|
Name |
Accession |
Description |
Interval |
E-value |
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
13-535 |
6.12e-89 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 280.99 E-value: 6.12e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 13 FTAIIAVCILFIIGIIFARLYRRASAEQAFVRTG-LGGQKVVMSGGAIVMPIFHEIIPINMNTLKLEVSRStiDSLITKD 91
Cdd:COG2268 8 IIIGVIVVVLLLLLIILARFYRKVPPNEALVITGrGGGYKVVTGGGAFVLPVLHRAERMSLSTMTIEVERT--EGLITKD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 92 RMRVDVVVAFFVRVKPSVEGIATAAQTLGQRTlsPEDLRMLVEDKFVDALRATAAQMTMHELQDTRENFVQGVQNTVAED 171
Cdd:COG2268 86 GIRVDVDAVFYVKVNSDPEDIANAAERFLGRD--PEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 172 LSKNGLELESVSLTNFNQtskehfnPNNAFDAEGLTKLTQETERRRRERNEVEQDVEVAVREKNRdalsrkleieqQEAF 251
Cdd:COG2268 164 LAKNGLELESVAITDLED-------ENNYLDALGRRKIAEIIRDARIAEAEAERETEIAIAQANR-----------EAEE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 252 MTLEQEQQVKTRT-AEQNARIAAFEAERRREAEQTRILAERQIQETEIEREQAVrsrkveaerevrikeieqQQVTEIAN 330
Cdd:COG2268 226 AELEQEREIETARiAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAEREV------------------QRQLEIAE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 331 QTKSIAIAAKSEQQSQAEARAnlalaeavsaqqnvettrqtaeadrakqvaliaaaqdaetkavELTVRAKAEKEAAEMQ 410
Cdd:COG2268 288 REREIELQEKEAEREEAELEA-------------------------------------------DVRKPAEAEKQAAEAE 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 411 AAAIvelAEATRKKGLAEAEAQRALNDAINVLSDEQtslkFKLALLQALPAVIEKSVEPMKSIDGIKIIQvdglnrgsaa 490
Cdd:COG2268 325 AEAE---AEAIRAKGLAEAEGKRALAEAWNKLGDAA----ILLMLIEKLPEIAEAAAKPLEKIDKITIID---------- 387
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 446263191 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 |
1.76e-39 |
|
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: 139.77 E-value: 1.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 406 AAEMQAAAIVELAEATRKKGLAEAEAQRALNDAINVLSDEQTSLKFKLALLQALPAVIEKSVEPMKSIDGIKIIQVDGLN 485
Cdd:pfam15975 1 EAEAEADAIKLRAEAKRKKALAEAEGIRALNEAENALSDEQIALQVKLALLEALPEIIAESVKPLEKIDGIKILQVDGLG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 446263191 486 RGSAAGdANTGNVGGGNLAEQALSAALSYRTQAPLIDSLLNE 527
Cdd:pfam15975 81 GGAAGG-GGGGGGGGGSLAEQAVDSALGYRAQAPLIDSLLKE 121
|
|
| SPFH_flotillin |
cd03399 |
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ... |
59-209 |
3.49e-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: 3.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 59 IVMPIFHEIIPINMNTLKLEVSRSTIdslITKDRMRVDVVVAFFVRVKPSVEGIATAA-QTLGQRTlspEDLRMLVEDKF 137
Cdd:cd03399 1 FVIPFLQRVQRLSLETMTIDVKVEEV---LTKDGIPVDVTAVAQVKVGSDPEEIAAAAeRFLGKST---EEIRELVKETL 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446263191 138 VDALRATAAQMTMHELQDTRENFVQGVQNTVAEDLSKNGLELESVSLTNFNQTSkEHFNPNNAFDAEGLTKL 209
Cdd:cd03399 75 EGHLRAIVGTMTVEEIYQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDISDDN-GYLESLGRKQAAEVKKD 145
|
|
| PHB |
smart00244 |
prohibitin homologues; prohibitin homologues |
30-196 |
2.28e-15 |
|
prohibitin homologues; prohibitin homologues
Pssm-ID: 214581 [Multi-domain] Cd Length: 160 Bit Score: 73.85 E-value: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 30 ARLYRRASAEQAFVRTGLGGQKVVMSGGAIVMPIFHEIIPINMNTLKLEVSRSTIdslITKDRmrVDVVVAFFVRVKpSV 109
Cdd:smart00244 1 AAIKVVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQET---ITKDN--VKVSVDAVVYYR-VL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 110 EGIATAAQTLGQRTlspEDLRMLVEDkfvdALRATAAQMTMHELQ-DTRENFVQGVQNTVAEDLSKNGLELESVSLTN-- 186
Cdd:smart00244 75 DPLRAVYRVLDADY---AVIEQLAQT----TLRSVIGKRTLDELLtDQREKISENIREELNEAAEAWGIKVEDVEIKDir 147
|
170
....*....|
gi 446263191 187 FNQTSKEHFN 196
Cdd:smart00244 148 LPEEIKEAME 157
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
226-459 |
2.56e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.21 E-value: 2.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 226 DVEVAVREKNRDALSRKLEIEQQEAFMTLEQEQQVKTRTAEQNARIAAFEAERRREAEQTRILAERQIQETEIEREQAVR 305
Cdd:COG1196 266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 306 SRKVEAEREVRIKEIEQQQVTEIANQTKSIAIAAKSEQQSQAEARANLALAEAVSAQQNVETTRQTAEADRAKQVALIAA 385
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446263191 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 |
4.92e-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: 4.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 40 QAFVRTGLGG-QKVVMSGGAIVMPIFHEIIPINMNTLKLEVSRSTIdslITKDRMRVDVVVAFFVRVKPsvegiaTAAQT 118
Cdd:pfam01145 7 EVGVVTRFGKlSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTV---LTKDGVPVNVDVTVIYRVNP------DDPPK 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 119 LGQRTLSPEDLRMLVEDKFVDALRATAAQMTMHELQDTRENFVQGVQNTVAEDLSKNGLELESVSLTNFN 188
Cdd:pfam01145 78 LVQNVFGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDID 147
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
228-459 |
1.39e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.82 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 228 EVAVREKNRDALSRKLEIEQQEAFMTLEQEQQVKTRTAEQNARIAAFEAERRREAEQTRILAERQIQETEIEREQAVRSR 307
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 308 KVEAEREvriKEIEQQQVTEIANQTKSIAIAAKSEQQSQAEARANLALAEAVSAQQNVETTRQTAEADRAKQVALIAAAQ 387
