|
Name |
Accession |
Description |
Interval |
E-value |
| gamma_tubulin |
cd02188 |
The gamma-tubulin family; Gamma-tubulin is a ubiquitous phylogenetically conserved member of ... |
265-618 |
0e+00 |
|
The gamma-tubulin family; Gamma-tubulin is a ubiquitous phylogenetically conserved member of tubulin superfamily. Gamma is a low abundance protein present within the cells in both various types of microtubule-organizing centers and cytoplasmic protein complexes. Gamma-tubulin recruits the alpha/beta-tubulin dimers that form the minus ends of microtubules and is thought to be involved in microtubule nucleation and capping.
Pssm-ID: 276957 [Multi-domain] Cd Length: 430 Bit Score: 528.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 265 RRWDKPKNIYLSKHGGGSGNNWISRFSQGEKIHEDILDIIDEEADGSDSQRGFVLHYSIAWGTGSGLGSYLLE*LNDRYP 344
Cdd:cd02188 81 KNLFNPENIYLSKEGGGAGNNWASGYSQGEKVQEEILDIIDREAEGSDSLEGFVLCHSIAGGTGSGMGSYLLERLSDRYP 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 345 MKLVQTYSVFPYQNEMSHMVCQPNNSLLMLKRLTQKADCVVVLDDMALNWIATDCMHIQNLSFSQINQLVSTITLASTTI 424
Cdd:cd02188 161 KKLIQTYSVFPNQEESSDVVVQPYNSILTLKRLTLNADCVVVLDNTALNRIATDRLKIDNPSFSQINSLISTVMSASTST 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 425 LCYLSFMNNDLIGLIASLILTPQFYFLTTDYTPtLTMDQSVANMRKTTVLEVMRWLLQRKSMMVLTGRdcqTSHCYITIL 504
Cdd:cd02188 241 LRFPGYMNNDLVSLISSLIPTPRLHFLMTSYTP-LTSDQVASSVRKTTVLDVMRRLLQPKNRMVSTST---KNGCYISIL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 505 TIIQGEVDPTQVHKSLQRIQEGKLANFIPWGPASIQVALLRRCSYLPSAQWTSRIIMANHTSISSLFESSCQQFDKLQKW 584
Cdd:cd02188 317 NIIQGEVDPTQVHKSLQRIRERKLANFIPWGPASIQVALSKKSPYVQTAHRVSGLMLANHTSISSLFEKILSQYDKLRKR 396
|
330 340 350
....*....|....*....|....*....|....
gi 1149889000 585 DTFLEEFFKEPMFKDNFDEMDRSRKVVQEFIDEY 618
Cdd:cd02188 397 NAFLENYRKEDMFQDNLEEFDESREVVQSLIDEY 430
|
|
| PLN00222 |
PLN00222 |
tubulin gamma chain; Provisional |
270-634 |
7.69e-172 |
|
tubulin gamma chain; Provisional
Pssm-ID: 215108 [Multi-domain] Cd Length: 454 Bit Score: 497.83 E-value: 7.69e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 270 PKNIYLSKHGGGSGNNWISRFSQGEKIHEDILDIIDEEADGSDSQRGFVLHYSIAWGTGSGLGSYLLE*LNDRYPMKLVQ 349
Cdd:PLN00222 88 HENIFVSDHGGGAGNNWASGYHQGEQVEEDIMDMIDREADGSDSLEGFVLCHSIAGGTGSGMGSYLLEALNDRYSKKLVQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 350 TYSVFPYQNEMSHMVCQPNNSLLMLKRLTQKADCVVVLDDMALNWIATDCMHIQNLSFSQINQLVSTITLASTTILCYLS 429
Cdd:PLN00222 168 TYSVFPNQMETSDVVVQPYNSLLTLKRLTLNADCVVVLDNTALNRIAVDRLHLENPTFAQTNSLVSTVMSASTTTLRYPG 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 430 FMNNDLIGLIASLILTPQFYFLTTDYTPtLTMDQSVANMRKTTVLEVMRWLLQRKSMMV--LTGRDCQTSHCYITILTII 507
Cdd:PLN00222 248 YMNNDLVGLLASLIPTPRCHFLMTGYTP-LTVERQANVIRKTTVLDVMRRLLQTKNIMVssYARTKEASQAKYISILNII 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 508 QGEVDPTQVHKSLQRIQEGKLANFIPWGPASIQVALLRRCSYLPSAQWTSRIIMANHTSISSLFESSCQQFDKLQKWDTF 587
Cdd:PLN00222 327 QGEVDPTQVHKSLQRIRERKLANFIEWGPASIQVALSRKSPYVQTAHRVSGLMLANHTSIRHLFSKCLSQYDKLRKKQAF 406
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1149889000 588 LEEFFKEPMFKDN-FDEMDRSRKVVQEFIDEYHAGTQLDYISWGSQEQ 634
Cdd:PLN00222 407 LDNYRKFPMFADNdLSEFDESREIVESLVDEYKACESPDYIKWGMEDP 454
|
|
| Tubulin_FtsZ_Cetz-like |
cd00286 |
Tubulin protein family of FtsZ and CetZ-like; This family includes tubulin alpha-, beta-, ... |
265-543 |
1.65e-71 |
|
Tubulin protein family of FtsZ and CetZ-like; This family includes tubulin alpha-, beta-, gamma-, delta-, epsilon, and zeta-tubulins as well as FtsZ and CetZ, all of which are involved in polymer formation. Tubulin is the major component of microtubules, but also exists as a heterodimer and as a curved oligomer. Microtubules exist in all eukaryotic cells and are responsible for many functions, including cellular transport, cell motility, and mitosis. FtsZ forms a ring-shaped septum at the site of bacterial cell division, which is required for constriction of cell membrane and cell envelope to yield two daughter cells. FtsZ can polymerize into tubes, sheets, and rings in vitro and is ubiquitous in eubacteria, archaea, and chloroplasts. A recent study found that CetZ proteins, formerly annotated FtsZ type 2, are not required for cell division, whereas FtsZ proteins play an important role. Instead, CetZ proteins are shown to be involved in controlling archaeal cell shape dynamics. The results from inactivation studies of CetZ proteins in Haloferax volcanii suggest that CetZ1 is essential for normal swimming motility and rod-cell development.
Pssm-ID: 276954 [Multi-domain] Cd Length: 332 Bit Score: 234.61 E-value: 1.65e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 265 RRWDKPKNIYLSKHGGGSGNNWISRFSQ-GEKIHEDILDIIDEEADGSDSQRGFVLHYSIAWGTGSGLGSYLLE*LNDRY 343
Cdd:cd00286 41 RQLFHPENIILIQKYHGAGNNWAKGHSVaGEEYQEEILDAIRKEVEECDELQGFFITHSLGGGTGSGLGPLLAERLKDEY 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 344 PMKLVQTYSVFPYQNEMShmVCQPNNSLLMLKRLTQKADCVVVLDDMALNWIATDCMHIQNLSFSQINQLVSTITLASTT 423
Cdd:cd00286 121 PNRLVVTFSILPGPDEGV--IVYPYNAALTLKTLTEHADCLLLVDNEALYDICPRPLHIDAPAYDHINELVAQRLGSLTE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 424 ILCYLSFMNNDLIGLIASLILTPQFYFLTTDYTPtLTMDQSVANmRKTTVLEVMRWLLQRKSMMVltGRDCqTSHCYITI 503
Cdd:cd00286 199 ALRFEGSLNVDLRELAENLVPLPRGHFLMLGYAP-LDSATSATP-RSLRVKELTRRAFLPANLLV--GCDP-DHGEAIAA 273
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1149889000 504 LTIIQGEVD--PTQVHKSLQRIQEGKLANFiPWGPASIQVAL 543
Cdd:cd00286 274 LLVIRGPPDlsSKEVERAIARVKETLGHLF-SWSPAGVKTGI 314
|
|
| Tubulin |
cd06059 |
The tubulin superfamily and related homologs; The tubulin superfamily includes five distinct ... |
269-618 |
7.54e-70 |
|
The tubulin superfamily and related homologs; The tubulin superfamily includes five distinct families, the alpha-, beta-, gamma-, delta-, and epsilon-tubulins and a sixth family (zeta-tubulin) which is present only in kinetoplastid protozoa. The alpha- and beta-tubulins are the major components of microtubules, while gamma-tubulin plays a major role in the nucleation of microtubule assembly. The delta- and epsilon-tubulins are widespread but unlike the alpha, beta, and gamma-tubulins they are not ubiquitous among eukaryotes. The alpha/beta-tubulin heterodimer is the structural subunit of microtubules. The alpha- and beta-tubulins share 40% amino-acid sequence identity, exist in several isotype forms, and undergo a variety of posttranslational modifications. The structures of alpha- and beta-tubulin are basically identical: each monomer is formed by a core of two beta-sheets surrounded by alpha-helices. The monomer structure is very compact, but can be divided into three regions based on function: the amino-terminal nucleotide-binding region, an intermediate taxol-binding region and the carboxy-terminal region which probably constitutes the binding surface for motor proteins. Also included in this group is the mitochondrial Misato/DML1 protein family, involved in mitochondrial fusion and in mitochondrial distribution and morphology.
Pssm-ID: 276963 [Multi-domain] Cd Length: 387 Bit Score: 232.09 E-value: 7.54e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 269 KPKNIYLSKHGggSGNNWISRFSQ-GEKIHEDILDIIDEEADGSDSQRGFVLHYSIAWGTGSGLGSYLLE*LNDRYPMKL 347
Cdd:cd06059 47 DPNQFVTGVSG--AGNNWAVGYYVyGPKYIESILDRIRKQVEKCDSLQGFFILHSLGGGTGSGLGSYLLELLEDEYPKVY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 348 VQTYSVFPYqNEMSHMVCQPNNSLLMLKRLTQKADCVVVLDDMALNWIATD---CMHIQNLSFSQINQLVSTITLASTTI 424
Cdd:cd06059 125 RFTFSVFPS-PDDDNVITSPYNSVLALNHLTEHADCVLPIDNEALYDICNRqpaTLDIDFPPFDDMNNLVAQLLSSLTSS 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 425 LCYLSFMNNDLIGLIASLILTPQFYFLTTDYTPtLTMDQSVaNMRKTTVLEVMRWLLQRKSMMVltgRDCQTSHCYITIL 504
Cdd:cd06059 204 LRFEGSLNVDLNEITTNLVPFPRLHFLLPSLSP-LTSANDV-TLEPLTLDQLFSDLFSKDNQLV---GCDPRHGTYLACA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 505 TIIQGEV-DPTQVHKSLQRIQEGKlaNFIPWGPASIQVALlrrCSYLPSAQWTSRIIMANHTSISSLFESSCQQFDKLQK 583
Cdd:cd06059 279 LLLRGKVfSLSDVRRNIDRIKPKL--KFISWNPDGFKVGL---CSVPPVGQKYSLLFLSNNTSIASTFERLIERFDKLYK 353
|
330 340 350
....*....|....*....|....*....|....*
gi 1149889000 584 WDTFLEEFFKEPMFKDNFDEmdrSRKVVQEFIDEY 618
Cdd:cd06059 354 RKAFLHHYTGEGMEEGDFSE---ARESLANLIQEY 385
|
|
| beta_tubulin |
cd02187 |
The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ... |
281-618 |
3.32e-49 |
|
The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, beta-, gamma-, delta-, and epsilon-tubulins and a sixth family (zeta-tubulin) which is present only in kinetoplastid protozoa. The alpha- and beta-tubulins are the major components of microtubules, while gamma-tubulin plays a major role in the nucleation of microtubule assembly. The delta- and epsilon-tubulins are widespread but unlike the alpha, beta, and gamma-tubulins they are not ubiquitous among eukaryotes. The alpha/beta-tubulin heterodimer is the structural subunit of microtubules. The alpha- and beta-tubulins share 40% amino-acid sequence identity, exist in several isotype forms, and undergo a variety of posttranslational modifications. The structures of alpha- and beta-tubulin are basically identical: each monomer is formed by a core of two beta-sheets surrounded by alpha-helices. The monomer structure is very compact, but can be divided into three regions based on function: the amino-terminal nucleotide-binding region, an intermediate taxol-binding region and the carboxy-terminal region which probably constitutes the binding surface for motor proteins.
