|
Name |
Accession |
Description |
Interval |
E-value |
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
13-535 |
7.58e-89 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 280.61 E-value: 7.58e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 13 FTAIIAVCILFIIGIIFARLYRRASAEQAFVRTG-LGGQKVVMSGGAIVMPIFHEIIPINMNTLKLEVSRStiDSLITKD 91
Cdd:COG2268 8 IIIGVIVVVLLLLLIILARFYRKVPPNEALVITGrGGGYKVVTGGGAFVLPVLHRAERMSLSTMTIEVERT--EGLITKD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 92 RMRVDVVVAFFVRVKPSVEGIATAAQTLGQRTlsPEDLRMLVEDKFVDALRATAAQMTMHELQDTRENFVQGVQNTVAED 171
Cdd:COG2268 86 GIRVDVDAVFYVKVNSDPEDIANAAERFLGRD--PEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 172 LSKNGLELESVSLTNFNQtskehfnPNNAFDAEGLTKLTQETERRRRERNEVEQDVEVAVREKNRdalsrkleieqQEAF 251
Cdd:COG2268 164 LAKNGLELESVAITDLED-------ENNYLDALGRRKIAEIIRDARIAEAEAERETEIAIAQANR-----------EAEE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 252 MTLEQEQQVKTRT-AEQNAKIAAFEAERRREAEQTRILAERQIQETEIDREQAVrsrkveaerevrikeieqQQVTEIAN 330
Cdd:COG2268 226 AELEQEREIETARiAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAEREV------------------QRQLEIAE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 331 QTKSIAIAAKSEQQSQAEARAnlalaeavsaqqnvettrqtaeadrakqvaliaaaqdaetkavELTVRAKAEKEAAEMQ 410
Cdd:COG2268 288 REREIELQEKEAEREEAELEA-------------------------------------------DVRKPAEAEKQAAEAE 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 411 AAAIvelAEATRKKGLAEAEAQRALNDAINVLSDEQtslkFKLALLQALPAVIEKSVEPMKSIDGIKIIQvdglnrggta 490
Cdd:COG2268 325 AEAE---AEAIRAKGLAEAEGKRALAEAWNKLGDAA----ILLMLIEKLPEIAEAAAKPLEKIDKITIID---------- 387
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 15833187 491 gDANTGNVGGGNLAEQAlsaalsyrtqAPLIDSLLNEIGVSGGSL 535
Cdd:COG2268 388 -GGNGGNGAGSAVAEAL----------APLLESLLEETGLDLPGL 421
|
|
| Flot |
pfam15975 |
Flotillin; Flotillin is a family of lipid-membrane-associated proteins found in bacteria, ... |
406-527 |
5.26e-40 |
|
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: 141.31 E-value: 5.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 406 AAEMQAAAIVELAEATRKKGLAEAEAQRALNDAINVLSDEQTSLKFKLALLQALPAVIEKSVEPMKSIDGIKIIQVDGLN 485
Cdd:pfam15975 1 EAEAEADAIKLRAEAKRKKALAEAEGIRALNEAENALSDEQIALQVKLALLEALPEIIAESVKPLEKIDGIKILQVDGLG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 15833187 486 rGGTAGDANTGNVGGGNLAEQALSAALSYRTQAPLIDSLLNE 527
Cdd:pfam15975 81 -GGAAGGGGGGGGGGGSLAEQAVDSALGYRAQAPLIDSLLKE 121
|
|
| SPFH_flotillin |
cd03399 |
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ... |
59-209 |
3.28e-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: 129.16 E-value: 3.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 59 IVMPIFHEIIPINMNTLKLEVSRSTIdslITKDRMRVDVVVAFFVRVKPSVEGIATAA-QTLGQRTlspEDLRMLVEDKF 137
Cdd:cd03399 1 FVIPFLQRVQRLSLETMTIDVKVEEV---LTKDGIPVDVTAVAQVKVGSDPEEIAAAAeRFLGKST---EEIRELVKETL 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15833187 138 VDALRATAAQMTMHELQDTRENFVQGVQNTVAEDLSKNGLELESVSLTNFNQTSkEHFNPNNAFDAEGLTKL 209
Cdd:cd03399 75 EGHLRAIVGTMTVEEIYQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDISDDN-GYLESLGRKQAAEVKKD 145
|
|
| PHB |
smart00244 |
prohibitin homologues; prohibitin homologues |
30-196 |
1.88e-15 |
|
prohibitin homologues; prohibitin homologues
Pssm-ID: 214581 [Multi-domain] Cd Length: 160 Bit Score: 73.85 E-value: 1.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 30 ARLYRRASAEQAFVRTGLGGQKVVMSGGAIVMPIFHEIIPINMNTLKLEVSRSTIdslITKDRmrVDVVVAFFVRVKpSV 109
Cdd:smart00244 1 AAIKVVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQET---ITKDN--VKVSVDAVVYYR-VL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 110 EGIATAAQTLGQRTlspEDLRMLVEDkfvdALRATAAQMTMHELQ-DTRENFVQGVQNTVAEDLSKNGLELESVSLTN-- 186
Cdd:smart00244 75 DPLRAVYRVLDADY---AVIEQLAQT----TLRSVIGKRTLDELLtDQREKISENIREELNEAAEAWGIKVEDVEIKDir 147
|
170
....*....|
gi 15833187 187 FNQTSKEHFN 196
Cdd:smart00244 148 LPEEIKEAME 157
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
226-459 |
9.76e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 77.67 E-value: 9.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 226 DVEVAVREKNRDALSRKLEIEQQEAFMTLEQEQQVKTRTAEQNAKIAAFEAERRREAEQTRILAERQIQETEIDREQAVR 305
Cdd:COG1196 266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 306 SRKVEAEREVRIKEIEQQQVTEIANQTKSIAIAAKSEQQSQAEARANLALAEAVSAQQNVETTRQTAEADRAKQVALIAA 385
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15833187 386 AQDAETKAVELTVRAKAEKEAAEMQAAAIVELAEATRKKGLAEAEAQRALNDAINVLSDEQTSLKFKLALLQAL 459
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
|
| Band_7 |
pfam01145 |
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ... |
40-188 |
4.34e-14 |
|
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: 70.43 E-value: 4.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 40 QAFVRTGLGG-QKVVMSGGAIVMPIFHEIIPINMNTLKLEVSRSTIdslITKDRMRVDVVVAFFVRVKPsvegiaTAAQT 118
Cdd:pfam01145 7 EVGVVTRFGKlSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTV---LTKDGVPVNVDVTVIYRVNP------DDPPK 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 119 LGQRTLSPEDLRMLVEDKFVDALRATAAQMTMHELQDTRENFVQGVQNTVAEDLSKNGLELESVSLTNFN 188
Cdd:pfam01145 78 LVQNVFGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDID 147
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
232-459 |
1.07e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 232 REKNRDALSRKLEIEQQEAFMTLEQEQQVKTRTAEQNAKIAAFEAERRREAEQTRILAERQIQETEIDREQAVRSRKVEA 311
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 312 EREVRIKEIEQQQVTEIANQTKSIAIAAKSEQQSQAEARANLALAEAVSAQQNVETTR----QTAEADRAKQVALIAAAQ 387
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELaeaeEELEELAEELLEALRAAA 396
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15833187 388 DAETKAVELTVRAKAEKEAAEMQAAAIVELAEATRKKGLAEAEAQRALNDAINVLSDEQTSLKFKLALLQAL 459
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
255-438 |
1.84e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 59.82 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 255 EQEQQVKTRTAEQNAKiaaFEAERRREAEQTRILAERQ-IQETEIDREQAVRSRKvEAEREVRIKEIEQQQVTEIANQTK 333
Cdd:PRK09510 67 QQQQQKSAKRAEEQRK---KKEQQQAEELQQKQAAEQErLKQLEKERLAAQEQKK-QAEEAAKQAALKQKQAEEAAAKAA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 334 SIAIAAKSEQQSQAEARANLALAEAVSAQQNVETTRQTAEAD-RAKQVALIAAAQDAETKAvELTVRAKAEKEAAEMQAA 412
Cdd:PRK09510 143 AAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKkKAEAEAAAKAAAEAKKKA-EAEAKKKAAAEAKKKAAA 221
|
170 180
....*....|....*....|....*.