Cdd:COG1196 334 ELEEELE---ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446263191 388 DAETKAVELTVRAKAEKEAAEMQAAAIVELAEATRKKGLAEAEAQRALNDAINVLSDEQTSLKFKLALLQAL 459
Cdd:COG1196 411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
228-468 |
3.39e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 228 EVAVREKNRDALSRKLEIEQQEAFMTLEQEQ--QVKTRTAEQNARIAAFEAERRREAEQTRILAER------QIQETEIE 299
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAEleELEAELEELEAELAELEAELEELRLELEELELEleeaqaEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 300 REQAVRSRKVEAEREVRIKEIEQQQVTEIANQTKSIA-IAAKSEQQSQAEARANLALAEAVSAQQNVETTRQTAEADRAK 378
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEeLEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 379 QVALIAAAQDAETKAVELTVRAKAEKEAAEMQAAAIVELAEATRKKGLAEAEAQRALNDAINVLSDEQTSLKFKLALLQA 458
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
250
....*....|
gi 446263191 459 LPAVIEKSVE 468
Cdd:COG1196 457 EEEALLELLA 466
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
245-428 |
1.78e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 59.82 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 245 IEQQEAFMTLEQEQ---QVKTRTAEQNARIAAfEAERRREAEQTRIL-------AERQIQETEIEREQAVRSRKVEAERE 314
Cdd:PRK09510 67 QQQQQKSAKRAEEQrkkKEQQQAEELQQKQAA-EQERLKQLEKERLAaqeqkkqAEEAAKQAALKQKQAEEAAAKAAAAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 315 VRIKEIEQQQVTEIANQTKSIAIA-AKSEQQSQAEARANlALAEAVSAQQNVETTRQTAEADrAKQVALIAAAQDAETKA 393
Cdd:PRK09510 146 KAKAEAEAKRAAAAAKKAAAEAKKkAEAEAAKKAAAEAK-KKAEAEAAAKAAAEAKKKAEAE-AKKKAAAEAKKKAAAEA 223
|
170 180 190
....*....|....*....|....*....|....*
gi 446263191 394 VELTVRAKAEKEAAEMQAAAIVELAEATRKKGLAE 428
Cdd:PRK09510 224 KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
244-465 |
7.14e-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: 57.55 E-value: 7.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 244 EIEQQEAFMTLEQEQQVK-TRTAEQNARIAAFEAERRREAEQTRILAERQIQETEIEREQAVRSRKVEAEREVRIKEIEQ 322
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAKkEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 323 QQVTEianqtKSIAIAAKSEQQSQAEARANlalAEAVSAQQNVETTRQTAEADRAKQVALIAAAQDAETKAVELTVRAKA 402
Cdd:TIGR02794 127 KQAAE-----AKAKAEAEAERKAKEEAAKQ---AEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKA 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446263191 403 E--KEAAEMQAAAIVELAEATRKKGLAEAEAQRALNDAINVLSDEQTSLKFKLALLQALPAVIEK 465
Cdd:TIGR02794 199 EaaKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDK 263
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
231-434 |
1.16e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 231 VREKNRDALSRKLEIEQ--QEAFMTLEQEQQVKTRTAEQNARI-AAFEAERRREAEQTRiLAERQIQETEIEREQAVRSR 307
Cdd:PTZ00121 1160 AEDARKAEEARKAEDAKkaEAARKAEEVRKAEELRKAEDARKAeAARKAEEERKAEEAR-KAEDAKKAEAVKKAEEAKKD 1238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 308 KVEAER--EVRIKEIEQQQVTEIANQTKSIAIAAKSEQQSQAEaraNLALAEAVSAQQNVETTRQTAEADRAKQVALIA- 384
Cdd:PTZ00121 1239 AEEAKKaeEERNNEEIRKFEEARMAHFARRQAAIKAEEARKAD---ELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAk 1315
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446263191 385 AAQDAETKAVELTVRAKA-EKEAAEMQAAAIVELAEATRKKGLAEAEAQRA 434
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAaKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
|
| HflC |
COG0330 |
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
15-313 |
2.67e-08 |
|
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440099 [Multi-domain] Cd Length: 279 Bit Score: 55.23 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 15 AIIAVCILFIIGIIFARLYRRASAEQAFVRTGLGG-QKVVMSGGAIVMPIFHEIIPINMNTLKLEVSRSTIdslITKDRm 93
Cdd:COG0330 3 LILLLILLVLVLVLLFSSVYIVPQGERGVVLRFGKyVRTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEV---LTKDN- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 94 rVDVVVAFFVRVKpsVEGIATAAQTLgqrtlspEDLRMLVEDKFVDALRATAAQMTMHELQDT-RENFVQGVQNTVAEDL 172
Cdd:COG0330 79 -NIVDVDAVVQYR--ITDPAKFLYNV-------ENAEEALRQLAESALREVIGKMTLDEVLSTgRDEINAEIREELQEAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 173 SKNGLELESVSLTNfnqtskehFNPNnafdaegltkltqeterrrrerneveQDVEVAVREKNRdalsrkleieqqeafm 252
Cdd:COG0330 149 DPYGIEVVDVEIKD--------IDPP--------------------------EEVQDAMEDRMK---------------- 178
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446263191 253 tleqeqqvktrtAEQNARIAAFEAERRREAEQTRILAERQ--IQETEIEREQAVRSRKVEAER 313
Cdd:COG0330 179 ------------AEREREAAILEAEGYREAAIIRAEGEAQraIIEAEAYREAQILRAEGEAEA 229
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
225-438 |
4.06e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 225 QDVEVAVREKNRDALSRKLEIEQQEAFMTLEQEQQVKTRTAEQNARIAAFEAERRREAEQTRILAERQIQETEIE--REQ 302
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAelEEE 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 303 AVRSRKVEAEREVRIKEIEQQQVTEIANQTKSIAIAAKSEQQSQAEARANLALAEAVSAQQNVETTRQTAEADRAKQVAL 382
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446263191 383 IAAAQDAETKAVELTVRAKAEKEAAEMQAAAIVELAEATRKKGLAEAEAQRALNDA 438
Cdd:COG1196 517 AGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAG 572
|
|
| SPFH_prohibitin |
cd03401 |