Pssm-ID: 276956 [Multi-domain] Cd Length: 425 Bit Score: 177.76 E-value: 3.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 281 GSGNNW-ISRFSQGEKIHEDILDIIDEEADGSDSQRGFVLHYSIAWGTGSGLGSYLLE*LNDRYPMKLVQTYSVFPyQNE 359
Cdd:cd02187 95 GAGNNWaKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGLGTLLLSKLREEYPDRIMSTFSVLP-SPK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 360 MSHMVCQPNNSLLMLKRLTQKADCVVVLDDMALNWIATDCMHIQNLSFSQINQLVSTITLASTTILCYLSFMNNDLIGLI 439
Cdd:cd02187 174 VSDTVVEPYNAVLSLHQLVENADETFCIDNEALYNICQRTLKLTQPTYDDLNHLISQVMSGITSSLRFPGQLNSDLRKLA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 440 ASLILTPQFYFLTTDYTPtLTMDQSVANmRKTTVLEVMRWLLQRKSMMVltgrDCQTSHC-YITILTIIQGEVDPTQVHK 518
Cdd:cd02187 254 TNLVPFPRLHFLTPGFAP-LTSRGSQQY-RKLTVPELTQQLFDAKNMMA----ACDPRHGrYLTAAAIFRGRISTKEVDE 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 519 SLQRIQEGKLANFIPWGPASIQVALlrrCSYLPSAQWTSRIIMANHTSISSLFESSCQQFDKLQKWDTFLEEFFKEPMfk 598
Cdd:cd02187 328 QMSKVQNKNSSYFVEWIPNNVKTSV---CDIPPRGLKMSATFIGNSTAIQELFKRLSEQFTAMFRRKAFLHWYTGEGM-- 402
|
330 340
....*....|....*....|..
gi 1149889000 599 dnfDEMD--RSRKVVQEFIDEY 618
Cdd:cd02187 403 ---DEMEftEAESNLNDLISEY 421
|
|
| PTZ00010 |
PTZ00010 |
tubulin beta chain; Provisional |
269-618 |
1.79e-39 |
|
tubulin beta chain; Provisional
Pssm-ID: 240228 [Multi-domain] Cd Length: 445 Bit Score: 151.08 E-value: 1.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 269 KPKNIYLSKhgGGSGNNW-ISRFSQGEKIHEDILDIIDEEADGSDSQRGFVLHYSIAWGTGSGLGSYLLE*LNDRYPMKL 347
Cdd:PTZ00010 86 RPDNFIFGQ--SGAGNNWaKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQITHSLGGGTGSGMGTLLISKLREEYPDRI 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 348 VQTYSVFPyQNEMSHMVCQPNNSLLMLKRLTQKADCVVVLDDMALNWIATDCMHIQNLSFSQINQLVSTITLASTTILCY 427
Cdd:PTZ00010 164 MMTFSVFP-SPKVSDTVVEPYNATLSVHQLVENADESMCIDNEALYDICFRTLKLTTPTYGDLNHLVSAVMSGVTCCLRF 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 428 LSFMNNDLIGLIASLILTPQFYFLTTDYTPtLTMDQSvANMRKTTVLEVMRWLLQRKSMMVLTgrDCQTSHcYITILTII 507
Cdd:PTZ00010 243 PGQLNSDLRKLAVNLVPFPRLHFFMMGFAP-LTSRGS-QQYRGLSVPELTQQMFDAKNMMCAA--DPRHGR-YLTASALF 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 508 QGEVDPTQVHKSLQRIQEGKLANFIPWGPASIQVALlrrCSYLPSAQWTSRIIMANHTSISSLFESSCQQFDKLQKWDTF 587
Cdd:PTZ00010 318 RGRMSTKEVDEQMLNVQNKNSSYFVEWIPNNIKSSV---CDIPPKGLKMSVTFIGNSTAIQEMFRRVGEQFTAMFRRKAF 394
|
330 340 350
....*....|....*....|....*....|...
gi 1149889000 588 LEEFFKEPMfkdnfDEMD--RSRKVVQEFIDEY 618
Cdd:PTZ00010 395 LHWYTGEGM-----DEMEftEAESNMNDLVSEY 422
|
|
| alpha_tubulin |
cd02186 |
The alpha-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ... |
282-620 |
3.03e-39 |
|
The alpha-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, beta-, gamma-, delta-, and epsilon-tubulins and a sixth family (zeta-tubulin) which is present only in kinetoplastid protozoa. The alpha- and beta-tubulins are the major components of microtubules, while gamma-tubulin plays a major role in the nucleation of microtubule assembly. The delta- and epsilon-tubulins are widespread but unlike the alpha, beta, and gamma-tubulins they are not ubiquitous among eukaryotes. The alpha/beta-tubulin heterodimer is the structural subunit of microtubules. The alpha- and beta-tubulins share 40% amino-acid sequence identity, exist in several isotype forms, and undergo a variety of posttranslational modifications. The structures of alpha- and beta-tubulin are basically identical: each monomer is formed by a core of two beta-sheets surrounded by alpha-helices. The monomer structure is very compact, but can be divided into three regions based on function: the amino-terminal nucleotide-binding region, an intermediate taxol-binding region and the carboxy-terminal region which probably constitutes the binding surface for motor proteins.
Pssm-ID: 276955 [Multi-domain] Cd Length: 434 Bit Score: 150.00 E-value: 3.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 282 SGNNWIS-RFSQGEKIHEDILDIIDEEADGSDSQRGFVLHYSIAWGTGSGLGSYLLE*LNDRYPMKLVQTYSVFPYqNEM 360
Cdd:cd02186 98 AANNFARgYYTIGKEIIDPVLDRIRKLAEQCDGLQGFLIFHSVGGGTGSGLTSLLLERLSVDYGKKSKLEFSIYPS-PQV 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 361 SHMVCQPNNSLLMLKRLTQKADCVVVLDDMALNWIATDCMHIQNLSFSQINQLVSTITLASTTILCYLSFMNNDLIGLIA 440
Cdd:cd02186 177 STSVVEPYNSVLTTHSLLEHSDCSILLDNEALYDICRRQLDIERPTYTNLNRLIAQVVSSLTASLRFDGALNVDLNEFQT 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 441 SLILTPQFYFLTTDYTPtlTMDQSVANMRKTTVLEVMRWLLQRKSMMVltgrDCQTSHC-YITILTIIQGEVDPTQVHKS 519
Cdd:cd02186 257 NLVPYPRIHFPLVSYAP--IISAEKANHEQLSVQEITNSCFEPANQMV----KCDPRHGkYMACCLLYRGDVVPKDVNAA 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 520 LQRIQEGKLANFIPWGPASIQVALlrrCSYLPSAQWTSRI-------IM-ANHTSISSLFESSCQQFDKLQKWDTFLEEF 591
Cdd:cd02186 331 IATIKTKRTIQFVDWCPTGFKVGI---NYQPPTVVPGSDLakvdrsvCMlANSTAIAEAFQRLDHKFDLLYSKRAFVHWY 407
|
330 340
....*....|....*....|....*....
gi 1149889000 592 FKEPMFKDNFDEmdrSRKVVQEFIDEYHA 620
Cdd:cd02186 408 VGEGMEEGEFSE---AREDLAALEKDYEE 433
|
|
| Tubulin_C |
pfam03953 |
Tubulin C-terminal domain; This family includes the tubulin alpha, beta and gamma chains. ... |
446-575 |
6.87e-38 |
|
Tubulin C-terminal domain; This family includes the tubulin alpha, beta and gamma chains. Members of this family are involved in polymer formation. Tubulins are GTPases. FtsZ can polymerize into tubes, sheets, and rings in vitro and is ubiquitous in eubacteria and archaea. Tubulin is the major component of microtubules. (The FtsZ GTPases have been split into their won family).
Pssm-ID: 397858 [Multi-domain] Cd Length: 125 Bit Score: 136.59 E-value: 6.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 446 PQFYFLTTDYTPTLTMDQsvANMRKTTVLEVMRWLLQRKSMMVltgrDCQTSH-CYITILTIIQGEVDPTQVHKSLQRIQ 524
Cdd:pfam03953 1 PRLHFLLTSYAPLTSANK--ASHEKTSVLDVTRRLFDPKNQMV----SCDPRNgKYMACALLYRGDVSPKDVHRAIQRIK 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1149889000 525 EGKLANFIPWGPASIQVALLRRCSYLPSAQWTSRIIMANHTSISSLFESSC 575
Cdd:pfam03953 75 EKRSAQFVEWCPTGIKVAICSQSPYVVPGSKVSGLMLANTTSIAELFQRLL 125
|
|
| PLN00220 |
PLN00220 |
tubulin beta chain; Provisional |
281-605 |
7.54e-36 |
|
tubulin beta chain; Provisional
Pssm-ID: 215107 [Multi-domain] Cd Length: 447 Bit Score: 140.73 E-value: 7.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 281 GSGNNWI-SRFSQGEKIHEDILDIIDEEADGSDSQRGFVLHYSIAWGTGSGLGSYLLE*LNDRYPMKLVQTYSVFPyQNE 359
Cdd:PLN00220 96 GAGNNWAkGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDRMMLTFSVFP-SPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 360 MSHMVCQPNNSLLMLKRLTQKADCVVVLDDMALNWIATDCMHIQNLSFSQINQLVSTiTLASTTilCYLSF---MNNDLI 436
Cdd:PLN00220 175 VSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPSFGDLNHLISA-TMSGVT--CCLRFpgqLNSDLR 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 437 GLIASLILTPQFYFLTTDYTPtLTMDQSvANMRKTTVLEVMRWLLQRKSMMVLT----GRdcqtshcYITILTIIQGEVD 512
Cdd:PLN00220 252 KLAVNLIPFPRLHFFMVGFAP-LTSRGS-QQYRALTVPELTQQMWDAKNMMCAAdprhGR-------YLTASAMFRGKMS 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 513 PTQVHKSLQRIQEGKLANFIPWGPASIQVALlrrCSYLPSAQWTSRIIMANHTSISSLFESSCQQFDKLQKWDTFLEEFF 592
Cdd:PLN00220 323 TKEVDEQMINVQNKNSSYFVEWIPNNVKSSV---CDIPPKGLKMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYT 399
|
330
....*....|...
gi 1149889000 593 KEPMfkdnfDEMD 605
Cdd:PLN00220 400 GEGM-----DEME 407
|
|
| epsilon_tubulin |
cd02190 |
The epsilon-tubulin family; The tubulin superfamily includes five distinct families, the ... |
280-620 |
4.38e-32 |
|
The epsilon-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, beta-, gamma-, delta-, and epsilon-tubulins and a sixth family (zeta-tubulin) which is present only in kinetoplastid protozoa. The epsilon-tubulins which are widespread but not ubiquitous among eukaryotes play a role in basal body/centriole morphogenesis.