gi 15833187 413 AIVELAEATRKKGLAEAEAQRALNDA 438
Cdd:PRK09510 222 EAKAAAAKAAAEAKAAAEKAAAAKAA 247
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
245-465 |
2.40e-09 |
|
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: 59.09 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 245 IEQQEAFMTLEQEQQVKTRTAEQNAKIAAFEAERRREAEQTRILAERQIQETEIDREQAVRSRKVEAEREvRIKEIEQQQ 324
Cdd:TIGR02794 43 VDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAK-QAEEKQKQA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 325 VTEIANQTKSIAIAAKSEQQSQAEARANlALAEAVSAQQNVETTRQTAEADRAKQVALIAAAQDAETKAVELTVRAKAE- 403
Cdd:TIGR02794 122 EEAKAKQAAEAKAKAEAEAERKAKEEAA-KQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEa 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15833187 404 -KEAAEMQAAAIVELAEATRKKGLAEAEAQRALNDAINVLSDEQTSLKFKLALLQALPAVIEK 465
Cdd:TIGR02794 201 aKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDK 263
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
231-434 |
1.51e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 231 VREKNRDALSRKLEIEQ--QEAFMTLEQEQQVKTRTAEQNAKI-AAFEAERRREAEQTR-------ILAERQIQETEIDR 300
Cdd:PTZ00121 1160 AEDARKAEEARKAEDAKkaEAARKAEEVRKAEELRKAEDARKAeAARKAEEERKAEEARkaedakkAEAVKKAEEAKKDA 1239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 301 EQAVRSRKVEAEREVRikEIEQQQVTEIANQTKSIaiaaKSEQQSQAEaraNLALAEAVSAQQNVETTRQTAEADRAKQV 380
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIR--KFEEARMAHFARRQAAI----KAEEARKAD---ELKKAEEKKKADEAKKAEEKKKADEAKKK 1310
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15833187 381 ALIA-AAQDAETKAVELTVRAKA-EKEAAEMQAAAIVELAEATRKKGLAEAEAQRA 434
Cdd:PTZ00121 1311 AEEAkKADEAKKKAEEAKKKADAaKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
|
| SPFH_prohibitin |
cd03401 |
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ... |
43-290 |
3.42e-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: 53.67 E-value: 3.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 43 VRTGLGGQKVVMSGGA-IVMPIFHEIIPINMNTLKLEVSRSTIdsliTKDRMRVDVVVAffVRVKPSVEGIATAAQTLGq 121
Cdd:cd03401 13 FRRGKGVKDEVLGEGLhFKIPWIQVVIIYDVRTQPREITLTVL----SKDGQTVNIDLS--VLYRPDPEKLPELYQNLG- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 122 rtlsPEDLRMLVEDKFVDALRATAAQMTMHELQDTRENFVQGVQNTVAEDLSKNGLELESVSLTNFNqtskehfnpnnaF 201
Cdd:cd03401 86 ----PDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNID------------F 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 202 DAEgltkltqeterrrrerneveqdVEVAVREKNrdalsrkleieqqeafmtleqeqqvktrTAEQNAKIAAFEAER-RR 280
Cdd:cd03401 150 PDE----------------------YEKAIEAKQ----------------------------VAEQEAERAKFELEKaEQ 179
|
250
....*....|
gi 15833187 281 EAEQTRILAE 290
Cdd:cd03401 180 EAERKVIEAE 189
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
265-438 |
3.63e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 55.58 E-value: 3.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 265 AEQNAKIAAFEAERRREAEQTRILAERQIQETEidreqavrsRKVEAEREvRIKEIEQQQVTEIANQTKSIAIAAKSEQQ 344
Cdd:PRK09510 61 VEQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQ---------QKQAAEQE-RLKQLEKERLAAQEQKKQAEEAAKQAALK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 345 SQAEARANLALAEAVSAQQNVETTRQTAEADRAKQVALIAAAQDAETKAvELTVRAKAEKEAAEMQAAAIVELAEATRKK 424
Cdd:PRK09510 131 QKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKA-AAEAKKKAEAEAAAKAAAEAKKKAEAEAKK 209
|
170
....*....|....