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ... |
43-187 |
4.13e-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: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 43 VRTGLGGQKVVMSGGA-IVMPIFHEIIPINMNTLKLEVSRSTIdsliTKDRMRVDVVVAffVRVKPSVEGIATAAQTLGq 121
Cdd:cd03401 13 FRRGKGVKDEVLGEGLhFKIPWIQVVIIYDVRTQPREITLTVL----SKDGQTVNIDLS--VLYRPDPEKLPELYQNLG- 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446263191 122 rtlsPEDLRMLVEDKFVDALRATAAQMTMHELQDTRENFVQGVQNTVAEDLSKNGLELESVSLTNF 187
Cdd:cd03401 86 ----PDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNI 147
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
231-434 |
4.43e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 4.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 231 VREKNRDALSRKLEIEQQEAfmtleQEQQVKTRTAEQNARIAAFEAERRREAEQTRILAERQIQETEIEREQAVRSRKVE 310
Cdd:PTZ00121 1347 AAKAEAEAAADEAEAAEEKA-----EAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAD 1421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 311 aerEVRIKEIEQQQVTEIANQTKSIAIAAKSEQQSQAEARANLALAEAVSAQQNVETTRQTAEADRAKQvaLIAAAQDAE 390
Cdd:PTZ00121 1422 ---EAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE--AKKKAEEAK 1496
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446263191 391 TKAVELTVRAKAEKEAAEMQAAAIVELAEATRKkglAEaEAQRA 434
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKADEAKKAEEAKKADEAKK---AE-EAKKA 1536
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
203-445 |
7.47e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 7.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 203 AEGLTKLTQETERRRRERNEVEQDVEVAVR-EKNRDALSRKLEIEQQ------EAFMTLEQEQQVKTRTAEQNARIAAFE 275
Cdd:PTZ00121 1542 AEEKKKADELKKAEELKKAEEKKKAEEAKKaEEDKNMALRKAEEAKKaeeariEEVMKLYEEEKKMKAEEAKKAEEAKIK 1621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 276 AERRREAEQTRILAERQIQETEIEREQAVRSRKVEAEREVRIKEIEQQqvteiANQTKSIAIAAKSEQQSqaEARANLAL 355
Cdd:PTZ00121 1622 AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK-----AEEDKKKAEEAKKAEED--EKKAAEAL 1694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 356 AEAVSAQQNVETTRQTAEADRAKQVALIAAAQDAETKAVELTVRAKAEKEAAEMQAAAIVELAEATRKKGLAEAEAQRAL 435
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIR 1774
|
250
....*....|
gi 446263191 436 NDAINVLSDE 445
Cdd:PTZ00121 1775 KEKEAVIEEE 1784
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
272-433 |
7.48e-07 |
|
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: 51.38 E-value: 7.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 272 AAFEAERRREAEQTRILAERQIQETEIEREQAVRSRKVEAEREVRIKEIEQQQVTEIANQTKSIAIAAKSEQQSQAEARA 351
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 352 NLALAEAVSAQQNVETTRQTAEADR-AKQVALIAAAQDAETKAVELTVRAKAEKEA---AEMQAAAIVELAEATRKKGLA 427
Cdd:TIGR02794 126 AKQAAEAKAKAEAEAERKAKEEAAKqAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAkaeAEAKAKAEEAKAKAEAAKAKA 205
|
....*.
gi 446263191 428 EAEAQR 433
Cdd:TIGR02794 206 AAEAAA 211
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
254-432 |
1.22e-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: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 254 LEQEQQVKTRTAEQNARIAAFEAERRR--EAEQTRILAERQIQ----ETEIEREQAVRSRKVEAeREVRIKEIEQQQVTE 327
Cdd:pfam15709 328 REQEKASRDRLRAERAEMRRLEVERKRreQEEQRRLQQEQLERaekmREELELEQQRRFEEIRL-RKQRLEEERQRQEEE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 328 IANQTKSIAIAAKSEQQSQAEARANlaLAEAVSAQQNVETTRQTAEADRAKQVALIAAAQD------AETKAVELTVRAK 401
Cdd:pfam15709 407 ERKQRLQLQAAQERARQQQEEFRRK--LQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQkrlmemAEEERLEYQRQKQ 484
|
170 180 190
....*....|....*....|....*....|.
gi 446263191 402 AEKEAAEMQAAAIVELAEATRKKGLAEAEAQ 432
Cdd:pfam15709 485 EAEEKARLEAEERRQKEEEAARLALEEAMKQ 515
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
277-468 |
2.28e-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: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 277 ERRREAE----QTR--------ILAE--RQIQETEIEREQAVRSRKVEAEREVRIKEIEQQQVTEIANQTKSIAIAAKSE 342
Cdd:COG1196 172 ERKEEAErkleATEenlerledILGEleRQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEEL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 343 QQSQAEARANLALAEAVSAQQNVETTRQTAEADRAKQVALIAAAQDAETKAvELTVRAKAEKEAAEMQAAAIVELAEATR 422
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ-DIARLEERRRELEERLEELEEELAELEE 330
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446263191 423 KKGLAEAEAQRALNDAINVLSDEQTSLKFKLALLQALPAVIEKSVE 468
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
230-468 |
2.59e-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: 50.44 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 230 AVREKNRDALSRKLEIEQQEAFMTLEQEQqvktrTAEQNARIAAFEAERRREAEQTRILAERQIQETEIEREQAVRSRKV 309
Cdd:TIGR02168 664 GSAKTNSSILERRREIEELEEKIEELEEK-----IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 310 EAEREVRIKEIEQQQVtEIANQTKSIAIAAKSEQQSQAEARAnlALAEAVSAQQNVETTRQTAEADRAKQVALIAAAQDA 389
Cdd:TIGR02168 739 EAEVEQLEERIAQLSK-ELTELEAEIEELEERLEEAEEELAE--AEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 390 ETKAVELTVRAKAEKEAAEMQAAAIVELAEATRKKGLAEAEAQRALND---AINVLSDEQTSLKFKLALLQALPAVIEKS 466
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEleeLIEELESELEALLNERASLEEALALLRSE 895
|
..