Pssm-ID: 276959 [Multi-domain] Cd Length: 449 Bit Score: 129.67 E-value: 4.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 280 GGSGNNW-ISRFSQGEKIHEDILDIIDEEADGSDSQRGFVLHYSIAWGTGSGLGSYLLE*LNDRYPMKLVQTYSVFPYQN 358
Cdd:cd02190 101 SGAGNNWaHGYHEYGPQYGESILEKLRRAAEKCDSLQSFFLLHSLGGGTGSGLGSYILELLEDEFPDVYRFVTSVFPSGD 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 359 EmsHMVCQPNNSLLMLKRLTQKADCVVVLDDMAL-------NWIATDCMHIQNL---------------SFSQINQLVST 416
Cdd:cd02190 181 D--DVITSPYNSVLALRELTEHADCVLPVENQALmdivnkiKSSKDKGKTGVLAainssgggqkkgkkkPFDDMNNIVAN 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 417 ITLASTtilCYLSF---MNNDLIGLIASLILTPQFYFLTTDYTP----------TLTMDQSVANmrkttvlevmrwLLQR 483
Cdd:cd02190 259 LLLNLT---SSMRFegsLNVDLNEITTNLVPFPRLHFLLSSLSPlyaladvrlpPRRLDQMFSD------------AFSR 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 484 KSMMVltgrDCQ-TSHCYITILTIIQGEVDPTQVHKSLQRIQEgKLaNFIPWGPASIQVALlrrCSYLPSAQWTSRIIMA 562
Cdd:cd02190 324 DHQLL----KADpKHGLYLACALLVRGNVSISDLRRNIDRLKR-QL-KFVSWNQDGWKIGL---CSVPPVGQPYSLLCLA 394
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149889000 563 NHTSISSLFESSCQQFDKLQKWDTFL---EEFFKEPMFKDnfdemdrSRKVVQEFIDEYHA 620
Cdd:cd02190 395 NNTCIKPTFTEMHERFDKLYKRKAHLhhyTQYMEQDDFDE-------ALESLLDLIEEYKD 448
|
|
| PTZ00387 |
PTZ00387 |
epsilon tubulin; Provisional |
281-618 |
3.20e-30 |
|
epsilon tubulin; Provisional
Pssm-ID: 240395 [Multi-domain] Cd Length: 465 Bit Score: 124.45 E-value: 3.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 281 GSGNNWISRFSQ-GEKIHEDILDIIDEEADGSDSQRGFVLHYSIAWGTGSGLGSYLLE*LNDRYPMKLVQTYSVFPyqNE 359
Cdd:PTZ00387 97 GAGNNWAVGHMEyGDKYIDSISESVRRQVEQCDSLQSFFLMHSLGGGTGSGLGTRILGMLEDEFPHVFRFCPVVFP--SA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 360 MSHMVCQPNNSLLMLKRLTQKADCVVVLDDMALNWIA---------------------------TDCMHIQNLSFSQINQ 412
Cdd:PTZ00387 175 VDDVITSPYNSFFALRELIEHADCVLPLDNDALANIAdsalsrkkkklakgnikrgpqphkysvAKPTETKKLPYDKMNN 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 413 LVSTITLASTTILCYLSFMNNDLIGLIASLILTPQFYFLTTDYTPTLTMDQSVANMRktTVLEVMRWLLQRKSMMVLTGR 492
Cdd:PTZ00387 255 IVAQLLSNLTSSMRFEGSLNVDINEITTNLVPYPRLHFLTSSIAPLVSLKDVAVGPR--RLDQMFKDCLDPDHQMVAATP 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 493 DcqtSHCYITILTIIQGEVDPTQVHKSLQRIQEGKlaNFIPWGPASIQVALlrrCSYLPSAQWTSRIIMANHTSISSLFE 572
Cdd:PTZ00387 333 E---AGKYLATALIVRGPQNVSDVTRNILRLKEQL--NMIYWNEDGFKTGL---CNVSPLGQPYSLLCLANNCCIRNKFE 404
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1149889000 573 SSCQQFDKLQKWDTFLEEfFKEPMFKDNFDEmdrSRKVVQEFIDEY 618
Cdd:PTZ00387 405 SMLERFNKLYKRKSHVHH-YTEYLEQAYFDE---TLETIQNLIDDY 446
|
|
| delta_zeta_tubulin-like |
cd02189 |
The delta- and zeta-tubulin families; The tubulin superfamily includes five distinct families, ... |
257-620 |
4.07e-29 |
|
The delta- and zeta-tubulin families; The tubulin superfamily includes five distinct families, the alpha-, beta-, gamma-, delta-, and epsilon-tubulins and a sixth family (zeta-tubulin) which is present only in kinetoplastid protozoa. The alpha- and beta-tubulins are the major components of microtubules, while gamma-tubulin plays a major role in the nucleation of microtubule assembly. The delta- and epsilon-tubulins are widespread but unlike the alpha, beta, and gamma-tubulins they are not ubiquitous among eukaryotes. Delta-tubulin plays an essential role in forming the triplet microtubules of centrioles and basal bodies.
Pssm-ID: 276958 [Multi-domain] Cd Length: 433 Bit Score: 120.45 E-value: 4.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 257 EQMKRHWNRRwdkPKNIYLSKhgGGSGNNW-ISRFSQGEKIHEDILDIIDEEADGSDSQRGFVLHYSIAWGTGSGLGSYL 335
Cdd:cd02189 71 RARSGAWSYD---PKNVVCGQ--SGSGNNWaLGYYVHGPSLLEDILEALRREAERCDRLSGFLVLHSLAGGTGSGLGSRV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 336 LE*LNDRYPMKLVQTYSVFPYqnEMSHMVCQPNNSLLMLKRLTQKADCVVVLDDMALNWIATDCMHIQNL-SFSQINQLV 414
Cdd:cd02189 146 TELLRDEYPKAYLLNTVVWPY--SSGEVPVQNYNTLLTLSHLQESSDGILLFENDDLHKICSKLLGLKNPvSFSDINRVI 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 415 S-----------TITLASTTILCYLSFMNNDLIGL----IASLILTPQFYFLTTDYTpTLTMDQSVANMRK-----TTVL 474
Cdd:cd02189 224 ArqlagvllpssSPTSPSPLRRCPLGDLLEHLCPHpaykLLTLRSLPQMPEPSRAFS-TYTWPSLLKRLRQmlitgAKLE 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 475 EVMRWLLQRKSMMvltgrdcQTSHCYITILTIIQGEvDPTQVHKSLQRiQEGKLANFIPWGPA--SIQVALLRRCSYLPS 552
Cdd:cd02189 303 EGIDWQLLDTSGS-------HNPNKSLAALLVLRGK-DAMKVHSADLS-AFKDPVLYSPWVPNpfNVSVSPRPFNGYEKS 373
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149889000 553 AqwtsrIIMANHTSI----SSLFESSCQQFDKlqkwDTFLEEFFKEPMFKDNFDEmdrSRKVVQEFIDEYHA 620
Cdd:cd02189 374 V-----TLLSNSQNIvgplDSLLEKAWQMFKA----GAYLHQYEKYGVEEEDFLD---AFATLEQIIAAYKS 433
|
|
| Tubulin |
pfam00091 |
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ... |
251-393 |
1.01e-27 |
|
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma chains, as well as the bacterial FtsZ family of proteins. Members of this family are involved in polymer formation. FtsZ is the polymer-forming protein of bacterial cell division. It is part of a ring in the middle of the dividing cell that is required for constriction of cell membrane and cell envelope to yield two daughter cells. FtsZ and tubulin are GTPases. FtsZ can polymerize into tubes, sheets, and rings in vitro and is ubiquitous in eubacteria and archaea. Tubulin is the major component of microtubules.
Pssm-ID: 459669 [Multi-domain] Cd Length: 190 Bit Score: 110.39 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 251 DTSA-HLEQMKRHWNrrwdkPKNIYLSKhgGGSGNNW-ISRFSQGEKIHEDILDIIDEEADGSDSQRGFVLHYSIAWGTG 328
Cdd:pfam00091 51 DTDPqALNEIKAGFN-----PNKILLGK--EGTGGNGaGGYPEIGREAAEESLEEIRKEVEGCDMLQGFFITASLGGGTG 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149889000 329 SGLGSYLLE*LNDRYPMKLVQTYSVFPYqnEMSHMVCQPNNSLLMLKRLTQKADCVVVLDDMALN 393
Cdd:pfam00091 124 SGAAPVIAEILKELYPGALTVAVVTFPF--GFSEGVVRPYNAILGLKELIEHSDSVIVIDNDALY 186
|
|
| PLN00221 |
PLN00221 |
tubulin alpha chain; Provisional |
290-603 |
4.10e-26 |
|
tubulin alpha chain; Provisional
Pssm-ID: 177802 Cd Length: 450 Bit Score: 111.82 E-value: 4.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 290 FSQGEKIHEDILDIIDEEADGSDSQRGFVLHYSIAWGTGSGLGSYLLE*LNDRYPMKLVQTYSVFPyQNEMSHMVCQPNN 369
Cdd:PLN00221 108 YTIGKEIVDLCLDRIRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTVYP-SPQVSTAVVEPYN 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 370 SLLMLKRLTQKADCVVVLDDMALNWIATDCMHIQNLSFSQINQLVSTITLASTTILCYLSFMNNDLIGLIASLILTPQFY 449
Cdd:PLN00221 187 SVLSTHSLLEHTDVAVLLDNEAIYDICRRSLDIERPTYTNLNRLISQVISSLTASLRFDGALNVDITEFQTNLVPYPRIH 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 450 FLTTDYTPTLTMDQsvANMRKTTVLEVMRWLLQRKSMMVltgrDCQTSHC-YITILTIIQGEVDPTQVHKSLQRIQEGKL 528
Cdd:PLN00221 267 FMLSSYAPVISAEK--AYHEQLSVAEITNSAFEPASMMA----KCDPRHGkYMACCLMYRGDVVPKDVNAAVATIKTKRT 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 529 ANFIPWGPASIQVALlrrcSYLPS--------AQWTSRIIM-ANHTSISSLFESSCQQFDKLQKWDTFLEEFFKEPMFKD 599
Cdd:PLN00221 341 IQFVDWCPTGFKCGI----NYQPPtvvpggdlAKVQRAVCMiSNSTAVAEVFSRIDHKFDLMYAKRAFVHWYVGEGMEEG 416
|
....