gi 15833187 425 GLAEAEAQRALNDA 438
Cdd:PRK09510 210 KAAAEAKKKAAAEA 223
|
|
| HflC |
COG0330 |
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
15-313 |
1.84e-07 |
|
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440099 [Multi-domain] Cd Length: 279 Bit Score: 52.92 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 15 AIIAVCILFIIGIIFARLYRRASAEQAFVRTGLGG-QKVVMSGGAIVMPIFHEIIPINMNTLKLEVSRSTIdslITKDRm 93
Cdd:COG0330 3 LILLLILLVLVLVLLFSSVYIVPQGERGVVLRFGKyVRTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEV---LTKDN- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 94 rVDVVVAFFVRVKpsVEGIATAAQTLgqrtlspEDLRMLVEDKFVDALRATAAQMTMHELQDT-RENFVQGVQNTVAEDL 172
Cdd:COG0330 79 -NIVDVDAVVQYR--ITDPAKFLYNV-------ENAEEALRQLAESALREVIGKMTLDEVLSTgRDEINAEIREELQEAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 173 SKNGLELESVSLTNfnqtskehFNPNnafdaegltkltqeterrrrerneveQDVEVAVREKNRdalsrkleieqqeafm 252
Cdd:COG0330 149 DPYGIEVVDVEIKD--------IDPP--------------------------EEVQDAMEDRMK---------------- 178
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15833187 253 tleqeqqvktrtAEQNAKIAAFEAERRREAEQTRILAERQ--IQETEIDREQAVRSRKVEAER 313
Cdd:COG0330 179 ------------AEREREAAILEAEGYREAAIIRAEGEAQraIIEAEAYREAQILRAEGEAEA 229
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
230-433 |
2.07e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 230 AVREKNRDALSRKLEIEQ-QEAFMTLEQEQQVKTRTAEQ--NAKIAAFEAERRREAEQTRILAE-RQIQETeidrEQAVR 305
Cdd:PTZ00121 1075 SYKDFDFDAKEDNRADEAtEEAFGKAEEAKKTETGKAEEarKAEEAKKKAEDARKAEEARKAEDaRKAEEA----RKAED 1150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 306 SRKVEAERevRIKEIEQQQVTEIANQTKSIAIAAKSEQQSQAEARANLALAEAVSAQQNVETTRQTAEADRAKQVALIAA 385
Cdd:PTZ00121 1151 AKRVEIAR--KAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEA 1228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15833187 386 AQDAE--TKAVELTVRAKAEKEAAEMQAAAIVELAEATRKKGLAEAEAQR 433
Cdd:PTZ00121 1229 VKKAEeaKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR 1278
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
225-438 |
2.45e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 225 QDVEVAVREKNRDALSRKLEIEQ-QEAFMTLEQEQQVKTRTAEQNAKIAAFEAERRREAEQTRILAERQIQETEIDREQA 303
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEElAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 304 VRSRKVEAEREVRIKEIEQQQVTEIANQTKSIAiaakSEQQSQAEARANLALAEAV-SAQQNVETTRQTAEADRAKQVAL 382
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEALLELLAELLEEAA----LLEAALAELLEELAEAAARlLLLLEAEADYEGFLEGVKAALLL 516
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15833187 383 IAAAQDAETKAVELTVRAKAEKEAAEMQAAAIVELAEATRKKGLAEAEAQRALNDA 438
Cdd:COG1196 517 AGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAG 572
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
231-434 |
3.67e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 231 VREKNRDALSRKLEIEQQEAfmtleQEQQVKTRTAEQNAKIAAFEAERRREAEQTRILAERQIQETEIDREQAVRSRKVE 310
Cdd:PTZ00121 1347 AAKAEAEAAADEAEAAEEKA-----EAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAD 1421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 311 aerEVRIKEIEQQQVTEIANQTKSIAIAAKSEQQSQAEARANLALAEAVSAQQNVETTRQTAEADRAKQvaLIAAAQDAE 390
Cdd:PTZ00121 1422 ---EAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE--AKKKAEEAK 1496
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15833187 391 TKAVELTVRAKAEKEAAEMQAAAIVELAEATRKkglAEaEAQRA 434
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKADEAKKAEEAKKADEAKK---AE-EAKKA 1536
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
231-424 |
9.73e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 9.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 231 VREKNRDAlsRKLEIEQQEAfmtlEQEQQVKTRTAEQNAKIAAFEAERRREAEQTRILAERQiqeteiDREQAVRSRKVE 310
Cdd:PTZ00121 1235 AKKDAEEA--KKAEEERNNE----EIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKK------KADEAKKAEEKK 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 311 AEREVRIKEIEQQQVTEI---ANQTKSIAIAAKSEQQsQAEARANLALAEAVSAQQNVETTRQTAEADRAKQVALIAAAQ 387
Cdd:PTZ00121 1303 KADEAKKKAEEAKKADEAkkkAEEAKKKADAAKKKAE-EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD 1381
|
170 180 190
....*....|....*....|....*....|....*...
gi 15833187 388 DAETKAVELTVRAKAEKEAAEMQAAAI-VELAEATRKK 424
Cdd:PTZ00121 1382 AAKKKAEEKKKADEAKKKAEEDKKKADeLKKAAAAKKK 1419
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
254-432 |
1.19e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 51.11 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 254 LEQEQQVKTRTAEQNAKIAAFEAERRR--EAEQTRILAERQIQ----ETEIDREQAVRSRKVEAeREVRIKEIEQQQVTE 327
Cdd:pfam15709 328 REQEKASRDRLRAERAEMRRLEVERKRreQEEQRRLQQEQLERaekmREELELEQQRRFEEIRL-RKQRLEEERQRQEEE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 328 IANQTKSIAIAAKSEQQSQAEARANlaLAEAVSAQQNVETTRQTAEADRAKQVALIAAAQD------AETKAVELTVRAK 401
Cdd:pfam15709 407 ERKQRLQLQAAQERARQQQEEFRRK--LQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQkrlmemAEEERLEYQRQKQ 484
|
170 180 190
....*....|....*....|....*....|.
gi 15833187 402 AEKEAAEMQAAAIVELAEATRKKGLAEAEAQ 432
Cdd:pfam15709 485 EAEEKARLEAEERRQKEEEAARLALEEAMKQ 515
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
230-468 |
1.33e-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: 51.60 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 230 AVREKNRDALSRKLEIEQQEAFMTLEQEQqvktrTAEQNAKIAAFEAERRREAEQTRILAERQIQETEIDREQAVRSRKV 309
Cdd:TIGR02168 664 GSAKTNSSILERRREIEELEEKIEELEEK-----IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 310 EAEREVRIKEIEQQQVtEIANQTKSIAIAAKSEQQSQAEARAnlALAEAVSAQQNVETTRQTAEADRAKQVALIAAAQDA 389
Cdd:TIGR02168 739 EAEVEQLEERIAQLSK-ELTELEAEIEELEERLEEAEEELAE--AEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 390 ETKAVELTVRAKAEKEAAEMQAAAIVELAEATRKKGLAEAEAQRALND---AINVLSDEQTSLKFKLALLQALPAVIEKS 466
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEleeLIEELESELEALLNERASLEEALALLRSE 895
|
..