gi 446263191 467 VE 468
Cdd:TIGR02168 896 LE 897
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
232-432 |
1.54e-05 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 47.67 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 232 REKNRDALSRKLEIEQQEafmtLEQEQQVKTRTAEQNARIAAFEAERRREAEQTRILAERQIQETE-----IEREQAVRS 306
Cdd:PRK07735 19 KEEARKRLVAKHGAEISK----LEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREgteevTEEEKAKAK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 307 RKVEAEREVRIKEIEQQQVTEIANQTKSIAIAAKSEQQSQAEARANLALAEAVSAQQNVETTRQTAEADRAKQVALIAAA 386
Cdd:PRK07735 95 AKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAK 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446263191 387 QDAETKAVELTVRAKAEKEAAEMQAAAIVELAEATRKKGLAEAEAQ 432
Cdd:PRK07735 175 AKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAK 220
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
244-435 |
1.56e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.81 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 244 EIEQQEAFMTLEQE-----QQVKTRTAEQNARIAAFEAERRRE--------AEQTRILAERQ-----IQETEIERE-QAV 304
Cdd:pfam17380 286 ERQQQEKFEKMEQErlrqeKEEKAREVERRRKLEEAEKARQAEmdrqaaiyAEQERMAMERErelerIRQEERKRElERI 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 305 RSRKVEAE----REVRIKEIEQQQVTEIANQTKSIAIAAK-SEQQSQAEARANLALAEAVSAQQ---------------- 363
Cdd:pfam17380 366 RQEEIAMEisrmRELERLQMERQQKNERVRQELEAARKVKiLEEERQRKIQQQKVEMEQIRAEQeearqrevrrleeera 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446263191 364 -NVETTRQtAEADRAKQVALIAAAQDAETKAVELTVRAKAEKEAAEMQAAAIVELAEATRKKGLAEAEAQRAL 435
Cdd:pfam17380 446 rEMERVRL-EEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKL 517
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
264-434 |
1.67e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 264 TAEQNARIAAFEAERRREAEQTRILAERQIQETEIEREQAVRSRKVEAEREVR-IKEIEQQQVTEIANQTKSIAIAAKSE 342
Cdd:PTZ00121 1082 DAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARkAEDARKAEEARKAEDAKRVEIARKAE 1161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 343 QQSQAEARANLALAEAVSAQQNVETTRQTAEADRAKQVALIAAAQDAE-TKAVELTVRAKAEKEAAEmqaaaiVELAEAT 421
Cdd:PTZ00121 1162 DARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEeERKAEEARKAEDAKKAEA------VKKAEEA 1235
|
170
....*....|...
gi 446263191 422 RKKglaEAEAQRA 434
Cdd:PTZ00121 1236 KKD---AEEAKKA 1245
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
225-424 |
2.85e-05 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 46.93 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 225 QDVEVaVREKNRDALSR--KLEIEqqeafmtleqeqqVKTRTAEQNARiaaFEAERRREAEQTRIlaERQIQETEIEREQ 302
Cdd:PTZ00491 636 QSVEP-VDERTRDSLQKsvQLAIE-------------ITTKSQEAAAR---HQAELLEQEARGRL--ERQKMHDKAKAEE 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 303 AvrsrkveaerevRIKEIEQQqvteianqTKSIAIAAKSEQQSQAEARANLALAEavsAQQNVETTRQTAEADRakqval 382
Cdd:PTZ00491 697 Q------------RTKLLELQ--------AESAAVESSGQSRAEALAEAEARLIE---AEAEVEQAELRAKALR------ 747
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446263191 383 IAAAQDAETKAVELTVRAKAEKEAAEMQAAAIVELAEATRKK 424
Cdd:PTZ00491 748 IEAEAELEKLRKRQELELEYEQAQNELEIAKAKELADIEATK 789
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
255-524 |
5.75e-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: 5.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 255 EQEQQVKTRTAEQNARIAAFEAERRREAEQTRILaERQIQETEIEREQAVRSRKVEAEREVRIKEIEQQQVTEIANQtkS 334
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQKQILRERLANL-ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESL--E 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 335 IAIAAKSEQQSQAEARANLALAEAVSAQQNVETTRQTAEADRAKQVALIAAAQDAETKAVELTVRAKAEKEAAEMQAAAI 414
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 415 VELAEATRKKGLAEAEAQRA--------LNDAINVLSDEQTSLKFKLALLQALPAVIEKSVEpmksidgikiiQVDGLNR 486
Cdd:TIGR02168 438 LQAELEELEEELEELQEELErleealeeLREELEEAEQALDAAERELAQLQARLDSLERLQE-----------NLEGFSE 506
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446263191 487 GSAAGDANtGNVGGGNLA------------EQALSAALSYRTQAPLIDSL 524
Cdd:TIGR02168 507 GVKALLKN-QSGLSGILGvlselisvdegyEAAIEAALGGRLQAVVVENL 555
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
233-401 |
6.95e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 6.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 233 EKNRDALSRKLEIEQQEAFMTLEQEQQVKTRtAEQNARIAAFE---AERRREAEQTRILAERQIQETEIEREQAVRSRKV 309
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAEEENKIK-AAEEAKKAEEDkkkAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK 1710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 310 EAErevRIKEIEQQQVTEIANQTKSIAIAAKSEQQSQAEARANLALAEAVSAQQNVETTRQTAEADRAKQVALIAAAQDA 389
Cdd:PTZ00121 1711 EAE---EKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
|
170
....*....|..
gi 446263191 390 ETKAVELTVRAK 401
Cdd:PTZ00121 1788 EDEKRRMEVDKK 1799
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
303-438 |
7.90e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 45.25 E-value: 7.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 303 AVRSRkveAEREVRikeiEQQQVTEIANQTKSIAIAAKSEQQS---------QAEARANLALAEAVSAQQNVETTRQTAE 373
Cdd:PRK12472 187 AAPAR---AETLAR----EAEDAARAADEAKTAAAAAAREAAPlkaslrkleRAKARADAELKRADKALAAAKTDEAKAR 259
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446263191 374 ADRAKQvaliAAAQDAETKAVELTVrAKAEKEAAEMQAAAIVELAEATRKKglaEAEAQRALNDA 438
Cdd:PRK12472 260 AEERQQ----KAAQQAAEAATQLDT-AKADAEAKRAAAAATKEAAKAAAAK---KAETAKAATDA 316
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
274-454 |
9.51e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 9.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 274 FEAERRREA-EQTRILAERQIQETEIEREQAVRSRKVEAEREVRIKEIEQQQVTEIANQTKSIAIAAKSEQQSQAEArAN 352
Cdd:COG4913 606 FDNRAKLAAlEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDA-SS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 353 LALAEAVSAQQNVETTRQTAEADRAKQVALIAAAQDAETKAVELTVRAKAEKEAAEMQAAAIVELAEATRKKGLAEAEAQ 432
Cdd:COG4913 685 DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVE 764
|
170 180
....*....|....*....|..