gi 1149889000 600 NFDE 603
Cdd:PLN00221 417 EFSE 420
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
46-266 |
4.42e-14 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 75.98 E-value: 4.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 46 LLSKYEADAIQRTEELEEAKKKLAEKDKEYTNLRRNHQRAHNEALRLKKKIEGDLNDLELQLGHATHQAIEAQVATRLVQ 125
Cdd:pfam01576 725 LKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQ 804
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 126 AQLKEEQAGRDKEQQLAAELQEQAQALECRAALLASELEDLWATLEQGEHSWRLAEQELLEATECLNLLHLQNTGLLNQK 205
Cdd:pfam01576 805 AQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEK 884
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149889000 206 KKLEADLVQLSGEVEEAAQE-RWKAEKAKKAITDAVMMAEELKKEQDTSAHLEQMKRHWNRR 266
Cdd:pfam01576 885 RRLEARIAQLEEELEEEQSNtELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQ 946
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
47-261 |
3.52e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.05 E-value: 3.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 47 LSKYEADAIQRTEELEEAKKKLAEKDKEYTNLRRNHQR------AHNEALRLKKK----IEGDLNDLELQLGHATHQAIE 116
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEEleleleEAQAEEYELLAelarLEQDIARLEERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 117 AQVATRLVQAQLKEEQAGRDKEQQLAAELQEQAQALECRAALLASELEDLWATLEQGEHSWRLAEQELLEATECLNLLHL 196
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149889000 197 QNTGLLNQKKKLEADLVQLSGEVEEAAQERWKAEKAKKAITDAVmmAEELKKEQDTSAHLEQMKR 261
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL--EEAAEEEAELEEEEEALLE 463
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
41-261 |
5.89e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.20 E-value: 5.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 41 LLGWDLLskyEADAIQRTEELEEAKKKLAEKDKEYTNLRRNHQRAHNEALRLKKKIE---GDLNDLELQLGHATHQAIEA 117
Cdd:COG1196 231 LLKLREL---EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEeaqAEEYELLAELARLEQDIARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 118 QVATRLVQAQLKEEQAGRDKEQQLAAELQEQAQALECRAALLASELEDLWATLEQGEHSWRLAEQELLEATECLNLLHLQ 197
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149889000 198 NTGLLNQKKKLEADLVQLSGEVEEAAQERWKAEKAKKAITDAVmmAEELKKEQDTSAHLEQMKR 261
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL--AELEEEEEEEEEALEEAAE 449
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
47-259 |
3.23e-11 |
|
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: 66.62 E-value: 3.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 47 LSKYEADAIQRTEELEEAKKKLAEKDKEYTNLRRNHQRAHNEALRLKKK---IEGDLNDLELQLGHATHQAIEAQVATRL 123
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyaLANEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 124 VQAQLKEEQAGRDKEQQLAAELQEQAQALECRAALLASELEDLWATLEQGEHSWRLAEQELLEATECLNLLHLQNTGLLN 203
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1149889000 204 QKKKLEADLVQLSGEVEEAAQERWKAEKA--KKAITDAVMMAEELKKEQ-DTSAHLEQM 259
Cdd:TIGR02168 401 EIERLEARLERLEDRRERLQQEIEELLKKleEAELKELQAELEELEEELeELQEELERL 459
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
51-251 |
3.12e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.42 E-value: 3.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 51 EADAIQRTEELEEAKKKLAEKDKEYTNLRRNHQRAHNEALRLKKKIEgdlnDLELQLGHATHQAIEAQVATRLVQAQLKE 130
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELE----ELRLELEELELELEEAQAEEYELLAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 131 EQAGRDKEQQLAAELQEQAQALECRAALLASELEDLWATLEQGEHSWRLAEQELLEATEclnLLHLQNTGLLNQKKKLEA 210
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA---ELAEAEEALLEAEAELAE 376
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1149889000 211 DLVQLSGEVEEAAQERWKAEKAKKAITDAVMMAEELKKEQD 251
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
49-315 |
6.06e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.85 E-value: 6.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 49 KYEADAIQRTEELEEA--KKKLAEKDKEYTnlRRNHQRAHNEALRL--KKKIEGDLNDLELQLGHATHQAIEAQVAtRLV 124
Cdd:PTZ00121 1545 KKKADELKKAEELKKAeeKKKAEEAKKAEE--DKNMALRKAEEAKKaeEARIEEVMKLYEEEKKMKAEEAKKAEEA-KIK 1621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 125 QAQLKEEQAGRDKEQQLAAELQEQAQalecRAALLASELEDLWATLEQGEhswRLAEQELLEATEClnllhlqntgllnq 204
Cdd:PTZ00121 1622 AEELKKAEEEKKKVEQLKKKEAEEKK----KAEELKKAEEENKIKAAEEA---KKAEEDKKKAEEA-------------- 1680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 205 kKKLEADLVQLSGEVEEAAQERWKAEKAKKAITDAVMMAEELKK-EQDTSAHLEQMKRHWNRrwDKPKNIYLSKHGGGS- 282
Cdd:PTZ00121 1681 -KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKaEEENKIKAEEAKKEAEE--DKKKAEEAKKDEEEKk 1757
|
250 260 270
....*....|....*....|....*....|....*
gi 1149889000 283 --GNNWISRFSQGEKIHEDILDIIDEEADGSDSQR 315
Cdd:PTZ00121 1758 kiAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKR 1792
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
45-265 |
8.33e-10 |
|
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: 62.38 E-value: 8.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 45 DLLSKYEADAIQRTEELEEAKKKLAEKDKEYTNLRRNHQRAHNEALRLKKKIEGDLNDLE-----LQLGHATHQAIEAQV 119
Cdd:TIGR02168 712 EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEeaeeeLAEAEAEIEELEAQI 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 120 ATRLVQA-----QLKEEQAGRDKEQQLAAELQEQAQALECRAALLASELEDLWATLEQGEHSWRLAEQELLEATECLNLL 194
Cdd:TIGR02168 792 EQLKEELkalreALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL 871
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149889000 195 HLQNTGLLNQKKKLEADLVQLSGEVEEAAQERWKAEKAKKAITDAvmmAEELKKeqdtsaHLEQMKRHWNR 265
Cdd:TIGR02168 872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE---LEELRE------KLAQLELRLEG 933
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
49-261 |
1.26e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.61 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 49 KYEADAIQRTEE---LEEAKKKlAEKDKEYTNLRRNHQRAHNEALRLKKKIEGDLNDLELQLGHATHQAIEAQVATRLVQ 125
Cdd:PTZ00121 1289 KKKADEAKKAEEkkkADEAKKK-AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE 1367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 126 A-QLKEEQAGRD--------KEQQLAAELQEQAQALECRAALL--ASELEDLWATLEQGEHSWRLAEQELLEATECLNLL 194
Cdd:PTZ00121 1368 AaEKKKEEAKKKadaakkkaEEKKKADEAKKKAEEDKKKADELkkAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKAD 1447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149889000 195 HLQNTGllNQKKKLE-----ADLVQLSGEVEEAAQERWKAEKAKKAITDAVMMAEELKKEQDTSAHLEQMKR 261
Cdd:PTZ00121 1448 EAKKKA--EEAKKAEeakkkAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKK 1517
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
48-277 |
2.24e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 48 SKYEADAIQRTEE----LEEAKKKlAEKDKEYTNLRRNHQRAHNEALRLKKKIEgdlndlelQLGHATHQAIEAQVATRL 123
Cdd:PTZ00121 1376 AKKKADAAKKKAEekkkADEAKKK-AEEDKKKADELKKAAAAKKKADEAKKKAE--------EKKKADEAKKKAEEAKKA 1446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 124 VQAQLKEEQAGRDKEQQLAAELQEQAQALECRA--ALLASELEdlwatlEQGEHSWRLAEqELLEATEclnllhlqntgl 201
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAeeAKKADEAK------KKAEEAKKKAD-EAKKAAE------------ 1507
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149889000 202 lNQKKKLEADLVQLSGEVEEA--AQERWKAEKAKKAitDAVMMAEELKKEQDTSAHLEQMKRHWNRRWDKPKNIYLSK 277
Cdd:PTZ00121 1508 -AKKKADEAKKAEEAKKADEAkkAEEAKKADEAKKA--EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRK 1582
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
51-257 |
2.63e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 51 EADAIQRTEELEEAKKKLAEKDKEYTNLRRNHQRAHNEALRLKKKIEGDLNDLELQLGHATHQAIEAQVATRLVQAQLKE 130
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 131 EQAGRDKEQQLAAELQEQAQALECRAALLASELEDLWATLEQGEHswrlAEQELLEATECLNLLHLQNTGLLNQKKKLEA 210
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE----LLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1149889000 211 DLVQLSGEVEEAAQERWKAEKAKKAITDAVMMAEELKKEQDTSAHLE 257
Cdd:COG1196 499 AEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA 545
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
3-261 |
6.67e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 6.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 3 KVALITQKPEESPYDFYERLWGHQIRHETVYMPDCPVPLLGWDLLSKYEADAIQRTEE---------------LEEAKKK 67
Cdd:PTZ00121 1231 KAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEkkkadeakkaeekkkADEAKKK 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 68 lAEKDKEYTNLRRNHQRAHNEALRLKKKIEGDLNDLELQLGHATHQAIEAQVATRLVQAQLKEEQAGRDKEQQLAAELQE 147
Cdd:PTZ00121 1311 -AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE 1389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 148 QAQALECRAAllASELEDLWATLEQGEHSWRLAEQELLEATECLNLLHLQNTGllNQKKKLEadlvqlsgEVEEAAQERW 227
Cdd:PTZ00121 1390 KKKADEAKKK--AEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKA--EEAKKAD--------EAKKKAEEAK 1457
|
250 260 270
....*....|....*....|....*....|....
gi 1149889000 228 KAEKAKKAITDAvMMAEELKKEQDTSAHLEQMKR 261
Cdd:PTZ00121 1458 KAEEAKKKAEEA-KKADEAKKKAEEAKKADEAKK 1490
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
49-261 |
6.90e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 6.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 49 KYEADAIQRTEEL----EEAKKKL------AEKDKEYTNLRRNHQRAHNEALRL---KKKIEgdlndlELQLGHATHQAI 115
Cdd:PTZ00121 1476 KKKAEEAKKADEAkkkaEEAKKKAdeakkaAEAKKKADEAKKAEEAKKADEAKKaeeAKKAD------EAKKAEEKKKAD 1549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 116 EAQVATRLVQAQ--LKEEQAGRDKEQQL-----AAELQEQAQALECRAALLASELEDLWATLEQGEHSWRLAEQELLEAT 188
Cdd:PTZ00121 1550 ELKKAEELKKAEekKKAEEAKKAEEDKNmalrkAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 189 ECLNLLHLQNTGLLNQKKKLE-------ADLVQLSGEVEEAAQERWKAEKAKKAITDAVMMAEELKKEQDTSAHLEQMKR 261
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEelkkaeeENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKK 1709
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
51-234 |
8.21e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 8.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 51 EADAIQRTEELEEAKKKLAEKDKEytnlRRNHQRAHNEALRLKKKIEGDLNDLELQLGHATHQAIEAQvaTRLVQAQLKE 130
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAE----LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA--AQLEELEEAE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 131 EQAGRDKEQQLAAELQEQAQALECRAALLASELEdlwatlEQGEHSWRLAEQELLEATEclnllhLQNTGLLNQKKKLEA 210
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEA------LEEAAEEEAELEEEEEALL------ELLAELLEEAALLEA 477
|
170 180
....*....|....*....|....
