTRILAERQIQETEIEREQAVRSRKVEAEREvRIKEIEQQQ 324
Cdd:TIGR02794  43 VDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAK-QAEEKQKQA 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  325 ATEIANQTKSIAIAAKSEQQSQAEARANdALAEAVRAQQNVETTRQTAEADRAKQVALIAAAQDAETQAVELTVRAKAE- 403
Cdd:TIGR02794 122 EEAKAKQAAEAKAKAEAEAERKAKEEAA-KQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEa 200

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489114781  404 -KEAAELQAAAIVELAEATRKKGLAEAEAQRALNDAINVLSDEQTSLKFKLALLQSLPAVIEK 465
Cdd:TIGR02794 201 aKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDK 263
growth_prot_Scy NF041483
polarized growth protein Scy;
263-446 2.22e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 44.43  E-value: 2.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  263 RTAEQNAKIAAFEAERHR-----EAEQTRILAERQIQETEIEREQAVRSRKVEAEREVRIKEIEQQQATEIANQTKSIAI 337
Cdd:NF041483  520 RQAEETLERTRAEAERLRaeaeeQAEEVRAAAERAARELREETERAIAARQAEAAEELTRLHTEAEERLTAAEEALADAR 599

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  338 AAKSEQQSQAEARANDALAEAVRAQQNVEtTRQTAEADRAK-QVALIAAAQDAETQAVELTVRAKAEKEAAELQAAAive 416
Cdd:NF041483  600 AEAERIRREAAEETERLRTEAAERIRTLQ-AQAEQEAERLRtEAAADASAARAEGENVAVRLRSEAAAEAERLKSEA--- 675

                         170       180       190
                  ....*....|....*....|....*....|
gi 489114781  417 LAEATRKKGLAEAEAQRALNDAINVLSDEQ 446
Cdd:NF041483  676 QESADRVRAEAAAAAERVGTEAAEALAAAQ 705
growth_prot_Scy NF041483
polarized growth protein Scy;
265-430 1.05e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.12  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  265 AEQNAKIAAFEAERHREAEQTRILAERQIQETEIEREQAVRSRKVEAEREVRIKEIEQQQATEIANQTKSiAIAAKSEQQ 344
Cdd:NF041483  174 AEAEQALAAARAEAERLAEEARQRLGSEAESARAEAEAILRRARKDAERLLNAASTQAQEATDHAEQLRS-STAAESDQA 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  345 SQ--------AEARANDALAEAVRAQQNVETTRQTAEADRAKQVALIAAAQD-----AETQAVELTVRAKAEKEAAELQA 411
Cdd:NF041483  253 RRqaaelsraAEQRMQEAEEALREARAEAEKVVAEAKEAAAKQLASAESANEqrtrtAKEEIARLVGEATKEAEALKAEA 332

                         170
                  ....*....|....*....
gi 489114781  412 AAIVELAEATRKKGLAEAE 430
Cdd:NF041483  333 EQALADARAEAEKLVAEAA 351
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 353-435 5.91e-03

Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 38.67  E-value: 5.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 353 DALAEAVRAQQNVETTRQTAEADRAKQVALI-----AAAQDAETQAVELTVRAKAEKEAAELQAAAIVELAEATRKKGLa 427
Cdd:COG0330  171 DAMEDRMKAEREREAAILEAEGYREAAIIRAegeaqRAIIEAEAYREAQILRAEGEAEAFRIVAEAYSAAPFVLFYRSL- 249


                 ....*...
gi 489114781 428 eaEAQRAL 435
Cdd:COG0330  250 --EALEEV 255
 
Name Accession Description Interval E-value
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
29-535 5.22e-84

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 268.28  E-value: 5.22e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  29 FARLYRRASAEQAFVRTG-LGGQKVVMSGGAIVMPIFHEIIPINMNTLKLEVSRStvDSLITKDRMRVDVVVAFFVRVKP 107
Cdd:COG2268   24 LARFYRKVPPNEALVITGrGGGYKVVTGGGAFVLPVLHRAERMSLSTMTIEVERT--EGLITKDGIRVDVDAVFYVKVNS 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 108 SVEGIATAAQTLGQRTlsPEDLRVLIEDKFVDALRATASQMTMHELQDTRENFVQGVQNTVAEDLSKNGLELESVSLTNF 187
Cdd:COG2268  102 DPEDIANAAERFLGRD--PEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDL 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 188 NQtekvhfnPNNAFDAEGLTKLTQETERRRRERNEVEQDVEVAVREKNRdalsrkleieqQEAFMTLEQEQQVKTRT-AE 266
Cdd:COG2268  180 ED-------ENNYLDALGRRKIAEIIRDARIAEAEAERETEIAIAQANR-----------EAEEAELEQEREIETARiAE 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 267 QNAKIAAFEAERHREAEQTRILAERQIQETEIEREQAVrsrkveaerevrikeieqQQATEIANQTKSIAIAAKSEQQSQ 346
Cdd:COG2268  242 AEAELAKKKAEERREAETARAEAEAAYEIAEANAEREV------------------QRQLEIAEREREIELQEKEAEREE 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 347 AEARAndalaeavraqqnvettrqtaeadrakqvaliaaaqdaetqavELTVRAKAEKEAAELQAAAIvelAEATRKKGL 426
Cdd:COG2268  304 AELEA-------------------------------------------DVRKPAEAEKQAAEAEAEAE---AEAIRAKGL 337

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 427 AEAEAQRALNDAINVLSDEQtslkFKLALLQSLPAVIEKSVEPMKSIDGIKIIQvDGLNRGGAvgevtagnvtGGNLAEQ 506
Cdd:COG2268  338 AEAEGKRALAEAWNKLGDAA----ILLMLIEKLPEIAEAAAKPLEKIDKITIID-GGNGGNGA----------GSAVAEA 402

                        490       500
                 ....*....|....*....|....*....
gi 489114781 507 AlsaalayrtqAPLIDSLLNEIGLSGGSL 535
Cdd:COG2268  403 L----------APLLESLLEETGLDLPGL 421
Flot pfam15975
Flotillin; Flotillin is a family of lipid-membrane-associated proteins found in bacteria, ...
 406-527 9.31e-38

Flotillin; Flotillin is a family of lipid-membrane-associated proteins found in bacteria, archaea and eukaryotes. The family is found in association with pfam01145, another integral membrane-associated domain. Flotillins in vertebrates are associated with sphingolipids and cholesterol-enriched membrane microdomains known as lipid-rafts. These rafts along with other membrane components are important in cell-signalling. Flotillins in other organizms have roles in viral pathogenesis, endocytosis, and membrane shaping.