gi 446263191 433 RALNDAINVLSDEQTSLKFKLA 454
Cdd:COG4913 765 RELRENLEERIDALRARLNRAE 786
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
233-458 |
1.12e-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: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 233 EKNRDALSRKLEIEQQEAFMTLEQEQQVKTRTAEQNARIAAFEAERRREAEQ--------TRILAERQIQETEIEREQAV 304
Cdd:TIGR02168 697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqlskelTELEAEIEELEERLEEAEEE 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 305 RSRkVEAEREVRIKEIEQQQvtEIANQTKSIAIAAKSEQQSQAEARANLALAEAVSAQQNVETTRQ---------TAEAD 375
Cdd:TIGR02168 777 LAE-AEAEIEELEAQIEQLK--EELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRledleeqieELSED 853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 376 RAKQVALIAAAQDAETKAVELTVRAKAEKEAAEMQAAAIVELAEATRKKGLAEAEAQRALNDAINVLSDEQTSLKFKLAL 455
Cdd:TIGR02168 854 IESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG 933
|
...
gi 446263191 456 LQA 458
Cdd:TIGR02168 934 LEV 936
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
233-438 |
1.16e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 233 EKNRDALSRKLEIEQQ-EAFMTLEQEQQVKTRTAEQNARIAAFEAerrREAEQTRILAERQIQETEIEREQAVRSRKVEA 311
Cdd:PTZ00121 1198 DARKAEAARKAEEERKaEEARKAEDAKKAEAVKKAEEAKKDAEEA---KKAEEERNNEEIRKFEEARMAHFARRQAAIKA 1274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 312 EREVRIKEI---EQQQVTEIANQTKSIAIAAKSEQQSQAEARANLALAEAVSAQQNVETTRQTAEadRAKQVALIAAAQd 388
Cdd:PTZ00121 1275 EEARKADELkkaEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAE--EAKKAAEAAKAE- 1351
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446263191 389 AETKAVELTvRAKAEKEAAEMQAAAIVELAEATRKKGLAEAEAQRALNDA 438
Cdd:PTZ00121 1352 AEAAADEAE-AAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKA 1400
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
227-458 |
1.42e-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: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 227 VEVAVREKNRDALSRKLEIEQQEAFMTL-EQEQQVK-----TRTAEQNARIAAFEAERRREAEQTRILaERQIQETEIER 300
Cdd:TIGR02168 191 LEDILNELERQLKSLERQAEKAERYKELkAELRELElallvLRLEELREELEELQEELKEAEEELEEL-TAELQELEEKL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 301 EQaVRSRKVEAEREVRIKEIEQQQVT-EIANQTKSIAIAAKSEQQSQAE-ARANLALAEAVSAQQNVettrQTAEADRAK 378
Cdd:TIGR02168 270 EE-LRLEVSELEEEIEELQKELYALAnEISRLEQQKQILRERLANLERQlEELEAQLEELESKLDEL----AEELAELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 379 QVALIAAAQDAETKAVEltvRAKAEKEAAEMQAAAIVELAEATRKKgLAEAEAQRALNDA-INVLSDEQTSLKFKLALLQ 457
Cdd:TIGR02168 345 KLEELKEELESLEAELE---ELEAELEELESRLEELEEQLETLRSK-VAQLELQIASLNNeIERLEARLERLEDRRERLQ 420
|
.
gi 446263191 458 A 458
Cdd:TIGR02168 421 Q 421
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
233-432 |
1.78e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.34 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 233 EKNRDALSRKLEIEQQEAFMTLEQEQQVKTRTAEQNARIAAFEAERRREAEQTRILAER-----QIQETEIEREQAV-RS 306
Cdd:pfam17380 386 ERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERaremeRVRLEEQERQQQVeRL 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 307 RKVEAEREVRIKEIEQQQVTE-IANQTKSIAIAAKSEQQSQA---EARANLALAEAVSAQQNV---ETTRQTAEADRAKQ 379
Cdd:pfam17380 466 RQQEEERKRKKLELEKEKRDRkRAEEQRRKILEKELEERKQAmieEERKRKLLEKEMEERQKAiyeEERRREAEEERRKQ 545
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446263191 380 VALiaaaqdAETKAVELTVRAKAEK----EAAEMQAAAIVELAEATRKKGLAEAEAQ 432
Cdd:pfam17380 546 QEM------EERRRIQEQMRKATEErsrlEAMEREREMMRQIVESEKARAEYEATTP 596
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
230-477 |
2.46e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 230 AVREKNRDALSRKLEIEQQEAFMTLEQEQQVKTRTAEQNARIAAFEAERRREAEQTRILAERQIQETEIEREQAVRSRKV 309
Cdd:PTZ00121 1361 AAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKA 1440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 310 EAER---EVRIKEIEQQQVTEIANQTKSIAIAAKSEQQSQAEARANLALAEAVSAQQNVETTRQTAEADRAKQvaliAAA 386
Cdd:PTZ00121 1441 EEAKkadEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD----EAK 1516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 387 QDAETKAVELTVRAKAEKEAAEMQAAAIVELAEATRK-KGLAEAEAQRALNDAINVLSDEQTSLKFKLALLQALPAVIEK 465
Cdd:PTZ00121 1517 KAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKaEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEE 1596
|
250
....*....|..