gi 1149889000 211 DLVQLSGEVEEAAQERWKAEKAKK 234
Cdd:COG1196 478 ALAELLEELAEAAARLLLLLEAEA 501
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
55-268 |
1.96e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 55 IQRTEE-LEEAKKKLAEKDKEYTNLRRnhQRahnEALRLKKKIEGDLNDLELQLghathqaieAQVATRLVQAQLKEEQA 133
Cdd:COG1196 181 LEATEEnLERLEDILGELERQLEPLER--QA---EKAERYRELKEELKELEAEL---------LLLKLRELEAELEELEA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 134 GRDKEQQLAAELQEQAQALECRAALLASELEDLWATLEQGEHSWRLAEQELLEATECLNLLHLQNTGLLNQKKKLEADLV 213
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1149889000 214 QLSGEVEEAAQERWKAEKAKKAITDAV-MMAEELKKEQDTSAHLEQMKRHWNRRWD 268
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELeEAEAELAEAEEALLEAEAELAEAEEELE 382
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
51-245 |
7.19e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 7.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 51 EADAIQRTEELEEAKKKLAEKDKEYTNLRRNHQRAHNEALRLKKKIEgDLNDLELQLghatHQAIEAQVATRLvqAQLKE 130
Cdd:COG4913 273 ELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLD-ALREELDEL----EAQIRGNGGDRL--EQLER 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 131 EQAGRDKE----QQLAAELQEQAQALECRAALlasELEDLWATLEQgehswrlAEQELLEATECLNLLHLQNTGLLNQKK 206
Cdd:COG4913 346 EIERLEREleerERRRARLEALLAALGLPLPA---SAEEFAALRAE-------AAALLEALEEELEALEEALAEAEAALR 415
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1149889000 207 KLEADLVQLSGEVEEAAQERW----KAEKAKKAITDAVMMAEE 245
Cdd:COG4913 416 DLRRELRELEAEIASLERRKSnipaRLLALRDALAEALGLDEA 458
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
54-252 |
8.08e-07 |
|
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: 51.69 E-value: 8.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 54 AIQRTEELEEAKKKLAEKDKEYTNLRRNHQRAHNEalrlKKKIEGDLNDLELQLGhathqaieaqVATRLVQAQLKEEQA 133
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIA----------ALARRIRALEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 134 GRDKEQQLAAELQEQAQALECRAALLASELEDLWATLEQGEHSWRLAEQELLEATECLNLLHLQNTGLLNQKKKLEADLV 213
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1149889000 214 QLSGEVEEAAQERWKAEKAKKAITDAVMMAEELKKEQDT 252
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQK 199
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
49-240 |
8.94e-07 |
|
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: 52.37 E-value: 8.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 49 KYEADAIQRTEELEEAKKKLAEKDKEYTNLRRNHQRAHNEALRLKKKIE---GDLNDLELQLG--HATHQAIEAQVaTRL 123
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLEtlrSKVAQLELQIAslNNEIERLEARL-ERL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 124 V--QAQLKEEQAGRDKEQQLAA--ELQEQAQALECRAALLASELEDLWATLEQGEHSWRLAEQELLEATECLNLLHlqnt 199
Cdd:TIGR02168 413 EdrRERLQQEIEELLKKLEEAElkELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ---- 488
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1149889000 200 gllNQKKKLEADLVQLSGEVEEAAQErWKAEKAKKAITDAV 240
Cdd:TIGR02168 489 ---ARLDSLERLQENLEGFSEGVKAL-LKNQSGLSGILGVL 525
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
59-258 |
1.04e-06 |
|
chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 59 EELEEAKKK-------LAEKDKEYTNLR--RNHQRAHNEALRLKKKIEGDLNDLELQLGHATHQAIEAQVATrlvqaqLK 129
Cdd:TIGR02169 177 EELEEVEENierldliIDEKRQQLERLRreREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLAS------LE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 130 EEQAGRDKE-QQLAAELQEQAQALECRAALLASELEDLWATLEQGEHSWRlAEQELLEATECLNLLHLQNtgLLNQKKKL 208
Cdd:TIGR02169 251 EELEKLTEEiSELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELE-AEIASLERSIAEKERELED--AEERLAKL 327
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1149889000 209 EADLVQLSGEVE--EAAQERWKAEKAKkaitdavmMAEELKKEQDTSAHLEQ 258
Cdd:TIGR02169 328 EAEIDKLLAEIEelEREIEEERKRRDK--------LTEEYAELKEELEDLRA 371
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
49-261 |
1.22e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 49 KYEADAIQRTEEL----------EEAKKKLAEKDKEyTNLRRNHQRAhNEALRLKKKIEGDLNDLELQlGHATHQAIEAQ 118
Cdd:PTZ00121 1424 KKKAEEKKKADEAkkkaeeakkaDEAKKKAEEAKKA-EEAKKKAEEA-KKADEAKKKAEEAKKADEAK-KKAEEAKKKAD 1500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 119 VATRLVQAQLKEEQAGRDKEQQLAAEL---QEQAQALECRAALLASELEDLWAT--LEQGEHSwRLAEQELLEatECLNL 193
Cdd:PTZ00121 1501 EAKKAAEAKKKADEAKKAEEAKKADEAkkaEEAKKADEAKKAEEKKKADELKKAeeLKKAEEK-KKAEEAKKA--EEDKN 1577
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149889000 194 LHLQNTGLLNQKKKLEADLVQLSGEVEeaaqERWKAEKAKKAiTDAVMMAEELKKEQDTSAHLEQMKR 261
Cdd:PTZ00121 1578 MALRKAEEAKKAEEARIEEVMKLYEEE----KKMKAEEAKKA-EEAKIKAEELKKAEEEKKKVEQLKK 1640
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
40-232 |
2.11e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 40 PLLGWD---LLSKYEADAIQRTEELEEAKKKLAEKDKEYTNLRRnhQRAHNEALRlkkkiEGDLNDLELQLGHATHQAIE 116
Cdd:COG4913 602 YVLGFDnraKLAALEAELAELEEELAEAEERLEALEAELDALQE--RREALQRLA-----EYSWDEIDVASAEREIAELE 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 117 AQVAT--------RLVQAQLKEEQAGRDKEQQLAAELQEQAQALECRAALLASELEDLWATLEQGEHSWRLAEQELLEAt 188
Cdd:COG4913 675 AELERldassddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE- 753
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1149889000 189 eclnllHLQNTGLLNQKKKLEAdlvQLSGEVEEAAQERWKAEKA 232
Cdd:COG4913 754 ------RFAAALGDAVERELRE---NLEERIDALRARLNRAEEE 788
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
55-234 |
8.14e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 8.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 55 IQRTEELEEAKKKLAEKDKEYTNLRRNHQRAHNEALRLKKKIE---GDLNDLELQLGHATHQAIEAQVATRLVQAQLKEE 131
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEelrEELEKLEKLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 132 QAgRDKEQQLaAELQEQAQALECRAALLASELEDLWATLEQGehswrlAEQELLEATECLNLLHLQNTGLLNQKKKLEAD 211
Cdd:COG4717 150 EL-EERLEEL-RELEEELEELEAELAELQEELEELLEQLSLA------TEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
170 180
....*....|....*....|...
gi 1149889000 212 LVQLSGEVEEAAQERWKAEKAKK 234
Cdd:COG4717 222 LEELEEELEQLENELEAAALEER 244
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
43-248 |
9.16e-06 |
|
chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.91 E-value: 9.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 43 GWDLLSKYEA-----DAIQR-----TEELEEAKKKLAEKDKEYTNL--------RRNHQRAHNEALRLKKKIEgdlnDLE 104
Cdd:TIGR02169 225 GYELLKEKEAlerqkEAIERqlaslEEELEKLTEEISELEKRLEEIeqlleelnKKIKDLGEEEQLRVKEKIG----ELE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 105 LQLGHATHQAIEAQVATRLVQAQLKEEQAGRDKEQ----QLAAELQEQA---QALECRAALLASELEDLWATLEQGEHSW 177
Cdd:TIGR02169 301 AEIASLERSIAEKERELEDAEERLAKLEAEIDKLLaeieELEREIEEERkrrDKLTEEYAELKEELEDLRAELEEVDKEF 380
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149889000 178 RLAEQELLEATECLNLLHLQNTGLLNQKKKLEADLVQLSGEVEEAAQERWKAEKAKKA-ITDAVMMAEELKK 248
Cdd:TIGR02169 381 AETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINElEEEKEDKALEIKK 452
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
51-261 |
2.14e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 51 EADAIQRTEELEEAKKKLAEKDKEYTNLRRNHQRAHNEALRLKKKIEGDLNDLElqlghatHQAIEAQVATRLVQAQLKE 130
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA-------ELEEEEEEEEEALEEAAEE 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 131 EQAGRDKEQQLAAELQEQAQALECRAALLASELEDLWATLEQGEHSWRLAEQELLEATECLNLLHLQNTGLLNQKKKLEA 210
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLI 530
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1149889000 211 DLVQLSGEVEEAAQERWKAEKAKKAITDAVMMAEELKKEQD---TSAHLEQMKR 261
Cdd:COG1196 531 GVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgraTFLPLDKIRA 584
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
60-225 |
3.49e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 60 ELEEAKKKLAEKDKEYTNLRRNHQRAHNEALRLKKKIEgdlnDLELQLGHATHQAIEAQVATRLVQAQLKEEQ----AGR 135
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELE----QAEEELDELQDRLEAAEDLARLELRALLEERfaaaLGD 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 136 DKEQQLAAELQEQAQALECRAALLASELEDLwatLEQGEHSWRLAEQELL----EATECLNLLH-LQNTGLLNQKKKL-- 208
Cdd:COG4913 762 AVERELRENLEERIDALRARLNRAEEELERA---MRAFNREWPAETADLDadleSLPEYLALLDrLEEDGLPEYEERFke 838
|
170 180
....*....|....*....|...