Pssm-ID: 435047 [Multi-domain]  Cd Length: 121  Bit Score: 135.14  E-value: 9.31e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  406 AAELQAAAIVELAEATRKKGLAEAEAQRALNDAINVLSDEQTSLKFKLALLQSLPAVIEKSVEPMKSIDGIKIIQVDGLN 485
Cdd:pfam15975   1 EAEAEADAIKLRAEAKRKKALAEAEGIRALNEAENALSDEQIALQVKLALLEALPEIIAESVKPLEKIDGIKILQVDGLG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 489114781  486 rGGAVGEVTAGNVTGGNLAEQALSAALAYRTQAPLIDSLLNE 527
Cdd:pfam15975  81 -GGAAGGGGGGGGGGGSLAEQAVDSALGYRAQAPLIDSLLKE 121
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 59-209 2.47e-35

Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; The flotillin (reggie) like proteins are lipid raft-associated. Individual proteins of this SPFH family may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. In addition, microdomains formed from flotillin proteins may be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and interact with a variety of proteins. They may play a role 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.


Pssm-ID: 259798 [Multi-domain]  Cd Length: 145  Bit Score: 129.55  E-value: 2.47e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  59 IVMPIFHEIIPINMNTLKLEVSRSTVdslITKDRMRVDVVVAFFVRVKPSVEGIATAA-QTLGQRTlspEDLRVLIEDKF 137
Cdd:cd03399    1 FVIPFLQRVQRLSLETMTIDVKVEEV---LTKDGIPVDVTAVAQVKVGSDPEEIAAAAeRFLGKST---EEIRELVKETL 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489114781 138 VDALRATASQMTMHELQDTRENFVQGVQNTVAEDLSKNGLELESVSLTNFNQTEKvHFNPNNAFDAEGLTKL 209
Cdd:cd03399   75 EGHLRAIVGTMTVEEIYQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDISDDNG-YLESLGRKQAAEVKKD 145
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 226-523 2.01e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 79.60  E-value: 2.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 226 DVEVAVREKNRDALSRKLEIEQQEAFMTLEQEQQVKTRTAEQNAKIAAFEAERHREAEQTRILAERQIQETEIEREQAVR 305
Cdd:COG1196  266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 306 SRKVEAEREVRIKEIEQQQATEIANQTKSIAIAAKSEQQSQAEARANDALAEAVRAQQNVETTRQTAEADRAKQVALIAA 385
Cdd:COG1196  346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 386 AQDAETQAVELTVRAKAEKEAAELQAAAIVELAEATRKKGLAEAEAQRALNDAINVLSDEQTSLKFKLALLQSLPAVIEK 465
Cdd:COG1196  426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489114781 466 SVEPmksidgikIIQVDGLNRGGAVGEVTAGNVTGGNLAEQALSAALAYRTQAPLIDS 523
Cdd:COG1196  506 FLEG--------VKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVED 555
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 40-188 3.17e-15

SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent phylogenetic analysis has shown this domain to be a slipin or Stomatin-like integral membrane domain conserved from protozoa to mammals.


Pssm-ID: 426078 [Multi-domain]  Cd Length: 177  Bit Score: 73.89  E-value: 3.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781   40 QAFVRTGLGG-QKVVMSGGAIVMPIFHEIIPINMNTLKLEVSRSTVdslITKDRMRVDVVVAFFVRVKPsvegiaTAAQT 118
Cdd:pfam01145   7 EVGVVTRFGKlSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTV---LTKDGVPVNVDVTVIYRVNP------DDPPK 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  119 LGQRTLSPEDLRVLIEDKFVDALRATASQMTMHELQDTRENFVQGVQNTVAEDLSKNGLELESVSLTNFN 188
Cdd:pfam01145  78 LVQNVFGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDID 147
PHB smart00244
prohibitin homologues; prohibitin homologues
 30-188 7.49e-15

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 72.31  E-value: 7.49e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781    30 ARLYRRASAEQAFVRTGLGGQKVVMSGGAIVMPIFHEIIPINMNTLKLEVSRSTVdslITKDRmrVDVVVAFFVRVKpSV 109
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQET---ITKDN--VKVSVDAVVYYR-VL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781   110 EGIATAAQTLGQRtlspedlRVLIEDKFVDALRATASQMTMHELQ-DTRENFVQGVQNTVAEDLSKNGLELESVSLTNFN 188
Cdd:smart00244  75 DPLRAVYRVLDAD-------YAVIEQLAQTTLRSVIGKRTLDELLtDQREKISENIREELNEAAEAWGIKVEDVEIKDIR 147
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 232-457 1.54e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.19  E-value: 1.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 232 REKNRDALSRKLEIEQQEAFMTLEQEQQVKTRTAEQNAKIAAFEAERHREAEQTRILAERQIQETEIEREQAVRSRKVEA 311
Cdd:COG1196  237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 312 EREVRIKEIEQQQATEIANQTKSIAIAAKS----EQQSQAEARANDALAEAVRAQQNVETTRQTAEADRAKQVALIAAAQ 387
Cdd:COG1196  317 RLEELEEELAELEEELEELEEELEELEEELeeaeEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489114781 388 DAETQAVELTVRAKA-EKEAAELQAAAIVELAEATRKKGLAEAEAQRALNDAINVLSDEQTSLKFKLALLQ 457
Cdd:COG1196  397 ELAAQLEELEEAEEAlLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 228-468 2.34e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.42  E-value: 2.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 228 EVAVREKNRDALSRKLEIEQQEAfmtleQEQQVKTRTAEQNAKIAAFEAE-RHREAEQTRILAERQIQETEIEREQAV-- 304
Cdd:COG1196  217 ELKEELKELEAELLLLKLRELEA-----ELEELEAELEELEAELEELEAElAELEAELEELRLELEELELELEEAQAEey 291

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 305 ----RSRKVEAEREVRIKEIEQQQATEIANQTKSIAIAAKSEQQSQAEARANDALAEA-------VRAQQNVETTRQTAE 373
Cdd:COG1196  292 ellaELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAeeeleeaEAELAEAEEALLEAE 371

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 374 ADRAKQVALIAAAQDAETQAVELTVRAKAEKEAAELQAAAIVELAEATRKKGLAEAEAQRALNDAINVLSDEQTSLKFKL 453
Cdd:COG1196  372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451

                        250
                 ....*....|....*
gi 489114781 454 ALLQSLPAVIEKSVE 468
Cdd:COG1196  452 AELEEEEEALLELLA 466
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 255-434 4.48e-10

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 61.75  E-value: 4.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 255 EQEQQVKTRTAEQNAKiaaFEAERHREAEQTRILAERQ-IQETEIEREQAVRSRKvEAEREVRIKEIEQQQATEIANQTK 333
Cdd:PRK09510  67 QQQQQKSAKRAEEQRK---KKEQQQAEELQQKQAAEQErLKQLEKERLAAQEQKK-QAEEAAKQAALKQKQAEEAAAKAA 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 334 SIAIAAKSEQQSQAEARANDALAEAVRAQQNVETTRQTAEadrAKQVALIAAAQDAETQAveltvRAKAEKEAAELQAAA 413
Cdd:PRK09510 143 AAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE---AKKKAEAEAAAKAAAEA-----KKKAEAEAKKKAAAE 214

                        170       180
                 ....*....|....*....|.
gi 489114781 414 IVELAEATRKKGLAEAEAQRA 434
Cdd:PRK09510 215 AKKKAAAEAKAAAAKAAAEAK 235
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 245-450 2.23e-09