gi 15833187 467 VE 468
Cdd:TIGR02168 896 LE 897
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
203-445 |
1.75e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 203 AEGLTKLTQETERRRRERNEVEQDVEVAVR-EKNRDALSRKLEIEQQ------EAFMTLEQEQQVKTRTAEQNAKIAAFE 275
Cdd:PTZ00121 1542 AEEKKKADELKKAEELKKAEEKKKAEEAKKaEEDKNMALRKAEEAKKaeeariEEVMKLYEEEKKMKAEEAKKAEEAKIK 1621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 276 AERRREAEQTRILAERQIQETEIDREQAVRSRKVEAEREVRIKEIEQQqvteiANQTKSIAIAAKSEQQSqaEARANLAL 355
Cdd:PTZ00121 1622 AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK-----AEEDKKKAEEAKKAEED--EKKAAEAL 1694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 356 AEAVSAQQNVETTRQTAEADRAKQVALIAAAQDAETKAVELTVRAKAEKEAAEMQAAAIVELAEATRKKGLAEAEAQRAL 435
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIR 1774
|
250
....*....|
gi 15833187 436 NDAINVLSDE 445
Cdd:PTZ00121 1775 KEKEAVIEEE 1784
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
275-468 |
2.06e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 275 EAERRREAEQTR------ILAE--RQIQETEIDREQAVRSRKVEAEREVRIKEIEQQQVTEIANQTKSIAIAAKSEQQSQ 346
Cdd:COG1196 176 EAERKLEATEENlerledILGEleRQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 347 AEARANLALAEAVSAQQNVETTRQTAEADRAKQVALIAAAQDAETKAvELTVRAKAEKEAAEMQAAAIVELAEATRKKGL 426
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ-DIARLEERRRELEERLEELEEELAELEEELEE 334
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15833187 427 AEAEAQRALNDAINVLSDEQTSLKFKLALLQALPAVIEKSVE 468
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
244-433 |
2.17e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 50.51 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 244 EIEQQEAFMTLE-----QEQQVKTRTAEQNAKIAafEAERRREAE---QTRILAERQIQETEIDREQAvRSRKVEAEREv 315
Cdd:pfam17380 286 ERQQQEKFEKMEqerlrQEKEEKAREVERRRKLE--EAEKARQAEmdrQAAIYAEQERMAMERERELE-RIRQEERKRE- 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 316 rIKEIEQQQVTEIANQTKSIAIAAKSEQQSQAEARANLalaEAVSAQQNVETTRQTAEADRAKQVALIAAAQDaetKAVE 395
Cdd:pfam17380 362 -LERIRQEEIAMEISRMRELERLQMERQQKNERVRQEL---EAARKVKILEEERQRKIQQQKVEMEQIRAEQE---EARQ 434
|
170 180 190
....*....|....*....|....*....|....*...
gi 15833187 396 LTVRAKAEKEAAEMQAAAIVELAEATRKKGLAEAEAQR 433
Cdd:pfam17380 435 REVRRLEEERAREMERVRLEEQERQQQVERLRQQEEER 472
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
255-459 |
4.34e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 255 EQEQQVKT-----RTAEQNAKIAAFEAERRREAEQTRILAERQIQETEIDREQAVRSRKVEAEREVRIKEIEQQQV-TEI 328
Cdd:COG1196 197 ELERQLEPlerqaEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELrLEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 329 ANQTKSI-----AIAAKSEQQSQAEARANLALAEAVSAQQNVETTRQTAEADRAKQVALIAAAQDAETKAVELTVRAKAE 403
Cdd:COG1196 277 EELELELeeaqaEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15833187 404 KEAAEMQAAAIVELAEATRKKGLAEAEAQRALNDAINVLSDEQTSLKFKLALLQAL 459
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
232-428 |
1.19e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.88 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 232 REKNRDALSRKLEIEQQEAfmtLEQEQQvktRTAEQNAKIAAFEAERRREAEQTRILAERQIQETEIDREQAVrSRKVEA 311
Cdd:PRK09510 93 QQKQAAEQERLKQLEKERL---AAQEQK---KQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAA-AKKAAA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 312 EREVRikeieqqqvteianqtksiaiaAKSEQQSQAEARANlALAEAVSAQQNVETTRQTAEADrAKQVALIAAAQDAET 391
Cdd:PRK09510 166 EAKKK----------------------AEAEAAKKAAAEAK-KKAEAEAAAKAAAEAKKKAEAE-AKKKAAAEAKKKAAA 221
|
170 180 190
....*....|....*....|....*....|....*..
gi 15833187 392 KAVELTVRAKAEKEAAEMQAAAIVELAEATRKKGLAE 428
Cdd:PRK09510 222 EAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
303-438 |
6.36e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 45.63 E-value: 6.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 303 AVRSRkveAEREVRikeiEQQQVTEIANQTKSIAIAAKSEQQS---------QAEARANLALAEAVSAQQNVETTRQTAE 373
Cdd:PRK12472 187 AAPAR---AETLAR----EAEDAARAADEAKTAAAAAAREAAPlkaslrkleRAKARADAELKRADKALAAAKTDEAKAR 259
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15833187 374 ADRAKQvaliAAAQDAETKAVELTVrAKAEKEAAEMQAAAIVELAEATRKKglaEAEAQRALNDA 438
Cdd:PRK12472 260 AEERQQ----KAAQQAAEAATQLDT-AKADAEAKRAAAAATKEAAKAAAAK---KAETAKAATDA 316
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
269-454 |
7.17e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 7.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 269 AKIAAFEAERRReaeqtrilAERQIQETEIDREQAVRSRKVEAEREVRIKEIEQQQVTEIANQTKSIAIAAKSEQQSQAE 348
Cdd:COG4913 610 AKLAALEAELAE--------LEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLD 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 349 ArANLALAEAVSAQQNVETTRQTAEADRAKQVALIAAAQDAETKAVELTVRAKAEKEAAEMQAAAIVELAEATRKKGLAE 428
Cdd:COG4913 682 A-SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALG 760
|
170 180
....*....|....*....|....*.