gi 446263191 466 SVEPMKSIDGIK 477
Cdd:PTZ00121 1597 VMKLYEEEKKMK 1608
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
260-448 |
2.53e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 260 VKTRTAEQNARIAAFEAERRREAEQTRilAERQIQETEIEREQAVRSRKVEAEREVRIKEIEQQQVtEIANQTKSIAIAA 339
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKRILEEAKKE--AEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKL-EKRLLQKEENLDR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 340 KSEQQSQAEARANLALAEAVSAQQNVETTRQTAEADRAKQVAL---IAAAQDAETKAVEL-TVRAKAEKEAAEMqAAAIV 415
Cdd:PRK12704 101 KLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQElerISGLTAEEAKEILLeKVEEEARHEAAVL-IKEIE 179
|
170 180 190
....*....|....*....|....*....|...
gi 446263191 416 ELAEATrkkglAEAEAQRALNDAINVLSDEQTS 448
Cdd:PRK12704 180 EEAKEE-----ADKKAKEILAQAIQRCAADHVA 207
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
263-431 |
3.05e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.78 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 263 RTAEQNARiAAFEAERRREAEQTRIlaerqiqeteiEREqavrsrkvEAEREVRIKEIEQQQVTEIANQTKSiAIAAKSE 342
Cdd:PRK05035 439 RAIEQEKK-KAEEAKARFEARQARL-----------ERE--------KAAREARHKKAAEARAAKDKDAVAA-ALARVKA 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 343 QQSQAEARANLALAEAVSAQQNVETTRQTAEADRAKQVALIAAAQDAETKA-VELTV-RAKAEKeAAEMQAAAIVELAEA 420
Cdd:PRK05035 498 KKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAaVAAAIaRAKAKK-AAQQAANAEAEEEVD 576
|
170
....*....|.
gi 446263191 421 TRKKGLAEAEA 431
Cdd:PRK05035 577 PKKAAVAAAIA 587
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
247-469 |
3.21e-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: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 247 QQEAFMTLEQE-QQVKTRTAEQNARIAAFEAERR------REAEQTRILAERQIQETEIEREQAvrsRKVEAEREVRIKE 319
Cdd:COG4942 18 QADAAAEAEAElEQLQQEIAELEKELAALKKEEKallkqlAALERRIAALARRIRALEQELAAL---EAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 320 IEQQQVTEIANQTKSIAIAAKSEQQSQAEARanLALAEAVSAQQNVETTRQTAEADRAKQVALIAAAQDAETKAVELTVR 399
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALL--LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446263191 400 AKAEKEAAEMQAAAIVEL--AEATRKKGLAEAEAQR-ALNDAINVLSDEQTSLKFKLALLQALPAVIEKSVEP 469
Cdd:COG4942 173 RAELEALLAELEEERAALeaLKAERQKLLARLEKELaELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
231-451 |
3.29e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 231 VREKNRDALSRKLEIEQQEAFMTL------EQEQQVKTRTAEQNARIAAFEAERRREAEQTRILAERQIQETEIEREQAV 304
Cdd:COG4913 257 IRELAERYAAARERLAELEYLRAAlrlwfaQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 305 RSRKVEAEREVRIKEIEQQQVTEIANQtksiaiaakseqqsQAEARANLALAEAVSAQQnVETTRQTAEADRAKQVALIA 384
Cdd:COG4913 337 GDRLEQLEREIERLERELEERERRRAR--------------LEALLAALGLPLPASAEE-FAALRAEAAALLEALEEELE 401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446263191 385 AAQDAETKAVelTVRAKAEKEAAEMQAaaivELAEATRKKGLAEAEAQRALNDAINVLSDEQTSLKF 451
Cdd:COG4913 402 ALEEALAEAE--AALRDLRRELRELEA----EIASLERRKSNIPARLLALRDALAEALGLDEAELPF 462
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
232-434 |
3.94e-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: 43.51 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 232 REKNRDALSRKL-EIEQQEAfmtleQEQQVKTRTAEQNARIAAFEAE------RRREAEQTRILAERQIQETEIEREQAV 304
Cdd:TIGR02168 770 LEEAEEELAEAEaEIEELEA-----QIEQLKEELKALREALDELRAEltllneEAANLRERLESLERRIAATERRLEDLE 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 305 RSRKVEAEREVRI-KEIEQQQVTEIANQTKSIAIAAKSEQQSQAEARANLALAEAVSAQQNVETTRQTAEADRAKQVALI 383
Cdd:TIGR02168 845 EQIEELSEDIESLaAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446263191 384 AAAQDAETKAvELTVRAKAEKEAAEmqaaAIVELAEATRKKGLAEAEAQRA 434
Cdd:TIGR02168 925 AQLELRLEGL-EVRIDNLQERLSEE----YSLTLEEAEALENKIEDDEEEA 970
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
203-430 |
5.86e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 5.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 203 AEGLTKLTQETERRRRERNEVEQDVEVAVREKNRDALSRKLEIEQQEAFMTLEQEQQVKTRTAEQNARIAAFEAERRREA 282
Cdd:PTZ00121 1380 ADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKA 1459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 283 EQTRILAE--RQIQETEIEREQAVRSRKVEAEREVRIKEIEQ----QQVTEIANQTKSIAIAAKSEQQSQAEARANLALA 356
Cdd:PTZ00121 1460 EEAKKKAEeaKKADEAKKKAEEAKKADEAKKKAEEAKKKADEakkaAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEA 1539
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446263191 357 EAVSAQQNVETTRQTAEADRAKQVALIAAAQDAETKAVELTVRAKAEKEAAEMQAAAIVELAEATRKKGLAEAE 430
Cdd:PTZ00121 1540 KKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
246-443 |
1.23e-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: 41.86 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 246 EQQEAFMTLEQEQQVKTRTAEQNARIA---------AFEA--------ERRREAEQTRILAERQI-QETEIEREQAVRSR 307