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 59.43  E-value: 2.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 245 IEQQEAFMTLEQEQ---QVKTRTAEQNAKIAAfEAERHREAEQTRILAERQIQETEIEREQAVRSRKVEAEREVRIKEIE 321
Cdd:PRK09510  67 QQQQQKSAKRAEEQrkkKEQQQAEELQQKQAA-EQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAA 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 322 QQQATEIANQTKSIAIAAKSEQQSQAEARANDALAEAVRAQQNVETTRQTAEADRAKQVALIAAAQDAETQA-VELTVRA 400
Cdd:PRK09510 146 KAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKkAAAEAKA 225

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 489114781 401 KAEKEAAELQAAAIVElAEATRKKGLAEAEAQRALNDAINVLSDEQTSLK 450
Cdd:PRK09510 226 AAAKAAAEAKAAAEKA-AAAKAAEKAAAAKAAAEVDDLFGGLDSGKNAPK 274
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 43-193 1.38e-08

Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prohibitin (a lipid raft-associated integral membrane protein). Individual proteins of the SPFH (band 7) domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. These microdomains, in addition to being stable scaffolds, may also be dynamic units with their own regulatory functions. Prohibitin is a mitochondrial inner-membrane protein which may act as a chaperone for the stabilization of mitochondrial proteins. Human prohibitin forms a hetero-oligomeric complex with Bap-37 (prohibitin 2, an SPFH domain carrying homolog). This complex may protect non-assembled membrane proteins against proteolysis by the m-AAA protease. Prohibitin and Bap-37 yeast homologs have been implicated in yeast longevity and in the maintenance of mitochondrial morphology.


Pssm-ID: 259799 [Multi-domain]  Cd Length: 195  Bit Score: 54.83  E-value: 1.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  43 VRTGLGGQKVVMSGGA-IVMPIFHEIIPINMNTLKLEVSRSTvdslITKDRMRVDVVVAffVRVKPSVEGIATAAQTLGq 121
Cdd:cd03401   13 FRRGKGVKDEVLGEGLhFKIPWIQVVIIYDVRTQPREITLTV----LSKDGQTVNIDLS--VLYRPDPEKLPELYQNLG- 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489114781 122 rtlsPEDLRVLIEDKFVDALRATASQMTMHELQDTRENFVQGVQNTVAEDLSKNGLELESVSLTNFNQTEKV 193
Cdd:cd03401   86 ----PDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEY 153
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 245-465 1.45e-08

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: 56.78  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  245 IEQQEAFMTLEQEQQVKTRTAEQNAKIAAFEAERHREAEQTRILAERQIQETEIEREQAVRSRKVEAEREvRIKEIEQQQ 324
Cdd:TIGR02794  43 VDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAK-QAEEKQKQA 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  325 ATEIANQTKSIAIAAKSEQQSQAEARANdALAEAVRAQQNVETTRQTAEADRAKQVALIAAAQDAETQAVELTVRAKAE- 403
Cdd:TIGR02794 122 EEAKAKQAAEAKAKAEAEAERKAKEEAA-KQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEa 200

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489114781  404 -KEAAELQAAAIVELAEATRKKGLAEAEAQRALNDAINVLSDEQTSLKFKLALLQSLPAVIEK 465
Cdd:TIGR02794 201 aKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDK 263
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 211-438 7.14e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 7.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 211 QETERRRRERNEVEQDVEVAVREKNRDALSRKLEIEQQEAFMTLEQEQQVKTRTAEQNAKIAAFEAERHREAEQTRILAE 290
Cdd:COG1196  343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 291 RQIQETEIE--REQAVRSRKVEAEREVRIKEIEQQQATEIANQTKSIAIAAKSEQQSQAEARANDALAEAVRAQQNVETT 368
Cdd:COG1196  423 LEELEEALAelEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 369 RQTAEADRAKQVALIAAAQDAETQAVELTVRAKAEKEAAELQAAAIVELAEATRKKGLAEAEAQRALNDA 438
Cdd:COG1196  503 YEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAG 572
PTZ00121 PTZ00121
MAEBL; Provisional
 231-434 1.23e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.76  E-value: 1.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  231 VREKNRDALSRKLEIEQ--QEAFMTLEQEQQVKTRTAEQNAKI-AAFEAERHREAEQTRiLAERQIQETEIEREQAVRSR 307
Cdd:PTZ00121 1160 AEDARKAEEARKAEDAKkaEAARKAEEVRKAEELRKAEDARKAeAARKAEEERKAEEAR-KAEDAKKAEAVKKAEEAKKD 1238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  308 KVEAER--EVRIKEIEQQQATEIANQTKSIAIAAKSEQQSQAEARANdalAEAVRAQQNVETTRQTAEADRAKQVALIA- 384
Cdd:PTZ00121 1239 AEEAKKaeEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK---AEEKKKADEAKKAEEKKKADEAKKKAEEAk 1315

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 489114781  385 AAQDAETQAVELTVRAKA-EKEAAELQAAAIVELAEATRKKGLAEAEAQRA 434
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAaKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 50-313 1.02e-06

Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 50.61  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  50 QKVVMSGGAIVMPIFHEIIPINMNTLKLEVSRSTVdslITKDRmrVDVVVAFFVRVKpsVEGIATAAQTLgqrtlspEDL 129
Cdd:COG0330   39 VRTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEV---LTKDN--NIVDVDAVVQYR--ITDPAKFLYNV-------ENA 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 130 RVLIEDKFVDALRATASQMTMHELQDT-RENFVQGVQNTVAEDLSKNGLELESVSLTNFNQTEKVhfnpnnafdaegltk 208
Cdd:COG0330  105 EEALRQLAESALREVIGKMTLDEVLSTgRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEV--------------- 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 209 ltqeterrrrerneveqdvevavreknrdalsrkleieqQEAFmtleqEQQVKtrtAEQNAKIAAFEAERHREAEQTRIL 288
Cdd:COG0330  170 ---------------------------------------QDAM-----EDRMK---AEREREAAILEAEGYREAAIIRAE 202

                        250       260
                 ....*....|....*....|....*..
gi 489114781 289 AERQ--IQETEIEREQAVRSRKVEAER 313
Cdd:COG0330  203 GEAQraIIEAEAYREAQILRAEGEAEA 229
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 255-524 1.85e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.83  E-value: 1.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781   255 EQEQQVKTRTAEQNAKIAAFEAERhREAEQTRILAERQIQETEIEREQAVRSRKVEAEREVRIKEIEQQQATEIANQtkS 334
Cdd:TIGR02168  281 EEIEELQKELYALANEISRLEQQK-QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESL--E 357

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781   335 IAIAAKSEQQSQAEARANDALAEAVRAQQNVETTRQTAEADRAKQVALIAAAQDAETQAVELTVRAKAEKEAAELQAAAI 414
Cdd:TIGR02168  358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE 437

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781   415 VELAEATRKKGLAEAEAQRA--------LNDAINVLSDEQTSLKFKLALLQSLPAVIEKSVEPMKSI-DGIKIIQVDGLN 485
Cdd:TIGR02168  438 LQAELEELEEELEELQEELErleealeeLREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFsEGVKALLKNQSG 517

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 489114781   486 RGGAVGEVTAGnVTGGNLAEQALSAALAYRTQAPLIDSL 524
Cdd:TIGR02168  518 LSGILGVLSEL-ISVDEGYEAAIEAALGGRLQAVVVENL 555
PTZ00121 PTZ00121
MAEBL; Provisional
 203-408 2.11e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 2.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  203 AEGLTKLTQETERRRRERNEVEQDVEVAVR-EKNRDALSRKLEIEQQ------EAFMTLEQEQQVKTRTAEQNAKIAAFE 275
Cdd:PTZ00121 1542 AEEKKKADELKKAEELKKAEEKKKAEEAKKaEEDKNMALRKAEEAKKaeeariEEVMKLYEEEKKMKAEEAKKAEEAKIK 1621

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  276 AERHREAEQTRILAERQIQETEIEREQAVRSRKVEAEREVRIKEIEQQqateiANQTKSIAIAAKSEQQSqaEARANDAL 355
Cdd:PTZ00121 1622 AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK-----AEEDKKKAEEAKKAEED--EKKAAEAL 1694

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 489114781  356 AEAVRAQQNVETTRQTAEADRAKQVALIAAAQDAETQAVELTVRAKAEKEAAE 408
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
269-458 2.21e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.68  E-value: 2.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  269 AKIAAFEAERHReaeqtrilAERQIQETEIEREQAVRSRKVEAEREVRIKEIEQQQATEIANQTKSIAIAAKSEQQSQAE 348
Cdd:COG4913   610 AKLAALEAELAE--------LEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLD 681

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  349 ArANDALAEAVRAQQNVETTRQTAEADRAKQVALIAAAQDAETQAVELTVRAKAEKEAAELQAAAIVELAEATRkkgLAE 428
Cdd:COG4913   682 A-SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER---FAA 757

                         170       180       190
                  ....*....|....*....|....*....|
gi 489114781  429 AEAQRALNDAINVLSDEQTSLKFKLALLQS 458
Cdd:COG4913   758 ALGDAVERELRENLEERIDALRARLNRAEE 787
PRK12472 PRK12472
hypothetical protein; Provisional
 311-438 5.31e-06

hypothetical protein; Provisional


Pssm-ID: 237110 [Multi-domain]  Cd Length: 508  Bit Score: 49.10  E-value: 5.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 311 AEREVRikeiEQQQATEIANQTKSIAIAAKSEQQS---------QAEARANDALAEAVRAQQNVETTRQTAEADRAKQVA 381
Cdd:PRK12472 192 AETLAR----EAEDAARAADEAKTAAAAAAREAAPlkaslrkleRAKARADAELKRADKALAAAKTDEAKARAEERQQKA 267

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489114781 382 lIAAAQDAETQAVEltvrAKAEKEAAELQAAAIVELAEATRKKglaEAEAQRALNDA 438
Cdd:PRK12472 268 -AQQAAEAATQLDT----AKADAEAKRAAAAATKEAAKAAAAK---KAETAKAATDA 316
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 244-435 5.39e-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: 49.35  E-value: 5.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  244 EIEQQEAFMTLEQE-----QQVKTRTAEQNAKIAAFEAERHRE--------AEQTRILAERQ-----IQETEIERE-QAV 304
Cdd:pfam17380 286 ERQQQEKFEKMEQErlrqeKEEKAREVERRRKLEEAEKARQAEmdrqaaiyAEQERMAMERErelerIRQEERKRElERI 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  305 RSRKVEAE----REVRIKEIEQQQATEIANQTKSIAIAAK-SEQQSQAEARANDALAEAVRAQQNVETTRQTA--EADRA 377
Cdd:pfam17380 366 RQEEIAMEisrmRELERLQMERQQKNERVRQELEAARKVKiLEEERQRKIQQQKVEMEQIRAEQEEARQREVRrlEEERA 445

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 489114781  378 KQVALIAAAQDAETQAVELTVRAKAEKEAAELqaaaivELAEATRKKGLAEAEAQRAL 435
Cdd:pfam17380 446 REMERVRLEEQERQQQVERLRQQEEERKRKKL------ELEKEKRDRKRAEEQRRKIL 497
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 242-434 5.96e-06

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 48.69  E-value: 5.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  242 KLEIEQQEAFMTLEQEQQvktRTAEQNAKIAAFEAERHREAEQTRILAERQIQETEIEREQAVRSRKVEAEREVRIKEIE 321
Cdd:TIGR02794  72 KLEQQAEEAEKQRAAEQA---RQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEA 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  322 QQQAtEIANQTKSIAIAAKSEQQSQAEARANDALAEAVRAQQNVETTRQTAEADRAKQVALIAAAQDAETQAVEltvRAK 401
Cdd:TIGR02794 149 AKQA-EEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAA---AAE 224

                         170       180       190
                  ....*....|....*....|....*....|...
gi 489114781  402 AEKEAAELQAAAIVELAEATRKKGLAEAEAQRA 434
Cdd:TIGR02794 225 AERKADEAELGDIFGLASGSNAEKQGGARGAAA 257
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 232-428 1.17e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 47.88  E-value: 1.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 232 REKNRDALSRKLEIEQQEAfmtLEQEQQvktrtaeqnakiaafeaerhREAEQTRILAERQIQETEIEREQAVRSRKVEA 311
Cdd:PRK09510  93 QQKQAAEQERLKQLEKERL---AAQEQK--------------------KQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 312 EREVRIKEIEQQQATEIANQTksiaiaAKSEQQSQAEARANdALAEAVRAQQNVETTRQTAEADrAKQVALIAAAQDAET 391
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKK------AEAEAAKKAAAEAK-KKAEAEAAAKAAAEAKKKAEAE-AKKKAAAEAKKKAAA 221

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 489114781 392 QAVELTVRAKAEKEAAELQAAAIVELAEATRKKGLAE 428
Cdd:PRK09510 222 EAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 269-434 2.71e-05

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 46.86  E-value: 2.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 269 AKIAAFEAERHReAEQTRILAE-RQIQeteIEREqavrsrkvEAEREVRIKEIEQQQATEIANQTKSiAIAAKSEQQSQA 347
Cdd:PRK05035 436 AEIRAIEQEKKK-AEEAKARFEaRQAR---LERE--------KAAREARHKKAAEARAAKDKDAVAA-ALARVKAKKAAA 502

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 348 EARANDALAEAVRAQQNVETTRQTAEADRAKQVALIA-AAQDAETQAVELTV-RAKAEKeaAELQAAAIVELAEATRKKG 425
Cdd:PRK05035 503 TQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAaAAADPKKAAVAAAIaRAKAKK--AAQQAANAEAEEEVDPKKA 580


                 ....*....
gi 489114781 426 LAEAEAQRA 434
Cdd:PRK05035 581 AVAAAIARA 589
PTZ00491 PTZ00491
major vault protein; Provisional
 225-424 3.20e-05

major vault protein; Provisional


Pssm-ID: 240439 [Multi-domain]  Cd Length: 850  Bit Score: 46.93  E-value: 3.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 225 QDVEVaVREKNRDALSR--KLEIEqqeafmtleqeqqVKTRTAEQNAkiaafeaeRHReaeqtrilAERQIQETEIEREQ 302
Cdd:PTZ00491 636 QSVEP-VDERTRDSLQKsvQLAIE-------------ITTKSQEAAA--------RHQ--------AELLEQEARGRLER 685