gi 15833187 429 AEAQRALNDAINVLSDEQTSLKFKLA 454
Cdd:COG4913 761 DAVERELRENLEERIDALRARLNRAE 786
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
255-524 |
9.21e-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: 45.43 E-value: 9.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 255 EQEQQVKTRTAEQNAKIAAFEAERRREAEQTRILaERQIQETEIDREQAVRSRKVEAEREVRIKEIEQQQVTEIANQtkS 334
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQKQILRERLANL-ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESL--E 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 335 IAIAAKSEQQSQAEARANLALAEAVSAQQNVETTRQTAEADRAKQVALIAAAQDAETKAVELTVRAKAEKEAAEMQAAAI 414
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 415 VELAEATRKKGLAEAEAQRA--------LNDAINVLSDEQTSLKFKLALLQALPAVIEKSVEPMKSI-DGIKIIQVDGLN 485
Cdd:TIGR02168 438 LQAELEELEEELEELQEELErleealeeLREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFsEGVKALLKNQSG 517
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 15833187 486 RGGTAGDANTG-NVGGGnlAEQALSAALSYRTQAPLIDSL 524
Cdd:TIGR02168 518 LSGILGVLSELiSVDEG--YEAAIEAALGGRLQAVVVENL 555
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
227-458 |
9.53e-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: 45.43 E-value: 9.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 227 VEVAVREKNRDALSRKLEIEQQEAFMTL-EQEQQVK-----TRTAEQNAKIAAFEAERRREAEQTRILaERQIQETEIDR 300
Cdd:TIGR02168 191 LEDILNELERQLKSLERQAEKAERYKELkAELRELElallvLRLEELREELEELQEELKEAEEELEEL-TAELQELEEKL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 301 EQaVRSRKVEAEREVRIKEIEQQQVT-EIANQTKSIAIAAKSEQQSQAE-ARANLALAEAVSAQQNVettrQTAEADRAK 378
Cdd:TIGR02168 270 EE-LRLEVSELEEEIEELQKELYALAnEISRLEQQKQILRERLANLERQlEELEAQLEELESKLDEL----AEELAELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 379 QVALIAAAQDAETKAVEltvRAKAEKEAAEMQAAAIVELAEATRKKgLAEAEAQRALNDA-INVLSDEQTSLKFKLALLQ 457
Cdd:TIGR02168 345 KLEELKEELESLEAELE---ELEAELEELESRLEELEEQLETLRSK-VAQLELQIASLNNeIERLEARLERLEDRRERLQ 420
|
.
gi 15833187 458 A 458
Cdd:TIGR02168 421 Q 421
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
232-432 |
1.02e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 44.97 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 232 REKNRDALSRKLEIEQQEafmtLEQEQQVKTRTAEQNAKIAAFEAERRREAEQTRILAERQIQE-------TEIDREQAv 304
Cdd:PRK07735 19 KEEARKRLVAKHGAEISK----LEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKregteevTEEEKAKA- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 305 rSRKVEAEREVRIKEIEQQQVTEIANQTKSIAIAAKSEQQSQAEARANLALAEAVSAQQNVETTRQTAEADRAKQVALIA 384
Cdd:PRK07735 94 -KAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15833187 385 AAQDAETKAVELTVRAKAEKEAAEMQAAAIVELAEATRKKGLAEAEAQ 432
Cdd:PRK07735 173 AKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAK 220
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
233-458 |
1.87e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 233 EKNRDALSRKLEIEQQEAFMTLEQEQQVKTRTAEQNAKIAAFEAERRREAEQTRIL------AERQIQETEIDREQAVRS 306
Cdd:TIGR02168 697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLskelteLEAEIEELEERLEEAEEE 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 307 RK-VEAEREVRIKEIEQQQvtEIANQTKSIAIAAKSEQQSQAEARANLALAEAVSAQQNVETTRQ---------TAEADR 376
Cdd:TIGR02168 777 LAeAEAEIEELEAQIEQLK--EELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRledleeqieELSEDI 854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 377 AKQVALIAAAQDAETKAVELTVRAKAEKEAAEMQAAAIVELAEATRKKGLAEAEAQRALNDAINVLSDEQTSLKFKLALL 456
Cdd:TIGR02168 855 ESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL 934
|
..
gi 15833187 457 QA 458
Cdd:TIGR02168 935 EV 936
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
225-424 |
2.29e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 44.24 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 225 QDVEVaVREKNRDALSR--KLEIEqqeaFMTLEQEQQvktrtaeqnakiAAFEAERRREAEQTRIlaERQIQETeidreq 302
Cdd:PTZ00491 636 QSVEP-VDERTRDSLQKsvQLAIE----ITTKSQEAA------------ARHQAELLEQEARGRL--ERQKMHD------ 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 303 avrsrKVEAEREvRIKEIEQQqvteianqTKSIAIAAKSEQQSQAEARANLALAEavsAQQNVETTRQTAEADRakqval 382
Cdd:PTZ00491 691 -----KAKAEEQ-RTKLLELQ--------AESAAVESSGQSRAEALAEAEARLIE---AEAEVEQAELRAKALR------ 747
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15833187 383 IAAAQDAETKAVELTVRAKAEKEAAEMQAAAIVELAEATRKK 424
Cdd:PTZ00491 748 IEAEAELEKLRKRQELELEYEQAQNELEIAKAKELADIEATK 789
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
233-401 |
2.31e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 233 EKNRDALSRKLEIEQQEAFMTLEQEQQVKTRtAEQNAKIAAFE---AERRREAEQTRILAERQIQETEIDREQAVRSRKV 309
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAEEENKIK-AAEEAKKAEEDkkkAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK 1710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 310 EAErevRIKEIEQQQVTEIANQTKSIAIAAKSEQQSQAEARANLALAEAVSAQQNVETTRQTAEADRAKQVALIAAAQDA 389
Cdd:PTZ00121 1711 EAE---EKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
|
170
....*....|..
gi 15833187 390 ETKAVELTVRAK 401
Cdd:PTZ00121 1788 EDEKRRMEVDKK 1799
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
230-477 |
2.72e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 230 AVREKNRDALSRKLEIEQQEAFMTLEQEQQVKTRTAEQNAKIAAFEAERRREAEQTRILAERQIQETEIDREQAVRSRKV 309
Cdd:PTZ00121 1361 AAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKA 1440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 310 EAER---EVRIKEIEQQQVTEIANQTKSIAIAAKSEQQSQAEARANLALAEAVSAQQNVETTRQTAEadrAKQVALIAAA 386
Cdd:PTZ00121 1441 EEAKkadEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAE---AKKKADEAKK 1517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 387 QDAETKAVELTvRAKAEKEAAEMQAAAIVELAEATRK-KGLAEAEAQRALNDAINVLSDEQTSLKFKLALLQALPAVIEK 465
Cdd:PTZ00121 1518 AEEAKKADEAK-KAEEAKKADEAKKAEEKKKADELKKaEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEE 1596
|
250
....*....|..