gi 1149889000 209 ------EADLVQLSGEVEEAAQE 225
Cdd:COG4913 839 llnensIEFVADLLSKLRRAIRE 861
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
60-265 |
5.61e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.65 E-value: 5.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 60 ELEEAK-KKLAEKDKEYTNLRRNHQRAHNEALRlkkkiegDLnDLELQLGHATHQAIEAQVATRLVQAQLKEE---QAGR 135
Cdd:pfam15921 195 DFEEASgKKIYEHDSMSTMHFRSLGSAISKILR-------EL-DTEISYLKGRIFPVEDQLEALKSESQNKIElllQQHQ 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 136 DKEQQLAAE-------LQEQAQALECRAALLASELEdLWATLEQGEHSWRLAEQELLEATECLNLLHLQNTGLLNQKK-- 206
Cdd:pfam15921 267 DRIEQLISEheveitgLTEKASSARSQANSIQSQLE-IIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKie 345
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149889000 207 KLEADLVQLSGEVEEAAQERWKAEKAKKAITDAV--MMAEELKKEQDTSAHLEQMKRHWNR 265
Cdd:pfam15921 346 ELEKQLVLANSELTEARTERDQFSQESGNLDDQLqkLLADLHKREKELSLEKEQNKRLWDR 406
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
91-235 |
7.27e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.34 E-value: 7.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 91 RLKKKIeGDLNDLeLQLGHATHQAIEAQVATrlVQAQLKEEQAGRDKEQQLAAELQEQAQALECRAALLASELEDlwatl 170
Cdd:PRK09039 57 RLNSQI-AELADL-LSLERQGNQDLQDSVAN--LRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDS----- 127
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149889000 171 eqgehswrlAEQELLEATECLNLLHLQNTGLLNQKKKLEADLvqlsgeveEAAQERWKAEKAKKA 235
Cdd:PRK09039 128 ---------EKQVSARALAQVELLNQQIAALRRQLAALEAAL--------DASEKRDRESQAKIA 175
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
59-248 |
9.60e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 9.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 59 EELEEAKKKLAEKDKEYTNLRRNHQRAHNEALRLKKKIEGDLNDLELQLGHATHQAIEAQVATRLVQAQLKEEQAGRDKE 138
Cdd:PRK03918 549 EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEEL 628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 139 QQLAAELQEQAQALEcraaLLASELEDLWATLEQGEHswRLAEQELLEATECLNLLHLQNTGLLNQKKKLEADLVQLSGE 218
Cdd:PRK03918 629 DKAFEELAETEKRLE----ELRKELEELEKKYSEEEY--EELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE 702
|
170 180 190
....*....|....*....|....*....|
gi 1149889000 219 VEEAAQERWKAEKAKKAITDAVMMAEELKK 248
Cdd:PRK03918 703 LEEREKAKKELEKLEKALERVEELREKVKK 732
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
51-251 |
1.02e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 51 EADAIQRTEE---LEEAKKklAEKDKEYTNLRRNHQ-RAHNEALRLK--KKIEgdlndlelqlghATHQAIEAQVATRLV 124
Cdd:PTZ00121 1129 KAEEARKAEDarkAEEARK--AEDAKRVEIARKAEDaRKAEEARKAEdaKKAE------------AARKAEEVRKAEELR 1194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 125 QAQ--LKEEQAGRDKEQQLAAELQEQAQALECRAALLASELEDLWATLEQGEHSWRLAEQELLEATECLNLLHLQNTGLL 202
Cdd:PTZ00121 1195 KAEdaRKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKA 1274
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1149889000 203 NQKKKLE----------ADLVQLSGEVEEAAQERWKAEKAKKAiTDAVMMAEELKKEQD 251
Cdd:PTZ00121 1275 EEARKADelkkaeekkkADEAKKAEEKKKADEAKKKAEEAKKA-DEAKKKAEEAKKKAD 1332
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
47-207 |
1.35e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 47 LSKYEADAIQRTEELEEAKKKLAEKDKEYTNLRR-----NHQRAHNEALRLKKKIEGDLNDLELQLGHATHQaiEAQVAT 121
Cdd:COG4717 83 AEEKEEEYAELQEELEELEEELEELEAELEELREeleklEKLLQLLPLYQELEALEAELAELPERLEELEER--LEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 122 RLVQAQLKEEQAgRDKEQQLAAELQEQAQALECRAALLASELEDLWATLEQGEHSWRLAEQELLEATEclNLLHLQNTGL 201
Cdd:COG4717 161 LEEELEELEAEL-AELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE--ELEQLENELE 237
|
....*.
gi 1149889000 202 LNQKKK 207
Cdd:COG4717 238 AAALEE 243
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
57-158 |
1.43e-04 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 44.57 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 57 RTEELEEAKKKLAEKDKEYTNLRRNHQRAhnEALRLKKKIEGdlNDLElqlgHATHQAIEAQVATRLVQAQLKEEQAGRD 136
Cdd:PRK03598 105 RDEEIAQARAAVKQAQAAYDYAQNFYNRQ--QGLWKSRTISA--NDLE----NARSSRDQAQATLKSAQDKLSQYREGNR 176
|
90 100
....*....|....*....|...
gi 1149889000 137 KEQQLAAELQ-EQAQALECRAAL 158
Cdd:PRK03598 177 PQDIAQAKASlAQAQAALAQAEL 199
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
48-261 |
2.37e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.40 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 48 SKYEADAIQRTEELEEAKKKLAEKDKEYTNLRRNHQRAHNEALRLKKKIEGdlndlELQLgHATHQAIEAQVATRL---- 123
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQA-----ETEL-CAEAEEMRARLAARKqele 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 124 -----VQAQLKEEQagrDKEQQLAAE---LQEQAQALEcraallaSELEDLWATLEQGEHSWRLAEQELLEATECLNLLH 195
Cdd:pfam01576 75 eilheLESRLEEEE---ERSQQLQNEkkkMQQHIQDLE-------EQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLE 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 196 LQNTGLLNQKKKLEADLVQLS---GEVEEAAQERWKAE-KAKKAITDavmMAEELKKEQDTSAHLEQMKR 261
Cdd:pfam01576 145 DQNSKLSKERKLLEERISEFTsnlAEEEEKAKSLSKLKnKHEAMISD---LEERLKKEEKGRQELEKAKR 211
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
102-225 |
2.64e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 43.50 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 102 DLELQLghathQAIEAQVATrlVQAQLKEEQAGRDKEQQLAAeLQEQAQALECRAALLASEL---EDLWA-------TLE 171
Cdd:COG1566 80 DLQAAL-----AQAEAQLAA--AEAQLARLEAELGAEAEIAA-AEAQLAAAQAQLDLAQRELeryQALYKkgavsqqELD 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1149889000 172 QGEHSWRLAEQELLEATECLNLLHLQNTGlLNQKKKLEADLVQLSGEVEEAAQE 225
Cdd:COG1566 152 EARAALDAAQAQLEAAQAQLAQAQAGLRE-EEELAAAQAQVAQAEAALAQAELN 204
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
104-250 |
2.82e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.64 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 104 ELQLGHATHQAIEAQVATRLVQAQLKEEQAgrDKEQQLAAELQEQA---QALECRAALLASELED--LWATLEQGEhswr 178
Cdd:PRK09510 91 ELQQKQAAEQERLKQLEKERLAAQEQKKQA--EEAAKQAALKQKQAeeaAAKAAAAAKAKAEAEAkrAAAAAKKAA---- 164
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149889000 179 lAEQELLEATEclnllhlqntgllnQKKKLEADLvqlSGEVEEAAQERWKAEKAKKAITDAVMMAEELKKEQ 250
Cdd:PRK09510 165 -AEAKKKAEAE--------------AAKKAAAEA---KKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKK 218
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
59-224 |
3.52e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 59 EELEEAKKKLAEKDKEYTNLRRNHQRAHNEALRLKKKIEGDLNDLELqlGHATHQAIEAQVAT----------RL----V 124
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGL--DDADAEAVEARREEledrdeelrdRLeecrV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 125 QAQLKEEQAGRDKE------------QQLAAELQEQAQALECRAALLASELEDLWATLEQGEHSWRLAEQELLEATECLN 192
Cdd:PRK02224 336 AAQAHNEEAESLREdaddleeraeelREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLE 415
|
170 180 190
....*....|....*....|....*....|..
gi 1149889000 193 LLHLQNTGLLNQKKKLEADLVQLSGEVEEAAQ 224
Cdd:PRK02224 416 ELREERDELREREAELEATLRTARERVEEAEA 447
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
57-265 |
3.58e-04 |
|
chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 57 RTEELE------EAKKKLAEKDKE-------YTNLRRNHQRAHNEALRLK--------KKIEGDLNDLELQLGHATHQAI 115
Cdd:TIGR02169 813 RLREIEqklnrlTLEKEYLEKEIQelqeqriDLKEQIKSIEKEIENLNGKkeeleeelEELEAALRDLESRLGDLKKERD 892
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 116 EAQVATRLVQAQLKEEQAGRDKEQQLAAELQEQAQALECRaallASELEDLWATLEQ---GEHSWRLAEQELLEATECLN 192
Cdd:TIGR02169 893 ELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE----LSEIEDPKGEDEEipeEELSLEDVQAELQRVEEEIR 968
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149889000 193 LLHLQNTGLLNQKKKLEADLVQLSGEVEEAAQERwkaekakKAITDAVMMAEELKKEQDTSAhLEQMKRHWNR 265
Cdd:TIGR02169 969 ALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEER-------KAILERIEEYEKKKREVFMEA-FEAINENFNE 1033
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
45-282 |
3.77e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 45 DLLSKYEADAIQRTEELEEAKKKLaekdkeytNLRRNHQRAHNEALRLKKKIEGDLNDLElqlghATHQAIEA------- 117
Cdd:PRK04863 442 DWLEEFQAKEQEATEELLSLEQKL--------SVAQAAHSQFEQAYQLVRKIAGEVSRSE-----AWDVARELlrrlreq 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 118 -QVATRLVQ--AQLKEEQaGRDKEQQLAAELQEQAQALECRAALLASELEDLwatleQGEHswrlaEQELLEATECLNLL 194
Cdd:PRK04863 509 rHLAEQLQQlrMRLSELE-QRLRQQQRAERLLAEFCKRLGKNLDDEDELEQL-----QEEL-----EARLESLSESVSEA 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 195 HLQNTGLLNQKKKLEADLVQLSGEVEE--AAQERWKA--EKAKKAITDAVM----MAEELKKEQDTSA---HLEQMKRHW 263
Cdd:PRK04863 578 RERRMALRQQLEQLQARIQRLAARAPAwlAAQDALARlrEQSGEEFEDSQDvteyMQQLLERERELTVerdELAARKQAL 657
|
250
....*....|....*....