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 303 AVRSRKVEAEREvRIKEIEQQqateianqTKSIAIAAKSEQQSQAEARANDALAEavrAQQNVETTRQTAEADRakqval 382
Cdd:PTZ00491 686 QKMHDKAKAEEQ-RTKLLELQ--------AESAAVESSGQSRAEALAEAEARLIE---AEAEVEQAELRAKALR------ 747

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 489114781 383 IAAAQDAETQAVELTVRAKAEKEAAELQAAAIVELAEATRKK 424
Cdd:PTZ00491 748 IEAEAELEKLRKRQELELEYEQAQNELEIAKAKELADIEATK 789
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 246-443 4.05e-05

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 46.87  E-value: 4.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  246 EQQEAFMTLEQEQQVKTRTAEQNAKIAAFEAERHREAEQ--TRILAE----------RQI------QETEIEREQAVRSR 307
Cdd:COG3096   441 DYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYElvCKIAGEversqawqtaRELlrryrsQQALAQRLQQLRAQ 520

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  308 KVEAEREVRikeiEQQQATEIANQ-TKSIAIAAKS-----EQQSQAEARANDALAEAVRAQQNVETTRQTAEADRAKQVA 381
Cdd:COG3096   521 LAELEQRLR----QQQNAERLLEEfCQRIGQQLDAaeeleELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKE 596

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489114781  382 LIA------AAQDAETQAVELTvrAKAEKEAAELQAA---AIVELAEATRKKGLAeAEAQRALNDAINVLS 443
Cdd:COG3096   597 LAArapawlAAQDALERLREQS--GEALADSQEVTAAmqqLLEREREATVERDEL-AARKQALESQIERLS 664
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 244-440 4.90e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 4.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 244 EIEQQEAFMTLEQEQQVKTRTAEQNAKIAAFEAERHREAEQTRILAERQIQETEIEREQAVRSRKVEAEREVRIKEIEQQ 323
Cdd:COG1196  607 DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAE 686

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 324 QATEIANQTKSIAIAAKSEQQSQAEARANDALAEAVRAQQNVETTRQTAEADRAKQVALIAAAQDAETQAVELTVRAKAE 403
Cdd:COG1196  687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489114781 404 KEAAELQA----------AAIVELAEA-TRKKGLAE-----AEAQRALNDAIN 440
Cdd:COG1196  767 RELERLEReiealgpvnlLAIEEYEELeERYDFLSEqredlEEARETLEEAIE 819
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 227-458 5.45e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 5.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781   227 VEVAVREKNRDALSRKLEIEQQEAFMTL-EQEQQVK-----TRTAEQNAKIAAFEAERhREAEQTRILAERQIQETEIER 300
Cdd:TIGR02168  191 LEDILNELERQLKSLERQAEKAERYKELkAELRELElallvLRLEELREELEELQEEL-KEAEEELEELTAELQELEEKL 269

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781   301 EQaVRSRKVEAEREVRIKEIEQQQAT-EIANQTKSIAIAAKSEQQSQAEarandaLAEAVRAQQNVETTRQTAEADRAKQ 379
Cdd:TIGR02168  270 EE-LRLEVSELEEEIEELQKELYALAnEISRLEQQKQILRERLANLERQ------LEELEAQLEELESKLDELAEELAEL 342

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781   380 VALIAAAQDAETQAVELTVRAKAEKEAAELQAAAIVELAEATRKKgLAEAEAQRALNDA-INVLSDEQTSLKFKLALLQS 458
Cdd:TIGR02168  343 EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK-VAQLELQIASLNNeIERLEARLERLEDRRERLQQ 421
PTZ00121 PTZ00121
MAEBL; Provisional
 230-433 6.64e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 6.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  230 AVREKNRDALSRKLEIEQQEAFMTLEQEQQVKTRTAEQNAKIAAFEAERHREAEQTRILAERQIQETEIEREQAVRSRKV 309
Cdd:PTZ00121 1361 AAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKA 1440

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  310 EAER---EVRIKEIEQQQATEIANQTKSIAIAAKSEQQSQAEARANDALAEAVRAQQNVETTRQTAE----ADRAKQVAL 382
Cdd:PTZ00121 1441 EEAKkadEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEakkkADEAKKAEE 1520

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 489114781  383 IAAAQDA----ETQAVELTVRAKAEKEAAELQAAAIVELAEATRKKGLAEAEAQR 433
Cdd:PTZ00121 1521 AKKADEAkkaeEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEED 1575
PTZ00121 PTZ00121
MAEBL; Provisional
 225-401 8.87e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 8.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  225 QDVEVAVREKNRDALSRKLEIEQQEAFMTLEQEQQVKTRTAEQNAKIAAFE---AERHREAEQTRILAERQIQETEIERE 301
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDkkkAEEAKKAEEDEKKAAEALKKEAEEAK 1702

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  302 QAVRSRKVEAERevrIKEIEQQQATEIANQTKSIAIAAKSEQQSQAEARANDALAEAVRAQQNVETTRQTAEADRAKQVA 381
Cdd:PTZ00121 1703 KAEELKKKEAEE---KKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEA 1779

                         170       180
                  ....*....|....*....|
gi 489114781  382 LIAAAQDAETQAVELTVRAK 401
Cdd:PTZ00121 1780 VIEEELDEEDEKRRMEVDKK 1799
PTZ00121 PTZ00121
MAEBL; Provisional
 240-438 1.01e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  240 SRKLEIEQQ-EAFMTLEQEQQVKTRTAEQNAKIAAFEAerhREAEQTRILAERQIQETEIEREQAVRSRKVEAEREVRIK 318
Cdd:PTZ00121 1205 ARKAEEERKaEEARKAEDAKKAEAVKKAEEAKKDAEEA---KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKAD 1281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  319 EI---EQQQATEIANQTKSIAIAAKSEQQSQAEARANDALAEAVRAQQNVETTRQTAEADRAKQValiAAAQDAETQAVE 395
Cdd:PTZ00121 1282 ELkkaEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAE---AAKAEAEAAADE 1358

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 489114781  396 LTvRAKAEKEAAELQAAAIVELAEATRKKGLAEAEAQRALNDA 438
Cdd:PTZ00121 1359 AE-AAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKA 1400
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
253-434 1.26e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  253 TLEQEQQVKTRTAEQNAKIAAFEAERHR----EAEQTRILAERQIQETEIEREQAvRSRKVEAEREVRIKEIEQQQATEI 328
Cdd:COG4913   253 LLEPIRELAERYAAARERLAELEYLRAAlrlwFAQRRLELLEAELEELRAELARL-EAELERLEARLDALREELDELEAQ 331

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  329 ANQTKSIAIAAKSEQQSQAEARANDALAEAVRAQQNVETTRQTAEADRAKQVALIAAAQDAETQAVELtvrakaEKEAAE 408
Cdd:COG4913   332 IRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEE------LEALEE 405