gi 15833187 466 SVEPMKSIDGIK 477
Cdd:PTZ00121 1597 VMKLYEEEKKMK 1608
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
247-469 |
2.91e-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: 43.21 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 247 QQEAFMTLEQE-QQVKTRTAEQNAKIAAFEAERR------REAEQTRILAERQIQETEidrEQAVRSRKVEAEREVRIKE 319
Cdd:COG4942 18 QADAAAEAEAElEQLQQEIAELEKELAALKKEEKallkqlAALERRIAALARRIRALE---QELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 320 IEQQQVTEIANQTKSIAIAAKSEQQSQAEARanLALAEAVSAQQNVETTRQTAEADRAKQVALIAAAQDAETKAVELTVR 399
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALL--LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15833187 400 AKAEKEAAEMQAAAIVEL--AEATRKKGLAEAEAQR-ALNDAINVLSDEQTSLKFKLALLQALPAVIEKSVEP 469
Cdd:COG4942 173 RAELEALLAELEEERAALeaLKAERQKLLARLEKELaELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
233-432 |
3.11e-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: 43.57 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 233 EKNRDALSRKLEIEQQEAFMTLEQEQQVKTRTAEQNAKIAAFEAERRREAEQTRILAER-----QIQETEIDREQAV-RS 306
Cdd:pfam17380 386 ERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERaremeRVRLEEQERQQQVeRL 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 307 RKVEAEREVRIKEIEQQQVTE-IANQTKSIAIAAKSEQQSQA---EARANLALAEAVSAQQNV---ETTRQTAEADRAKQ 379
Cdd:pfam17380 466 RQQEEERKRKKLELEKEKRDRkRAEEQRRKILEKELEERKQAmieEERKRKLLEKEMEERQKAiyeEERRREAEEERRKQ 545
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15833187 380 VALiaaaqdAETKAVELTVRAKAEK----EAAEMQAAAIVELAEATRKKGLAEAEAQ 432
Cdd:pfam17380 546 QEM------EERRRIQEQMRKATEErsrlEAMEREREMMRQIVESEKARAEYEATTP 596
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
260-448 |
3.52e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 260 VKTRTAEQNAKIAAFEAER-----RREAEQTRILAERQIQEtEIDReqavrsRKVEAEREVRIKEIEQQQVtEIANQTKS 334
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKRileeaKKEAEAIKKEALLEAKE-EIHK------LRNEFEKELRERRNELQKL-EKRLLQKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 335 IAIAAKSEQQSQAEARANLALAEAVSAQQNVETTRQTAEADRAKQVAL---IAAAQDAETKAVEL-TVRAKAEKEAAEMq 410
Cdd:PRK12704 96 ENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQElerISGLTAEEAKEILLeKVEEEARHEAAVL- 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 15833187 411 AAAIVELAEATrkkglAEAEAQRALNDAINVLSDEQTS 448
Cdd:PRK12704 175 IKEIEEEAKEE-----ADKKAKEILAQAIQRCAADHVA 207
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
229-431 |
5.53e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 42.63 E-value: 5.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 229 VAVREKNRDALSRKLEiEQQEAFMTLEQEQQVKTRTAEQNAKIAAFEAERRREAEQTRilAERQIQETEIDREQAV---- 304
Cdd:PRK05035 478 EARAAKDKDAVAAALA-RVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQ--AEKQAAAAADPKKAAVaaai 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 305 ---RSRKVEAEREVRIKEIEQQQVTEIANQTKSIAIAAKSEQQsQAEARANLALAEAVSAQQNVETTRQTAEADRAKQVA 381
Cdd:PRK05035 555 araKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQ-AASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQA 633
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15833187 382 LIAAAQ--DAETKAVELTV-RAKAEKEAAEmQAAAIVELAEATRKKGLAEAEA 431
Cdd:PRK05035 634 NAEPEEpvDPRKAAVAAAIaRAKARKAAQQ-QANAEPEEAEDPKKAAVAAAIA 685
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
231-451 |
5.55e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 5.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 231 VREKNRDALSRKLEIEQQEAFMTL------EQEQQVKTRTAEQNAKIAAFEAERRREAEQTRILAERQIQETEIDREQAV 304
Cdd:COG4913 257 IRELAERYAAARERLAELEYLRAAlrlwfaQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 305 RSRKVEAEREVRIKEIEQQQVTEIANQtksiaiaakseqqsQAEARANLALAEAVSAQQnVETTRQTAEADRAKQVALIA 384
Cdd:COG4913 337 GDRLEQLEREIERLERELEERERRRAR--------------LEALLAALGLPLPASAEE-FAALRAEAAALLEALEEELE 401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15833187 385 AAQDAETKAVelTVRAKAEKEAAEMQAaaivELAEATRKKGLAEAEAQRALNDAINVLSDEQTSLKF 451
Cdd:COG4913 402 ALEEALAEAE--AALRDLRRELRELEA----EIASLERRKSNIPARLLALRDALAEALGLDEAELPF 462
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
263-471 |
5.82e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 42.63 E-value: 5.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 263 RTAEQNAKiAAFEAERRREAEQTRIlaERQIQETEIDREQAVRSRKVEAEREV-----RIKE---IEQQQVTEIANQTKS 334
Cdd:PRK05035 439 RAIEQEKK-KAEEAKARFEARQARL--EREKAAREARHKKAAEARAAKDKDAVaaalaRVKAkkaAATQPIVIKAGARPD 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 335 IAIAAKSEQQSQAEARANLALAEAVS---------------------AQQNVETTRQTAEADRAKQVAL-IA------AA 386