Cdd:COG3096 441 DYLAAFRAKEQQATEEVLELEQKLSVAdaarrqfekAYELvckiagevERSQAWQTARELLRRYRsQQALAQRLQQLRAQ 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 308 KVEAEREVRikeiEQQQVTEIANQ-TKSIAIAAKS-----EQQSQAEARANLALAEAVSAQQNVETTRQTAEADRAKQVA 381
Cdd:COG3096 521 LAELEQRLR----QQQNAERLLEEfCQRIGQQLDAaeeleELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKE 596
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 382 LIA------AAQDAETKAVELTVRAKAEKEA--AEMQAAAIVElAEATRKKGLAeAEAQRALNDAINVLS 443
Cdd:COG3096 597 LAArapawlAAQDALERLREQSGEALADSQEvtAAMQQLLERE-REATVERDEL-AARKQALESQIERLS 664
|
|
| SPFH_like |
cd02106 |
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ... |
84-188 |
1.42e-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: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 84 IDSLITKDRMRVDVVVAFFVRVKPSVEGIATAaqtlgqRTLSPEDLRMLVEDKFVDALRATAAQMTMHELQDTRENFVQG 163
Cdd:cd02106 9 VEPVGTADGVPVAVDLVVQFRITDYNALPAFY------LVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEIAKA 82
|
90 100
....*....|....*....|....*
gi 446263191 164 VQNTVAEDLSKNGLELESVSLTNFN 188
Cdd:cd02106 83 VKEDLEEDLENFGVVISDVDITSIE 107
|
|
| PHA00430 |
PHA00430 |
tail fiber protein |
321-438 |
1.43e-03 |
|
tail fiber protein
Pssm-ID: 222790 [Multi-domain] Cd Length: 568 Bit Score: 41.42 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 321 EQQQVTEIANQTKSIAIAAKSEQ---QSQAEARANLALAEAVSAQQ-NVETTRQTAEADRAKQVALIAAAQDAETKAVEL 396
Cdd:PHA00430 153 QIKTWNQSAWNARNEANRSRNEAdraRNQAERFNNESGASATNTKQwRSEADGSNSEANRFKGYADSMTSSVEAAKGQAE 232
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 446263191 397 TVRAK-------AEKEAAEMQAAAIVEL------AEATRKKGLAEAEAQRALNDA 438
Cdd:PHA00430 233 SSSKEantagdyATKAAASASAAHASEVnaansaTAAATSANRAKQQADRAKTEA 287
|
|
| PLN03086 |
PLN03086 |
PRLI-interacting factor K; Provisional |
242-313 |
1.57e-03 |
|
PRLI-interacting factor K; Provisional
Pssm-ID: 178635 [Multi-domain] Cd Length: 567 Bit Score: 41.40 E-value: 1.57e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446263191 242 KLEIEQQE----AFMTLEQEQQVKTRTAEQNARIAAFEAERRREAEQTRILAERQIQETEIEREQAVRSRKVEAER 313
Cdd:PLN03086 11 KLEREQRErkqrAKLKLERERKAKEEAAKQREAIEAAQRSRRLDAIEAQIKADQQMQESLQAGRGIVFSRIFEAVS 86
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
258-454 |
1.62e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 41.12 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 258 QQVKTRTAEQNARIAAFEAERRREAEQTRILAERQIQETEIEREQAV----RSRKVEAEREVRIKEIEQQQVTEIANQTK 333
Cdd:PRK07735 8 EDLKKEAARRAKEEARKRLVAKHGAEISKLEEENREKEKALPKNDDMtieeAKRRAAAAAKAKAAALAKQKREGTEEVTE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 334 SIAIAAKSEQQSQAEARANLALAEAVSAQQNVETTRQTAEADRAKQVALIAAAQDAETKAVELTVRAKAEKEAAEMQAAA 413
Cdd:PRK07735 88 EEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446263191 414 IVELAEATRKKGLAEAEAQRALNDAINVLSDEQTSLKFKLA 454
Cdd:PRK07735 168 KAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAA 208
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
229-431 |
2.28e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 40.70 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 229 VAVREKNRDALSRKLEiEQQEAFMTLEQEQQVKTRTAEQNARIAAFEAERRREAEQTRilAERQIQETEIEREQAV---- 304
Cdd:PRK05035 478 EARAAKDKDAVAAALA-RVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQ--AEKQAAAAADPKKAAVaaai 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 305 ---RSRKVEAEREVRIKEIEQQQVTEIANQTKSIAIAAKSEQQsQAEARANLALAEAVSAQQNVETTRQTAEADRAKQVA 381
Cdd:PRK05035 555 araKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQ-AASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQA 633
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446263191 382 LIAAAQ--DAETKAVELTV-RAKAEKEAAEmQAAAIVELAEATRKKGLAEAEA 431
Cdd:PRK05035 634 NAEPEEpvDPRKAAVAAAIaRAKARKAAQQ-QANAEPEEAEDPKKAAVAAAIA 685
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
289-408 |
2.91e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 40.24 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 289 AERQIQETEIEREQAVRSRKV--EAEREVR-----IKEIEQQQV---TEIANQTKSIAIAAKSEQQSQAEARANLALAEA 358
Cdd:PRK12472 192 AETLAREAEDAARAADEAKTAaaAAAREAAplkasLRKLERAKAradAELKRADKALAAAKTDEAKARAEERQQKAAQQA 271
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 446263191 359 VSAQQNVETTRQTAEADRAKQVALIAAAQDAETKAVELTVRAKAEKEAAE 408
Cdd:PRK12472 272 AEAATQLDTAKADAEAKRAAAAATKEAAKAAAAKKAETAKAATDAKLALE 321
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
231-324 |
3.11e-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: 40.49 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 231 VREKNRDALSRKLEIEQQEafmTLEQEQQVKTRTAEQNAR-IAAFEAERRREAEQTR-----ILAERQIQE-TEIEREQA 303
Cdd:pfam17380 489 AEEQRRKILEKELEERKQA---MIEEERKRKLLEKEMEERqKAIYEEERRREAEEERrkqqeMEERRRIQEqMRKATEER 565
|
90 100
....*....|....*....|...