                         170       180
                  ....*....|....*....|....*.
gi 489114781  409 LQAAAIVELAEATRKkgLAEAEAQRA 434
Cdd:COG4913   406 ALAEAEAALRDLRRE--LRELEAEIA 429
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 233-457 1.40e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 1.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781   233 EKNRDALSRKLEIEQQEAFMTLEQEQQVKTRTAEQNAKIAAFEAE--------RHREAEQTRILAERQIQETEIEREQAV 304
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEveqleeriAQLSKELTELEAEIEELEERLEEAEEE 776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781   305 RSRkVEAEREVRIKEIEQQQAtEIANQTKSIAIAAKSEQQSQAEA-----RANDALAEAVRAQQNVETTRQTAEADRAKQ 379
Cdd:TIGR02168  777 LAE-AEAEIEELEAQIEQLKE-ELKALREALDELRAELTLLNEEAanlreRLESLERRIAATERRLEDLEEQIEELSEDI 854

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781   380 VALIAAAQDAETQAVELT---VRAKAEKEAAELQAAAIVELAEATRKKGLAEAEAQRALNDAINVLSDEQTSLKFKLALL 456
Cdd:TIGR02168  855 ESLAAEIEELEELIEELEselEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL 934


                   .
gi 489114781   457 Q 457
Cdd:TIGR02168  935 E 935
PTZ00121 PTZ00121
MAEBL; Provisional
 231-423 1.43e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  231 VREKNRDALSRKLEIEQQEAfmtleQEQQVKTRTAEQNAKIAAFEAERHREAEQTRILAERQIQETEIEREQAVRSRKVE 310
Cdd:PTZ00121 1347 AAKAEAEAAADEAEAAEEKA-----EAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAD 1421

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  311 aerEVRIKEIEQQQATEIANQTKSIAIAAKSEQQSQAEARANDALAEAVRAQQNVETTRQTAEADRAKQvaLIAAAQDAE 390
Cdd:PTZ00121 1422 ---EAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE--AKKKAEEAK 1496

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 489114781  391 TQAVELTVRAKAEK------------EAAELQAAAIVELAEATRK 423
Cdd:PTZ00121 1497 KKADEAKKAAEAKKkadeakkaeeakKADEAKKAEEAKKADEAKK 1541
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 247-472 1.53e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.37  E-value: 1.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 247 QQEAFMTLEQE-QQVKTRTAEQNAKIAAFEAERH------REAEQTRILAERQIQETEIEREQAvrsRKVEAEREVRIKE 319
Cdd:COG4942   18 QADAAAEAEAElEQLQQEIAELEKELAALKKEEKallkqlAALERRIAALARRIRALEQELAAL---EAELAELEKEIAE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 320 IEQQQATEIANQTKSIAIAAKSEQQSQAEARAN-DALAEAVRAQQNVettRQTAEADRAKQVALIAAAQDAETQAVELTV 398
Cdd:COG4942   95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSpEDFLDAVRRLQYL---KYLAPARREQAEELRADLAELAALRAELEA 171

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489114781 399 RAKAEKEAAELQAAAIVELAEATRKKGLAEAEAQRALNDAINVLSDEQTSLKFKLALLQSLPAVIEKSVEPMKS 472
Cdd:COG4942  172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
PRK12704 PRK12704
phosphodiesterase; Provisional
 260-448 1.57e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.38  E-value: 1.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 260 VKTRTAEQNAKIAAFEAERHREAEQTRilAERQIQETEIEREQAVRSRKVEAEREVRIKEIEQQQAtEIANQTKSIAIAA 339
Cdd:PRK12704  24 VRKKIAEAKIKEAEEEAKRILEEAKKE--AEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKL-EKRLLQKEENLDR 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 340 KSEQQSQAEARANDALAEAVRAQQNVETTRQTAEADRAKQVAL---IAA--AQDAETQAVElTVRAKAEKEAAELqAAAI 414
Cdd:PRK12704 101 KLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQElerISGltAEEAKEILLE-KVEEEARHEAAVL-IKEI 178

                        170       180       190
                 ....*....|....*....|....*....|....
gi 489114781 415 VELAEATrkkglAEAEAQRALNDAINVLSDEQTS 448
Cdd:PRK12704 179 EEEAKEE-----ADKKAKEILAQAIQRCAADHVA 207
growth_prot_Scy NF041483
polarized growth protein Scy;
263-446 2.22e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 44.43  E-value: 2.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  263 RTAEQNAKIAAFEAERHR-----EAEQTRILAERQIQETEIEREQAVRSRKVEAEREVRIKEIEQQQATEIANQTKSIAI 337
Cdd:NF041483  520 RQAEETLERTRAEAERLRaeaeeQAEEVRAAAERAARELREETERAIAARQAEAAEELTRLHTEAEERLTAAEEALADAR 599

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  338 AAKSEQQSQAEARANDALAEAVRAQQNVEtTRQTAEADRAK-QVALIAAAQDAETQAVELTVRAKAEKEAAELQAAAive 416
Cdd:NF041483  600 AEAERIRREAAEETERLRTEAAERIRTLQ-AQAEQEAERLRtEAAADASAARAEGENVAVRLRSEAAAEAERLKSEA--- 675

                         170       180       190
                  ....*....|....*....|....*....|
gi 489114781  417 LAEATRKKGLAEAEAQRALNDAINVLSDEQ 446
Cdd:NF041483  676 QESADRVRAEAAAAAERVGTEAAEALAAAQ 705
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 230-458 3.23e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.89  E-value: 3.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781   230 AVREKNRDALSRKLEIEQQEAFMTLEQEQqvktrTAEQNAKIAAFEAErHREAEQTRILAERQIQETEIEREQAVRSRKV 309
Cdd:TIGR02168  664 GSAKTNSSILERRREIEELEEKIEELEEK-----IAELEKALAELRKE-LEELEEELEQLRKELEELSRQISALRKDLAR 737

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781   310 EAEREVRIKEIEQQQATEIANQTKSIaiaaksEQQSQAEARANDALAEAVRAQQNVETTRQTAEADRAKQVALIAAAQDA 389
Cdd:TIGR02168  738 LEAEVEQLEERIAQLSKELTELEAEI------EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE 811

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781   390 ETQ----AVELTVRAKAEKEAAELQAAAIVELAEATRKKGLAEAEAQRALND----------AINVLSDEQTSLKFKLAL 455
Cdd:TIGR02168  812 LTLlneeAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEleelieelesELEALLNERASLEEALAL 891


                   ...
gi 489114781   456 LQS 458
Cdd:TIGR02168  892 LRS 894
PRK07735 PRK07735
NADH-quinone oxidoreductase subunit C;
258-454 5.36e-04

NADH-quinone oxidoreductase subunit C;