Cdd:PRK05035 516 NSAVIAAREARKAQARARQAEKQAAAaadpkkaavaaaiarakakkaAQQAANAEAEEEVDPKKAAVAAaIArakakkAA 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 387 QDAETKAVELTVRAKAEKEAAemqAAAIVELAEATRKKGLAEAEAQRALNDAINVLSDEQTSLKFKLALLQALPAVIEKS 466
Cdd:PRK05035 596 QQAASAEPEEQVAEVDPKKAA---VAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEA 672
|
....*
gi 15833187 467 VEPMK 471
Cdd:PRK05035 673 EDPKK 677
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
203-430 |
6.77e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 6.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 203 AEGLTKLTQETERRRRERNEVEQDVEVAVREKNRDALSRKLEIEQQEAFMTLEQEQQVKTRTAEQNAKIAAFEAERRREA 282
Cdd:PTZ00121 1380 ADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKA 1459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 283 EQTRILAE--RQIQETEIDREQAVRSRKVEAEREVRIKEIEQ----QQVTEIANQTKSIAIAAKSEQQSQAEARANLALA 356
Cdd:PTZ00121 1460 EEAKKKAEeaKKADEAKKKAEEAKKADEAKKKAEEAKKKADEakkaAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEA 1539
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15833187 357 EAVSAQQNVETTRQTAEADRAKQVALIAAAQDAETKAVELTVRAKAEKEAAEMQAAAIVELAEATRKKGLAEAE 430
Cdd:PTZ00121 1540 KKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
232-434 |
9.92e-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: 41.97 E-value: 9.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 232 REKNRDALSRKL-EIEQQEAFMTlEQEQQVKTRTAEQNAKIAAFEAERRREAEQTRILA--ERQIQETEIDREQAVRSRK 308
Cdd:TIGR02168 770 LEEAEEELAEAEaEIEELEAQIE-QLKEELKALREALDELRAELTLLNEEAANLRERLEslERRIAATERRLEDLEEQIE 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 309 VEAEREVRI-KEIEQQQVTEIANQTKSIAIAAKSEQQSQAEARANLALAEAVSAQQNVETTRQTAEADRAKQVALIAAAQ 387
Cdd:TIGR02168 849 ELSEDIESLaAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15833187 388 DAETKAvELTVRAKAEKEAAEmqaaAIVELAEATRKKGLAEAEAQRA 434
Cdd:TIGR02168 929 LRLEGL-EVRIDNLQERLSEE----YSLTLEEAEALENKIEDDEEEA 970
|
|
| PHA00430 |
PHA00430 |
tail fiber protein |
321-438 |
1.31e-03 |
|
tail fiber protein
Pssm-ID: 222790 [Multi-domain] Cd Length: 568 Bit Score: 41.42 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 321 EQQQVTEIANQTKSIAIAAKSEQ---QSQAEARANLALAEAVSAQQ-NVETTRQTAEADRAKQVALIAAAQDAETKAVEL 396
Cdd:PHA00430 153 QIKTWNQSAWNARNEANRSRNEAdraRNQAERFNNESGASATNTKQwRSEADGSNSEANRFKGYADSMTSSVEAAKGQAE 232
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 15833187 397 TVRAK-------AEKEAAEMQAAAIVEL------AEATRKKGLAEAEAQRALNDA 438
Cdd:PHA00430 233 SSSKEantagdyATKAAASASAAHASEVnaansaTAAATSANRAKQQADRAKTEA 287
|
|
| SPFH_like |
cd02106 |
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ... |
84-188 |
1.46e-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: 38.50 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 84 IDSLITKDRMRVDVVVAFFVRVKPSVEGIATAaqtlgqRTLSPEDLRMLVEDKFVDALRATAAQMTMHELQDTRENFVQG 163
Cdd:cd02106 9 VEPVGTADGVPVAVDLVVQFRITDYNALPAFY------LVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEIAKA 82
|
90 100
....*....|....*....|....*
gi 15833187 164 VQNTVAEDLSKNGLELESVSLTNFN 188
Cdd:cd02106 83 VKEDLEEDLENFGVVISDVDITSIE 107
|
|
| PLN03086 |
PLN03086 |
PRLI-interacting factor K; Provisional |
242-313 |
1.48e-03 |
|
PRLI-interacting factor K; Provisional
Pssm-ID: 178635 [Multi-domain] Cd Length: 567 Bit Score: 41.40 E-value: 1.48e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15833187 242 KLEIEQQE----AFMTLEQEQQVKTRTAEQNAKIAAFEAERRREAEQTRILAERQIQETEIDREQAVRSRKVEAER 313
Cdd:PLN03086 11 KLEREQRErkqrAKLKLERERKAKEEAAKQREAIEAAQRSRRLDAIEAQIKADQQMQESLQAGRGIVFSRIFEAVS 86
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
246-443 |
1.52e-03 |
|
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: 41.48 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 246 EQQEAFMTLEQEQQVKTRTAEQNAKIA---------AFEA--------ERRREAEQTRILAERQI-QETEIDREQAVRSR 307
Cdd:COG3096 441 DYLAAFRAKEQQATEEVLELEQKLSVAdaarrqfekAYELvckiagevERSQAWQTARELLRRYRsQQALAQRLQQLRAQ 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 308 KVEAEREVRikeiEQQQVTEIANQ-TKSIAIAAKS-----EQQSQAEARANLALAEAVSAQQNVETTRQTAEADRAKQVA 381
Cdd:COG3096 521 LAELEQRLR----QQQNAERLLEEfCQRIGQQLDAaeeleELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKE 596
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 382 LIA------AAQDAETKAVELTVRAKAEKEA--AEMQAAAIVElAEATRKKGLAeAEAQRALNDAINVLS 443
Cdd:COG3096 597 LAArapawlAAQDALERLREQSGEALADSQEvtAAMQQLLERE-REATVERDEL-AARKQALESQIERLS 664
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
231-324 |
2.55e-03 |
|
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: 40.88 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 231 VREKNRDALSRKLEiEQQEAFMTLEQEQQVKTRTAEQNAKiAAFEAERRREAEQTR-----ILAERQIQE-TEIDREQAV 304
Cdd:pfam17380 489 AEEQRRKILEKELE-ERKQAMIEEERKRKLLEKEMEERQK-AIYEEERRREAEEERrkqqeMEERRRIQEqMRKATEERS 566
|
90 100
....*....|....*....|..