gi 1149889000 264 NRRWDKpkniyLSKHGGGS 282
Cdd:PRK04863 658 DEEIER-----LSQPGGSE 671
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
45-258 |
3.86e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 45 DLLSKYEADAIQRTEELEEAKKKLAEKDKEYTNLRRNHQRAHNEAL------RLKKKIE---GDLNDLELQLGHATHQAI 115
Cdd:PRK11281 73 DKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLstlslrQLESRLAqtlDQLQNAQNDLAEYNSQLV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 116 EAQVATRLVQAQLKEEQA-----------GRDKEQQLAAELQEQAQA----LECRAALLASELE--DLWATLEQGEHSWR 178
Cdd:PRK11281 153 SLQTQPERAQAALYANSQrlqqirnllkgGKVGGKALRPSQRVLLQAeqalLNAQNDLQRKSLEgnTQLQDLLQKQRDYL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 179 LAEQELLEAteclNLLHLQNtgLLNQKKkleadlVQLSgevEEAAQERWKAEKAKKAITDAVmmaeeLKKEQDTSAHLEQ 258
Cdd:PRK11281 233 TARIQRLEH----QLQLLQE--AINSKR------LTLS---EKTVQEAQSQDEAARIQANPL-----VAQELEINLQLSQ 292
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
45-262 |
3.96e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 45 DLLSKYEADAIQRTEELEEAKKKLAEKDKEYTNLRRnhQRAHNEALRLKKKIEGDLNDLELQLGhaTHQAIEAQVATRLV 124
Cdd:PRK03918 452 ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEK--VLKKESELIKLKELAEQLKELEEKLK--KYNLEELEKKAEEY 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 125 QaQLKEEQAGRDKEQQLAAELQEQAQALECRAALLASELEDLWATLEQGEHswRLAE------QELLEATECLNLLHLQN 198
Cdd:PRK03918 528 E-KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLK--ELEElgfesvEELEERLKELEPFYNEY 604
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149889000 199 TGLLNQKKKLEADLVQLSGEVEEAAQERWKAEKAKKAITDAVMMAEELKKEQDTSAHLEQMKRH 262
Cdd:PRK03918 605 LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEY 668
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
60-236 |
6.94e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 6.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 60 ELEEAKKKLAEKDKEYTNLRRNHQRAHNEALRLKKKIEgdlnDLELQLghathQAIEAQVATrlVQAQLKeeqagRDKEQ 139
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELE----DLEKEI-----KRLELEIEE--VEARIK-----KYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 140 QLAAE-------LQEQAQALECRAALLASELEDLWATLEQGEHSWRLAEQELLEATECLNLLhlqntgllnqKKKLEADL 212
Cdd:COG1579 82 LGNVRnnkeyeaLQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK----------KAELDEEL 151
|
170 180
....*....|....*....|....
gi 1149889000 213 VQLSGEVEEAAQERwkaEKAKKAI 236
Cdd:COG1579 152 AELEAELEELEAER---EELAAKI 172
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
47-240 |
8.11e-04 |
|
chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 8.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 47 LSKYEADAIQRTEELEEAKKKLAEKDKEYTNLRRNHQRAHNEALRLKKKIEG---DLNDLELQLghathqaieaqvaTRL 123
Cdd:TIGR02169 345 IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKlkrEINELKREL-------------DRL 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 124 VQAQLKEEQAGRDKEQQLAAELQEQAQalecraalLASELEDLWATLEQGEhsWRLAE-QELLEATEclnllhlqntgll 202
Cdd:TIGR02169 412 QEELQRLSEELADLNAAIAGIEAKINE--------LEEEKEDKALEIKKQE--WKLEQlAADLSKYE------------- 468
|
170 180 190
....*....|....*....|....*....|....*...
gi 1149889000 203 NQKKKLEADLVQLSGEVEEAAQERWKAEKAKKAITDAV 240
Cdd:TIGR02169 469 QELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
45-230 |
8.43e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.19 E-value: 8.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 45 DLLSKYEADAIQRTEELEEAKKKLAEK--DKEyTNLRRNHQRAhNEALRLKKKIEGDLNDLELQLGHATH---------Q 113
Cdd:pfam07888 118 DALLAQRAAHEARIRELEEDIKTLTQRvlERE-TELERMKERA-KKAGAQRKEEEAERKQLQAKLQQTEEelrslskefQ 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 114 AIEAQVATRLVQA-QLKEE----QAGRDKEQQLAAE----------LQEQAQALECRAALLASELEDL------------ 166
Cdd:pfam07888 196 ELRNSLAQRDTQVlQLQDTittlTQKLTTAHRKEAEnealleelrsLQERLNASERKVEGLGEELSSMaaqrdrtqaelh 275
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 167 WATLEQGEHSWRLAEQELL----EATECLNLLHLQNTGLLNQKK--KLEADLVQLSGEVEEAAQERWKAE 230
Cdd:pfam07888 276 QARLQAAQLTLQLADASLAlregRARWAQERETLQQSAEADKDRieKLSAELQRLEERLQEERMEREKLE 345
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
48-266 |
1.05e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 42.27 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 48 SKYEADAIQRTEELEEAKKKLAEKDKEYTNLRRNHQR-AHNEALRLKKKIEGDLNDLELQLGHATHQAIEAQVATRLVQA 126
Cdd:pfam02463 165 SRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKlKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 127 QLKEEQAGRDKEQQLAAELQEQAQALECRAALLASELEDLWATLEQGEHSWRLAEQELLEATECLNLLHLQNTGLLNQKK 206
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKK 324
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149889000 207 KLEADLVQLSGEVEEAAQERWKAEKAKKAITDAV--MMAEELKKEQDTSAHLEQMKRHWNRR 266
Cdd:pfam02463 325 KAEKELKKEKEEIEELEKELKELEIKREAEEEEEeeLEKLQEKLEQLEEELLAKKKLESERL 386
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
51-237 |
1.17e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 51 EADAIQrtEELEEAKKKLAEKDKEYTNLRRNHQRAHNEALRLKKKIEGdlndlelqlghathqaieaqvatrlVQAQLKE 130
Cdd:COG4372 39 ELDKLQ--EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE-------------------------LNEQLQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 131 EQAGRDKEQQLAAELQEQAQALECRAALLASELEDLWATLEQGEHSWRLAEQELLEATECLNLLHLQNTGLLNQKKKLEA 210
Cdd:COG4372 92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
|
170 180
....*....|....*....|....*..
gi 1149889000 211 DLVQLSGEVEEAAQERWKAEKAKKAIT 237
Cdd:COG4372 172 ELQALSEAEAEQALDELLKEANRNAEK 198
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
113-250 |
1.17e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.72 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 113 QAIEAQVATRLVQAQLKEEQAGRDKEQQLAAELQEQAQALEcrAALLASELEDLWAtleqgEHSWRLAEQELLEATEcln 192
Cdd:PRK09510 82 KKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEE--AAKQAALKQKQAE-----EAAAKAAAAAKAKAEA--- 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1149889000 193 llhlqntgllnQKKKLEAdlvqLSGEVEEAAQERWKAEKAKKAITDAVMMAEELKKEQ 250
Cdd:PRK09510 152 -----------EAKRAAA----AAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAK 194
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
47-254 |
1.30e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 41.95 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 47 LSKYEADAIQRTEELEEAKKKlAEKDKEYTNLRRnhQRAHNEALRLKKKIEGDLndlelqlghathQAIEAQVATRLVQA 126
Cdd:COG3064 18 LEQAEAEKRAAAEAEQKAKEE-AEEERLAELEAK--RQAEEEAREAKAEAEQRA------------AELAAEAAKKLAEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 127 qlkeEQAGRDKEQQLAAELQEQAQALEcraALLASELEDLWATLEQGEHSWRLAEQELLEATEclnllhlqntgllnqKK 206
Cdd:COG3064 83 ----EKAAAEAEKKAAAEKAKAAKEAE---AAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAE---------------EE 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1149889000 207 KLEADLVQLSGEVEEAAQERWKAEKAKKAITDAVMMAEELKKEQDTSA 254
Cdd:COG3064 141 RKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAA 188
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
51-251 |
1.63e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 51 EADAIQRteELEEAKKKLAEKDKEYTNLRRNHqrahnealrlkKKIEGDLNDLELQLghathQAIEAQVATrlVQAQLKe 130
Cdd:COG1579 18 ELDRLEH--RLKELPAELAELEDELAALEARL-----------EAAKTELEDLEKEI-----KRLELEIEE--VEARIK- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 131 eqagRDKEQQLAAELQEQAQALEcraallaSELEDLwaTLEQGEhswrlAEQELLEATEclnllhlQNTGLLNQKKKLEA 210
Cdd:COG1579 77 ----KYEEQLGNVRNNKEYEALQ-------KEIESL--KRRISD-----LEDEILELME-------RIEELEEELAELEA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1149889000 211 DLVQLSGEVEEAAQERwkaEKAKKAITDAVmmaEELKKEQD 251
Cdd:COG1579 132 ELAELEAELEEKKAEL---DEELAELEAEL---EELEAERE 166
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
80-256 |
1.73e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 80 RNHQRAHNEALRLKKKIEgDLNDLElqlghATHQAIEAQVATRLVQAQLKEeqagrdkeqqlAAELQEQAQALEcraaLL 159
Cdd:COG4913 235 DDLERAHEALEDAREQIE-LLEPIR-----ELAERYAAARERLAELEYLRA-----------ALRLWFAQRRLE----LL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 160 ASELEDLWATLEQGEHSWRLAEQELLEATECLNLLH---LQNTGllNQKKKLEADLVQLSGEVEEAAQERWKAEKAKKAI 236
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEaqiRGNGG--DRLEQLEREIERLERELEERERRRARLEALLAAL 371
|
170 180
....*....|....*....|.
gi 1149889000 237 T-DAVMMAEELKKEQDTSAHL 256
Cdd:COG4913 372 GlPLPASAEEFAALRAEAAAL 392
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
56-249 |
1.99e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 41.01 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 56 QRTEELEEAKKKLAEKDKEYTNLRRNHQRAHNEAlRLKKKIEgdlndlelqlgHATHQAIEAQVATRLVQAQLKEEQAGR 135
Cdd:COG2268 193 KIAEIIRDARIAEAEAERETEIAIAQANREAEEA-ELEQERE-----------IETARIAEAEAELAKKKAEERREAETA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 136 DKEQQLAAELQEQAQALECRAALLASELedlwatleqgEHSWRLAEQELLEAteclnllhlqntgllnqKKKLEADlVQL 215
Cdd:COG2268 261 RAEAEAAYEIAEANAEREVQRQLEIAER----------EREIELQEKEAERE-----------------EAELEAD-VRK 312
|
170 180 190
....*....|....*....|....*....|....*
gi 1149889000 216 SGEVE-EAAQERWKAEkAKKAITDAVMMAEELKKE 249
Cdd:COG2268 313 PAEAEkQAAEAEAEAE-AEAIRAKGLAEAEGKRAL 346
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
52-258 |
2.41e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 52 ADAIQRTEELEEAKKKLAEKDKEYTNLRRNHQRAHNEALRLKKKI----EGDLNDLELQLGHATHQAIEAQVATRLVQAQ 127
Cdd:COG4717 142 AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 128 LK--EEQAGRDKEQQLAAELQEQAQALECRAALLASELEDLWATLEQGEHSWRLAEQELLEATeclnLLHLQNTGLLNQK 205
Cdd:COG4717 222 LEelEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLG----LLALLFLLLAREK 297
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149889000 206 KKLEADL--VQLSGEVEEAAQERWKAEKAK---------KAITDAVMMAEELKKEQDTSAHLEQ 258
Cdd:COG4717 298 ASLGKEAeeLQALPALEELEEEELEELLAAlglppdlspEELLELLDRIEELQELLREAEELEE 361
|
|
| CCDC154 |
pfam15450 |
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that ... |
76-228 |
2.78e-03 |
|
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that suppresses cell proliferation by inducing G2/M arrest.