Pssm-ID: 236081 [Multi-domain]  Cd Length: 430  Bit Score: 42.66  E-value: 5.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 258 QQVKTRTAEQNAKIAAFEAERHREAEQTRILAERQIQETEIEREQAV----RSRKVEAEREVRIKEIEQQQATEIANQTK 333
Cdd:PRK07735   8 EDLKKEAARRAKEEARKRLVAKHGAEISKLEEENREKEKALPKNDDMtieeAKRRAAAAAKAKAAALAKQKREGTEEVTE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 334 SIAIAAKSEQQSQAEARANdALAEAVRAQQNVETTRQTAEADRAKQVALIAAAQDAETQAVELTVRAKAEKEAAELQAAA 413
Cdd:PRK07735  88 EEKAKAKAKAAAAAKAKAA-ALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAK 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 489114781 414 IVELAEATRK-KGLAEAEAQRALNDAINVLSDEQTSLKFKLA 454
Cdd:PRK07735 167 AKAAAAAKAKaAALAKQKAAEAGEGTEEVTEEEKAKAKAKAA 208
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 233-382 5.61e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.80  E-value: 5.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  233 EKNRDALSRKLEIEQQEAFMTLEQEQQVKTRTAEQNAKIAAFEAERHREAEQTRILAER-----QIQETEIEREQAV-RS 306
Cdd:pfam17380 386 ERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERaremeRVRLEEQERQQQVeRL 465

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  307 RKVEAEREVRIKEIE-QQQATEIANQTKSIAIAAKSEQQSQA---EARANDALAEAVRAQQNV---ETTRQTAEADRAKQ 379
Cdd:pfam17380 466 RQQEEERKRKKLELEkEKRDRKRAEEQRRKILEKELEERKQAmieEERKRKLLEKEMEERQKAiyeEERRREAEEERRKQ 545


                  ...
gi 489114781  380 VAL 382
Cdd:pfam17380 546 QEM 548
PRK07735 PRK07735
NADH-quinone oxidoreductase subunit C;
232-432 5.95e-04

NADH-quinone oxidoreductase subunit C;


Pssm-ID: 236081 [Multi-domain]  Cd Length: 430  Bit Score: 42.27  E-value: 5.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 232 REKNRDALSRKLEIEQQEafmtLEQEQQVKTRTAEQN-------AKIAAFEAERHREAEQTRILAERQIQETEIEREQAv 304
Cdd:PRK07735  19 KEEARKRLVAKHGAEISK----LEEENREKEKALPKNddmtieeAKRRAAAAAKAKAAALAKQKREGTEEVTEEEKAKA- 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 305 rSRKVEAEREVRIKEIEQQQATEIANQTKSIAIAAKSEQQSQAEARANDALAEAVRAQQNVETTRQTAEADRAKQVALIA 384
Cdd:PRK07735  94 -KAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAA 172

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 489114781 385 AAQDAETQAVELTVRAKAEKEAAELQAAAIVELAEATRKKGLAEAEAQ 432
Cdd:PRK07735 173 AKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAK 220
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 263-471 6.71e-04

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 42.63  E-value: 6.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 263 RTAEQNAKIAAFEAERHrEAEQTRIlaERQIQETEIEREQAVRSRKVEAEREV-----RIK-------EIEQQQATEIAN 330
Cdd:PRK05035 439 RAIEQEKKKAEEAKARF-EARQARL--EREKAAREARHKKAAEARAAKDKDAVaaalaRVKakkaaatQPIVIKAGARPD 515

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 331 QTKSIAIAAKSEQQSQAEARANDALAEA-----------------VRAQQNVETTRQTAEADRAKQVAL-IA------AA 386
Cdd:PRK05035 516 NSAVIAAREARKAQARARQAEKQAAAAAdpkkaavaaaiarakakKAAQQAANAEAEEEVDPKKAAVAAaIArakakkAA 595

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 387 QDAETQAVELTVRAKAEKEAAelqAAAIVELAEATRKKGLAEAEAQRALNDAINVLSDEQTSLKFKLALLQSLPAVIEKS 466
Cdd:PRK05035 596 QQAASAEPEEQVAEVDPKKAA---VAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEA 672


                 ....*
gi 489114781 467 VEPMK 471
Cdd:PRK05035 673 EDPKK 677
PTZ00121 PTZ00121
MAEBL; Provisional
 203-430 7.54e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 7.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  203 AEGLTKLTQETERRRRERNEVEQDVEVAVREKNRDALSRKLEIEQQEAFMTLEQEQQVKTRTAEQNAKIAAFEAERHREA 282
Cdd:PTZ00121 1380 ADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKA 1459

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  283 EQTRILAE--RQIQETEIEREQAVRSRKVEAEREVRIKEIEQ----QQATEIANQTKSIAIAAKSEQQSQAEARANDALA 356
Cdd:PTZ00121 1460 EEAKKKAEeaKKADEAKKKAEEAKKADEAKKKAEEAKKKADEakkaAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEA 1539

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489114781  357 EAVRAQQNVETTRQTAEADRAKQVALIAAAQDAETQAVELTVRAKAEKEAAELQAAAIVELAEATRKKGLAEAE 430
Cdd:PTZ00121 1540 KKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
growth_prot_Scy NF041483
polarized growth protein Scy;
265-430 1.05e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.12  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  265 AEQNAKIAAFEAERHREAEQTRILAERQIQETEIEREQAVRSRKVEAEREVRIKEIEQQQATEIANQTKSiAIAAKSEQQ 344
Cdd:NF041483  174 AEAEQALAAARAEAERLAEEARQRLGSEAESARAEAEAILRRARKDAERLLNAASTQAQEATDHAEQLRS-STAAESDQA 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  345 SQ--------AEARANDALAEAVRAQQNVETTRQTAEADRAKQVALIAAAQD-----AETQAVELTVRAKAEKEAAELQA 411
Cdd:NF041483  253 RRqaaelsraAEQRMQEAEEALREARAEAEKVVAEAKEAAAKQLASAESANEqrtrtAKEEIARLVGEATKEAEALKAEA 332

                         170
                  ....*....|....*....
gi 489114781  412 AAIVELAEATRKKGLAEAE 430
Cdd:NF041483  333 EQALADARAEAEKLVAEAA 351
PTZ00121 PTZ00121
MAEBL; Provisional
 230-434 1.61e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  230 AVREKNRDALSRKLEIEQQEAFMTLEQEQQVKTRTAEQNAKIAAFEAERHREAEQTRILAErQIQETEiEREQAVRSRKV 309
Cdd:PTZ00121 1453 AEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD-EAKKAE-EAKKADEAKKA 1530

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  310 EAER---EVRIKEiEQQQATEI--ANQTKSIAIAAKSEQQSQAEARANDALAEAVRAQQ------------NVETTRQTA 372
Cdd:PTZ00121 1531 EEAKkadEAKKAE-EKKKADELkkAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaeearieevmklYEEEKKMKA 1609

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489114781  373 EADRAKQVALIAAAQ----DAETQAVELTVRAKAE--KEAAELQAAAIVELAEATRKKGLAEAEAQRA 434
Cdd:PTZ00121 1610 EEAKKAEEAKIKAEElkkaEEEKKKVEQLKKKEAEekKKAEELKKAEEENKIKAAEEAKKAEEDKKKA 1677
PTZ00121 PTZ00121
MAEBL; Provisional
 189-438 1.69e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 1.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  189 QTEKVHFNPN-NAFDAEGLTKLTQETERRRRERNEVEQDVEVAVREKNRDALSRKLEIEQQEAfMTLEQEQQVKTRTAEQ 267
Cdd:PTZ00121 1244 KAEEERNNEEiRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADE-AKKKAEEAKKADEAKK 1322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  268 NAKIAAFEAER-HREAEQTRILAERQIQETEIEREQAVRSRKvEAEREVRIKEIEQQQATEIANQTKSIAIAAKSEQQSQ 346
Cdd:PTZ00121 1323 KAEEAKKKADAaKKKAEEAKKAAEAAKAEAEAAADEAEAAEE-KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAE 1401

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  347 AEARANDALAEAVRAQQNVETTRQTAE----ADRAKQVALIA-AAQDAETQAVELTVRAKAEKEAAELQAA-AIVELAEA 420
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADEAKKKAEekkkADEAKKKAEEAkKADEAKKKAEEAKKAEEAKKKAEEAKKAdEAKKKAEE 1481

                         250
                  ....*....|....*...
gi 489114781  421 TRKKGLAEAEAQRALNDA 438
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKA 1499
PRK12472 PRK12472
hypothetical protein; Provisional
 289-408 1.95e-03

hypothetical protein; Provisional


Pssm-ID: 237110 [Multi-domain]  Cd Length: 508  Bit Score: 41.01  E-value: 1.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 289 AERQIQETEIEREQAVRSRKV--EAEREVR-----IKEIEQQQA---TEIANQTKSIAIAAKSEQQSQAEARANDALAEA 358
Cdd:PRK12472 192 AETLAREAEDAARAADEAKTAaaAAAREAAplkasLRKLERAKAradAELKRADKALAAAKTDEAKARAEERQQKAAQQA 271

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 489114781 359 VRAQQNVETTRQTAEADRAKQVALIAAAQDAETQAVELTVRAKAEKEAAE 408
Cdd:PRK12472 272 AEAATQLDTAKADAEAKRAAAAATKEAAKAAAAKKAETAKAATDAKLALE 321
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 229-431 1.97e-03

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 41.09  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 229 VAVREKNRDALSRKLE-IEQQEAfmtleQEQQVKTRTAEQNAKIAAFEAERHREAEQTRilaERQIQETEIEREQAvRSR 307
Cdd:PRK05035 478 EARAAKDKDAVAAALArVKAKKA-----AATQPIVIKAGARPDNSAVIAAREARKAQAR---ARQAEKQAAAAADP-KKA 548

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 308 KVEAERE-VRIKEIEQQQATEIANQT---KSIAIAA--------KSEQQ-SQAEARANDALAEAVRAQQNVETTRQTAEA 374
Cdd:PRK05035 549 AVAAAIArAKAKKAAQQAANAEAEEEvdpKKAAVAAaiarakakKAAQQaASAEPEEQVAEVDPKKAAVAAAIARAKAKK 628

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489114781 375 DRAKQVALIAAAQDAETQAVELTV-RAKAEKEAAElQAAAIVELAEATRKKGLAEAEA 431
Cdd:PRK05035 629 AEQQANAEPEEPVDPRKAAVAAAIaRAKARKAAQQ-QANAEPEEAEDPKKAAVAAAIA 685
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 233-398 2.35e-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: 40.76  E-value: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  233 EKNRDALSRKlEIEQQEAFMTLEQEQQVKTRTAEQNAKIAAFEAERHREAEQTRILAERQIQETE-IEREQAVRSRKV-- 309
Cdd:pfam05262 195 NFRRDMTDLK-ERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKnLPKPADTSSPKEdk 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  310 ----EAEREVRIKEIEQQQATEIANQTK-SIAIAAKSEQQSQaEARANDALAEAVRAQQNV-ETTRQTAEADRAKQVALI 383
Cdd:pfam05262 274 qvaeNQKREIEKAQIEIKKNDEEALKAKdHKAFDLKQESKAS-EKEAEDKELEAQKKREPVaEDLQKTKPQVEAQPTSLN 352

                         170
                  ....*....|....*
gi 489114781  384 AAAQDAETQAVELTV 398
Cdd:pfam05262 353 EDAIDSSNPVYGLKV 367
PHA00430 PHA00430
tail fiber protein
 300-438 2.38e-03

tail fiber protein


Pssm-ID: 222790 [Multi-domain]  Cd Length: 568  Bit Score: 40.65  E-value: 2.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 300 REQAVRSRKvEAEREVRIKEIEQQQATEIANQTKSIAIAAKSEQQSQAEARANDALAEAVRAQQNVETTRQTAEADRAKQ 379
Cdd:PHA00430 165 RNEANRSRN-EADRARNQAERFNNESGASATNTKQWRSEADGSNSEANRFKGYADSMTSSVEAAKGQAESSSKEANTAGD 243

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489114781 380 VALIAAAQDAETQAVELTvrakaekeaAELQAAAivelaeATRKKGLAEAEAQRALNDA 438
Cdd:PHA00430 244 YATKAAASASAAHASEVN---------AANSATA------AATSANRAKQQADRAKTEA 287
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 84-188 2.39e-03

core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes 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: 259797 [Multi-domain]  Cd Length: 110  Bit Score: 37.73  E-value: 2.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781  84 VDSLITKDRMRVDVVVAFFVRVKPSVEGIATAaqtlgqRTLSPEDLRVLIEDKFVDALRATASQMTMHELQDTRENFVQG 163
Cdd:cd02106    9 VEPVGTADGVPVAVDLVVQFRITDYNALPAFY------LVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEIAKA 82

                         90       100
                 ....*....|....*....|....*
gi 489114781 164 VQNTVAEDLSKNGLELESVSLTNFN 188
Cdd:cd02106   83 VKEDLEEDLENFGVVISDVDITSIE 107
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 353-435 5.91e-03

Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 38.67  E-value: 5.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 353 DALAEAVRAQQNVETTRQTAEADRAKQVALI-----AAAQDAETQAVELTVRAKAEKEAAELQAAAIVELAEATRKKGLa 427
Cdd:COG0330  171 DAMEDRMKAEREREAAILEAEGYREAAIIRAegeaqRAIIEAEAYREAQILRAEGEAEAFRIVAEAYSAAPFVLFYRSL- 249


                 ....*...
gi 489114781 428 eaEAQRAL 435
Cdd:COG0330  250 --EALEEV 255
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 237-349 7.35e-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: 38.43  E-value: 7.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489114781 237 DALSRKLEIEQQEAFMTL--EQEQQVKTRTAEQNAKIAAFEAErhREAEQTRILAERQIQETEIEReqavrsrkveaere 314
Cdd:cd03406  162 EAIRRNYEAMEAEKTKLLiaEQHQKVVEKEAETERKRAVIEAE--KDAEVAKIQMQQKIMEKEAEK-------------- 225

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489114781 315 vRIKEIEQQqaTEIANQtKSIAIAAKSEQQSQAEA 349
Cdd:cd03406  226 -KISEIEDE--MHLARE-KARADAEYYRALREAEA 256
 
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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