gi 15833187 305 RSRKVEAEREV--RIKEIEQQQ 324
Cdd:pfam17380 567 RLEAMEREREMmrQIVESEKAR 588
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
258-454 |
3.03e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 40.35 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 258 QQVKTRTAEQNAKIAAFEAERRREAEQTRILAERQIQETEIDREQAV----RSRKVEAEREVRIKEIEQQQVTEIANQTK 333
Cdd:PRK07735 8 EDLKKEAARRAKEEARKRLVAKHGAEISKLEEENREKEKALPKNDDMtieeAKRRAAAAAKAKAAALAKQKREGTEEVTE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 334 SIAIAAKSEQQSQAEARANLALAEAVSAQQNVETTRQTAEADRAKQVALIAAAQDAETKAVELTVRAKAEKEAAEMQAAA 413
Cdd:PRK07735 88 EEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15833187 414 IVELAEATRKKGLAEAEAQRALNDAINVLSDEQTSLKFKLA 454
Cdd:PRK07735 168 KAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAA 208
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
263-447 |
3.17e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 40.58 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 263 RTAEQNAKIAAFEAERRR-----EAEQTRILAERQIQETEIDREQAVRSRKVEAEREVRIKEIEQQQVTEIANQTKSIAI 337
Cdd:NF041483 520 RQAEETLERTRAEAERLRaeaeeQAEEVRAAAERAARELREETERAIAARQAEAAEELTRLHTEAEERLTAAEEALADAR 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 338 AAKSEQQSQAEARANLALAEAVSAQQNVETtRQTAEADRAKQVALIAAAQ---DAETKAVELTVRAKAEKEA-------- 406
Cdd:NF041483 600 AEAERIRREAAEETERLRTEAAERIRTLQA-QAEQEAERLRTEAAADASAaraEGENVAVRLRSEAAAEAERlkseaqes 678
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15833187 407 -----AEMQAAAIVELAEATRKKGLAEAEAQRALNDAINVLSDEQT 447
Cdd:NF041483 679 adrvrAEAAAAAERVGTEAAEALAAAQEEAARRRREAEETLGSARA 724
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
289-408 |
3.29e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 40.24 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 289 AERQIQETEIDREQAVRSRKV--EAEREVR-----IKEIEQQQV---TEIANQTKSIAIAAKSEQQSQAEARANLALAEA 358
Cdd:PRK12472 192 AETLAREAEDAARAADEAKTAaaAAAREAAplkasLRKLERAKAradAELKRADKALAAAKTDEAKARAEERQQKAAQQA 271
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 15833187 359 VSAQQNVETTRQTAEADRAKQVALIAAAQDAETKAVELTVRAKAEKEAAE 408
Cdd:PRK12472 272 AEAATQLDTAKADAEAKRAAAAATKEAAKAAAAKKAETAKAATDAKLALE 321
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
225-434 |
5.33e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 225 QDVEVAVREKNRDALSRKLEIEQQEAFMTLEQEQqvktRTAEQNAKIAAfeaERRREAEQTRILAERQIQETEIDREQAv 304
Cdd:PTZ00121 1281 DELKKAEEKKKADEAKKAEEKKKADEAKKKAEEA----KKADEAKKKAE---EAKKKADAAKKKAEEAKKAAEAAKAEA- 1352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 305 RSRKVEAEREVRIKEIEQQQVTEiaNQTKSIAIAAKSEQQSQAEARANLALAEAVSAQQNVETTRQTAEADRAKQVA-LI 383
Cdd:PTZ00121 1353 EAAADEAEAAEEKAEAAEKKKEE--AKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAeEK 1430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15833187 384 AAAQDAETKAVELTVRAKAEKEAAEMQAAA-IVELAEATRKKGLAEAEAQRA 434
Cdd:PTZ00121 1431 KKADEAKKKAEEAKKADEAKKKAEEAKKAEeAKKKAEEAKKADEAKKKAEEA 1482
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
238-412 |
8.09e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 38.81 E-value: 8.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 238 ALSRKLEIEQQEAfmtLEQEQQVKTRTAEQNAKIAAFEAERRREAEQTRILAERQIQETEIDREQAVRSRKVEAEREVRI 317
Cdd:PRK07735 107 ALAKQKREGTEEV---TEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQ 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 318 KEIEQQQVTEIAnqTKSIAIAAKSEQQSQAEARAnlalaeAVSAQQNVETTRQTAEADRAKQVALIAAAQDAETKAVELT 397
Cdd:PRK07735 184 KAAEAGEGTEEV--TEEEKAKAKAKAAAAAKAKA------AALAKQKASQGNGDSGDEDAKAKAIAAAKAKAAAAARAKT 255
|
170
....*....|....*
gi 15833187 398 VRAKAEKEAAEMQAA 412
Cdd:PRK07735 256 KGAEGKKEEEPKQEE 270
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
203-438 |
9.35e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.97 E-value: 9.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 203 AEGLTKLTQETERRRRERNEveqdvevAVREKNRDALSRKLEiEQQEAfmtleQEQQVKTRTAEQNAKIAAFEAERRREA 282
Cdd:PTZ00121 1446 ADEAKKKAEEAKKAEEAKKK-------AEEAKKADEAKKKAE-EAKKA-----DEAKKKAEEAKKKADEAKKAAEAKKKA 1512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 283 EQTRILAERQIQETEIDREQAVRSRKVEAEREVR-IKEIEQQQVTEIANQTKsiaiaaKSEQQSQAEARANLALAEAVSA 361
Cdd:PTZ00121 1513 DEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKkADELKKAEELKKAEEKK------KAEEAKKAEEDKNMALRKAEEA 1586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 362 QQ----NVETTRQTAEADRAKQVALIAAAQDAETKAVELTvraKAEKEAAEMQAAAIVELAEATRKKGLAEAEAQRALND 437
Cdd:PTZ00121 1587 KKaeeaRIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK---KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKA 1663
|
.
gi 15833187 438 A 438
Cdd:PTZ00121 1664 A 1664
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
237-349 |
9.37e-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: 9.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 237 DALSRKLEIEQQEAFMTL--EQEQQVKTRTAEQNAKIAAFEAErrREAEQTRILAERQIQETEIDReqavrsrkveaere 314
Cdd:cd03406 162 EAIRRNYEAMEAEKTKLLiaEQHQKVVEKEAETERKRAVIEAE--KDAEVAKIQMQQKIMEKEAEK-------------- 225
|
90 100 110
....*....|....*....|....*....|....*
gi 15833187 315 vRIKEIEQQQVTEianQTKSIAIAAKSEQQSQAEA 349
Cdd:cd03406 226 -KISEIEDEMHLA---REKARADAEYYRALREAEA 256
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
232-458 |
9.79e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 38.80 E-value: 9.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 232 REKNRDALSRKLEIEQQEAFMTLEQEQQVKTRTAEQNAKIAAFEAERRREAEQTRILAERQIQETEIDreqavRSRKVE- 310
Cdd:TIGR00618 220 RKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERIN-----RARKAAp 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833187 311 -AEREVRIKEIEQQQVTEIANQTKSIAIAAKSEQQSQAEARANLALAEavsaQQNVETTRQTAE---ADRAKQVALIAAA 386
Cdd:TIGR00618 295 lAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEE----QRRLLQTLHSQEihiRDAHEVATSIREI 370
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15833187 387 QDAETKAVELTVRAKAEKEAAEMQ---AAAIVELAEATRKKGLAEAEAQRALNDAINVLSDEQTSLKFKLALLQA 458
Cdd:TIGR00618 371 SCQQHTLTQHIHTLQQQKTTLTQKlqsLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAA 445
|
|
| |