Pssm-ID: 464723 [Multi-domain] Cd Length: 526 Bit Score: 40.59 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 76 TNLRRNHQRAHNEALRLKKKIEgdlnDLELQLGHATHQAIEAQVATRLVQAQLKEEQAGRDKEQQLAAeLQEQAQALECR 155
Cdd:pfam15450 271 TKFVRQNQVSLNRVLLAEQKAR----DAKGQLEESQAGELASYVQENLEAVQLAGELAQQETQGALEL-LQEKSQVLEGS 345
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149889000 156 AALLASELEDLwatleqGEH----SWRLaeqELLEATECLNLLHLQNTGLLNQKKKLEaDLVQLSGEVEEAAQERWK 228
Cdd:pfam15450 346 VAELVRQVKDL------SDHflalSWRL---DLQEQTLGLKLSEAKKEWEGAERKSLE-DLAQWQKEVAAHLREVQE 412
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
45-262 |
2.96e-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: 41.09 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 45 DLLSKYEADAIQRTEELEEAKKKLAEKDKeytnlrrnHQRAHNEALRLKKKIEGDLNDL-------ELQLGHATHQAIEA 117
Cdd:COG3096 441 DYLAAFRAKEQQATEEVLELEQKLSVADA--------ARRQFEKAYELVCKIAGEVERSqawqtarELLRRYRSQQALAQ 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 118 QVATrlVQAQLKE-EQagRDKEQQLAAELQE---QAQALECRAALlasELEDLWATLEQGEHSwrlAEQELLEATEclnl 193
Cdd:COG3096 513 RLQQ--LRAQLAElEQ--RLRQQQNAERLLEefcQRIGQQLDAAE---ELEELLAELEAQLEE---LEEQAAEAVE---- 578
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149889000 194 lhlqntgllnQKKKLEADLVQLSGEVEEAAQE--RWKAEKAkKAITDAVMMAEELKKEQDTSAHLEQMKRH 262
Cdd:COG3096 579 ----------QRSELRQQLEQLRARIKELAARapAWLAAQD-ALERLREQSGEALADSQEVTAAMQQLLER 638
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
59-224 |
3.84e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 59 EELEEAKKKLAEKDKEYTNLRRNHQRAHnealrlkkkIEGDLNDLELQLGHATHQAIEAQVATRLVQAQLKEEQAGRDKE 138
Cdd:COG3206 182 EQLPELRKELEEAEAALEEFRQKNGLVD---------LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 139 QQLAAELQEQA--QALECRAALLASELEDLWATLeQGEHSWRLAEQELLEATE---------CLNLLHLQNTGLLNQKKK 207
Cdd:COG3206 253 PDALPELLQSPviQQLRAQLAELEAELAELSARY-TPNHPDVIALRAQIAALRaqlqqeaqrILASLEAELEALQAREAS 331
|
170
....*....|....*..
gi 1149889000 208 LEADLVQLSGEVEEAAQ 224
Cdd:COG3206 332 LQAQLAQLEARLAELPE 348
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
123-224 |
4.21e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.95 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 123 LVQAQLKEEQAGRDKE-QQLAAELQEQAQAL---ECRAALLASELEDLWATLEQGEhswrlAEQELLEAteclnlLHLQN 198
Cdd:PRK09039 39 VAQFFLSREISGKDSAlDRLNSQIAELADLLsleRQGNQDLQDSVANLRASLSAAE-----AERSRLQA------LLAEL 107
|
90 100
....*....|....*....|....*.
gi 1149889000 199 TGLLNQkkkLEADLVQLSGEVEEAAQ 224
Cdd:PRK09039 108 AGAGAA---AEGRAGELAQELDSEKQ 130
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
38-254 |
4.56e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 38 PVPLLGWDLLSKYEADAIQRTEELEEAKKKLAEKDKEYTNLRRNHQRAHNEALRLKKKI---EGDLNDLELQLGHAthqa 114
Cdd:COG3883 9 PTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIdklQAEIAEAEAEIEER---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 115 iEAQVATRLVQAQLKEEQAG------------------------RDKEQQLAAELQEQAQALECRAALLASELEDLWATL 170
Cdd:COG3883 85 -REELGERARALYRSGGSVSyldvllgsesfsdfldrlsalskiADADADLLEELKADKAELEAKKAELEAKLAELEALK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 171 EQGEHSWRLAEQELLEATECLNllhlqntGLLNQKKKLEADLVQLSGEVEEAAQERWKAEKAKKAITDAVMMAEELKKEQ 250
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLA-------QLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
....
gi 1149889000 251 DTSA 254
Cdd:COG3883 237 AAAA 240
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
49-252 |
4.96e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 39.96 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 49 KYEADAIQRTEELEEAKKKLAEKDKeytnlrrnhqrAHNEALRlKKKIEGDLNDLELQLGHATHQAIEAQVATRLVQAQL 128
Cdd:PRK07735 44 KEKALPKNDDMTIEEAKRRAAAAAK-----------AKAAALA-KQKREGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 129 KEEQAGRDKEQQLAAELQEQAQALECRAALLASELEDLW--ATLEQGEHSWRLAEQELLEATECLnllhlqnTGLLNQKK 206
Cdd:PRK07735 112 KREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTeeVTEEEEETDKEKAKAKAAAAAKAK-------AAALAKQK 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1149889000 207 KLEAdlvqlsGEVEEAAQERWKAEKAKKAITDAVMMAEELKKEQDT 252
Cdd:PRK07735 185 AAEA------GEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKAS 224
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
143-264 |
5.07e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.04 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 143 AELQEQAQALECRAALLASELEDLWATLEQGEHSWRLAEQELLEATECLNLLHLQNTGLLNQKKKLEADLVQLSGEVEEA 222
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1149889000 223 AQERWKAEKAKKAITDAVMMAEELKKEQDTSahLEQMKRHWN 264
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQ--IEQLKEELK 799
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
49-261 |
5.40e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 49 KYEADAIQRTEELEEAKKKLAEKDKEYTNLRRNHQRAHNEALRLKKKIEGDLNDLELQLGHAT--HQAIEA--------- 117
Cdd:PRK04863 352 RYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIqyQQAVQAlerakqlcg 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 118 -------QVATRLVQAQLKEEQAG---RDKEQQL-----AAELQEQAQALECRaalLASELEDlwatleqgEHSWRLAeQ 182
Cdd:PRK04863 432 lpdltadNAEDWLEEFQAKEQEATeelLSLEQKLsvaqaAHSQFEQAYQLVRK---IAGEVSR--------SEAWDVA-R 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 183 ELLEATECLNLLHLQNTGLLNQKKKLEADLVQlsgeveEAAQERWKAEKAKKAIT--DAVMMAEELKKEQDTS-AHLEQM 259
Cdd:PRK04863 500 ELLRRLREQRHLAEQLQQLRMRLSELEQRLRQ------QQRAERLLAEFCKRLGKnlDDEDELEQLQEELEARlESLSES 573
|
..
gi 1149889000 260 KR 261
Cdd:PRK04863 574 VS 575
|
|
| RP_RTVL_H_like |
cd06095 |
Retropepsin of the RTVL_H family of human endogenous retrovirus-like elements; This family ... |
24-48 |
6.27e-03 |
|
Retropepsin of the RTVL_H family of human endogenous retrovirus-like elements; This family includes aspartate proteases from retroelements with LTR (long terminal repeats) including the RTVL_H family of human endogenous retrovirus-like elements. While fungal and mammalian pepsins are bilobal proteins with structurally related N- and C-termini, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. Retroviral aspartyl protease is synthesized as part of the POL polyprotein that contains an aspartyl protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate peptidases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A.
Pssm-ID: 133159 Cd Length: 86 Bit Score: 36.16 E-value: 6.27e-03
10 20
....*....|....*....|....*
gi 1149889000 24 GHQIRHETVYMPDCPVPLLGWDLLS 48
Cdd:cd06095 62 GHTVSHSFLVVPNCPDPLLGRDLLS 86
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
125-249 |
7.43e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 39.65 E-value: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 125 QAQLKEEQAGRDKEQQLAAELQEQAQALECRAALLASELEDLWATLEQGEHSWRLAEQELLEA-------TECLNLLHLQ 197
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLeaeveqlEERIAQLSKE 755
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1149889000 198 NTGLLNQKKKLEADLVQLSGEVEEAAQERWK----AEKAKKAITDAVMMAEELKKE 249
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEEleaqIEQLKEELKALREALDELRAE 811
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
59-239 |
8.12e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.56 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 59 EELEEAKKKLAEKDKEYTNLRRNHQRAHNEALRLKKKIEGdLNDLELQLGHATHQAIEAQVATrlVQAQLKE-EQAGR-- 135
Cdd:PRK04863 837 AELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSA-LNRLLPRLNLLADETLADRVEE--IREQLDEaEEAKRfv 913
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 136 DKEQQLAAELQEQAQALECRaallASELEDLWATLEQGEHSWRLAEQELLEATECL-NLLHL---QNTGLLNQkkklEAD 211
Cdd:PRK04863 914 QQHGNALAQLEPIVSVLQSD----PEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVqRRAHFsyeDAAEMLAK----NSD 985
|
170 180
....*....|....*....|....*....
gi 1149889000 212 LV-QLSGEVEEAAQERwkaEKAKKAITDA 239
Cdd:PRK04863 986 LNeKLRQRLEQAEQER---TRAREQLRQA 1011
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
47-164 |
9.12e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 38.88 E-value: 9.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 47 LSKYEADAIQRtEELEEAKKKLAEKDKEYTNLRRNHQRahNEALRLKKKI-EGDLNDLELQLghathQAIEAQVATrlVQ 125
Cdd:COG1566 99 LARLEAELGAE-AEIAAAEAQLAAAQAQLDLAQRELER--YQALYKKGAVsQQELDEARAAL-----DAAQAQLEA--AQ 168
|
90 100 110
....*....|....*....|....*....|....*....
gi 1149889000 126 AQLKEEQAGRDKEQQLAAELQEQAQAlecRAALLASELE 164
Cdd:COG1566 169 AQLAQAQAGLREEEELAAAQAQVAQA---EAALAQAELN 204
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
47-250 |
9.82e-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: 9.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 47 LSKYEADAIQRTEELEEAKKKLAEKDkEYTNLRRNHQRAHNEALRLKKKIEGDLNDLELQ----------LGHATHQAIE 116
Cdd:TIGR00618 224 LEKELKHLREALQQTQQSHAYLTQKR-EAQEEQLKKQQLLKQLRARIEELRAQEAVLEETqerinrarkaAPLAAHIKAV 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 117 AQV--ATRLVQAQLKEEQAGRDKEQQLAAELQEQAQALECRAALLASEL--EDLWATLEQGEHSWRLAEQELLEATECLN 192
Cdd:TIGR00618 303 TQIeqQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHsqEIHIRDAHEVATSIREISCQQHTLTQHIH 382
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149889000 193 LLHLQNTGLLNQKKKLEADLVQLSGEVEEAAQE--RWKAEKAKKAITDAVMMAEELKKEQ 250
Cdd:TIGR00618 383 TLQQQKTTLTQKLQSLCKELDILQREQATIDTRtsAFRDLQGQLAHAKKQQELQQRYAEL 442
|
|
| |