gi 446263191 304 VRSRKVEAEREV--RIKEIEQQQ 324
Cdd:pfam17380 566 SRLEAMEREREMmrQIVESEKAR 588
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
233-435 |
3.11e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 233 EKNRDALSRKLEIEQQEAFMTLEQEQQVKTRTAEQNARiaafEAERRREAEQTRILAER-QIQETEIEREQAVRSRKVEa 311
Cdd:PTZ00121 1604 EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK----EAEEKKKAEELKKAEEEnKIKAAEEAKKAEEDKKKAE- 1678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 312 erEVRIKEIEQQQVTEianqtksiAIAAKSEQQSQAEARANLALAEAVSAQQnvetTRQTAEADRAKQVALIAAAQDAET 391
Cdd:PTZ00121 1679 --EAKKAEEDEKKAAE--------ALKKEAEEAKKAEELKKKEAEEKKKAEE----LKKAEEENKIKAEEAKKEAEEDKK 1744
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446263191 392 KAVELTVRAKAEKEAA------EMQAAAIVELAEATRKKGLAEAEAQRAL 435
Cdd:PTZ00121 1745 KAEEAKKDEEEKKKIAhlkkeeEKKAEEIRKEKEAVIEEELDEEDEKRRM 1794
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
263-447 |
3.37e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 40.58 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 263 RTAEQNARIAAFEAERRR-----EAEQTRILAERQIQETEIEREQAVRSRKVEAEREVRIKEIEQQQVTEIANQTKSIAI 337
Cdd:NF041483 520 RQAEETLERTRAEAERLRaeaeeQAEEVRAAAERAARELREETERAIAARQAEAAEELTRLHTEAEERLTAAEEALADAR 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 338 AAKSEQQSQAEARANLALAEAVSAQQNVETtRQTAEADRAKQVALIAAAQ---DAETKAVELTVRAKAEKEA-------- 406
Cdd:NF041483 600 AEAERIRREAAEETERLRTEAAERIRTLQA-QAEQEAERLRTEAAADASAaraEGENVAVRLRSEAAAEAERlkseaqes 678
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446263191 407 -----AEMQAAAIVELAEATRKKGLAEAEAQRALNDAINVLSDEQT 447
Cdd:NF041483 679 adrvrAEAAAAAERVGTEAAEALAAAQEEAARRRREAEETLGSARA 724
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
203-438 |
5.51e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 203 AEGLTKLTQETERRRRERNEveqdvevAVREKNRDALSRKLEiEQQEAfmtleQEQQVKTRTAEQNARIAAFEAERRREA 282
Cdd:PTZ00121 1446 ADEAKKKAEEAKKAEEAKKK-------AEEAKKADEAKKKAE-EAKKA-----DEAKKKAEEAKKKADEAKKAAEAKKKA 1512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 283 EQTRILAERQIQEteiEREQAVRSRKVEAERevRIKEIEQQQVTEIANQTKSIAIAAKSEQQSQAEARANLALAEAVSAQ 362
Cdd:PTZ00121 1513 DEAKKAEEAKKAD---EAKKAEEAKKADEAK--KAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAK 1587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 363 Q----NVETTRQTAEADRAKQVALIAAAQDAETKAVELTvraKAEKEAAEMQAAAIVELAEATRKKGLAEAEAQRALNDA 438
Cdd:PTZ00121 1588 KaeeaRIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK---KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAA 1664
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
232-458 |
7.97e-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: 39.18 E-value: 7.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 232 REKNRDALSRKLEIEQQEAFMTLEQEQQVKTRTAEQNARIAAFEAERRREAEqtrilAERQIQETEIEREQAVRSRKVE- 310
Cdd:TIGR00618 220 RKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEE-----LRAQEAVLEETQERINRARKAAp 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 311 -AEREVRIKEIEQQQVTEIANQTKSIAIAAKSEQQSQAEARANLALAEavsaQQNVETTRQTAE---ADRAKQVALIAAA 386
Cdd:TIGR00618 295 lAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEE----QRRLLQTLHSQEihiRDAHEVATSIREI 370
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446263191 387 QDAETKAVELTVRAKAEKEAAEMQ---AAAIVELAEATRKKGLAEAEAQRALNDAINVLSDEQTSLKFKLALLQA 458
Cdd:TIGR00618 371 SCQQHTLTQHIHTLQQQKTTLTQKlqsLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAA 445
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
238-412 |
9.21e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 38.81 E-value: 9.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 238 ALSRKLEIEQQEAfmtLEQEQQVKTRTAEQNARIAAFEAERRREAEQTRILAERQIQETEIEREQAVRSRKVEAEREVRI 317
Cdd:PRK07735 107 ALAKQKREGTEEV---TEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQ 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 318 KEIEQQQVTEIAnqTKSIAIAAKSEQQSQAEARAnlalaeAVSAQQNVETTRQTAEADRAKQVALIAAAQDAETKAVELT 397
Cdd:PRK07735 184 KAAEAGEGTEEV--TEEEKAKAKAKAAAAAKAKA------AALAKQKASQGNGDSGDEDAKAKAIAAAKAKAAAAARAKT 255
|
170
....*....|....*
gi 446263191 398 VRAKAEKEAAEMQAA 412
Cdd:PRK07735 256 KGAEGKKEEEPKQEE 270
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
269-434 |
9.21e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 38.87 E-value: 9.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 269 ARIAAFEAERRREAEQTRIL-----AERQIQETEIEREQAVRSRKVEAEREVRIKEIEQQQVTEIAnQTKSIAIAAKSEQ 343
Cdd:PRK10811 848 VRPQDVQVEEQREAEEVQVQpvvaeVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVE-TTHPEVIAAPVTE 926
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 344 QSQAEARANLALAEAVSAqqnvETTRQTAEADRAKQVAliAAAQDAETKAVELTVRAKAEKEAAEMQAAAIVE------- 416
Cdd:PRK10811 927 QPQVITESDVAVAQEVAE----HAEPVVEPQDETADIE--EAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETvtavepe 1000
|
170 180
....*....|....*....|...
gi 446263191 417 -----LAEATRKKGLAEAEAQRA 434
Cdd:PRK10811 1001 vapaqVPEATVEHNHATAPMTRA 1023
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
280-438 |
9.59e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.97 E-value: 9.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 280 REAEQTRILAERQIQETEIEREQAVRSRKVE---AEREVRIKEIEQQqvteiANQTKSIAIAAKSEQQSQAEARANLALA 356
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATEEAFGKAEEAKKTEtgkAEEARKAEEAKKK-----AEDARKAEEARKAEDARKAEEARKAEDA 1151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446263191 357 EAVSAQQNVETTRQTAEADRAKQVALIAAAQDAET--KAVELTVRAKAEKEAAEMQAAAIVELAEATRKKGLAEAEAQRA 434
Cdd:PTZ00121 1152 KRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEvrKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKK 1231
|
....
gi 446263191 435 LNDA 438
Cdd:PTZ00121 1232 AEEA 1235
|
|
| |
