|
Name |
Accession |
Description |
Interval |
E-value |
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
179-702 |
0e+00 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 561.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 179 FLSEEVEEGDHLQQHYLDLERQLLLLSEEKQNLAQENAALRERVGRSEVESAPG-LTAKKLLLLQSQLEQLQEENFRLES 257
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGtPGGKKYLLLQKQLEQLQEENFRLET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 258 SREDDRLRCLELEREVAELQQRNQALTSLSQEAQALKDEMDELRQSSERARQLEATLNSCRRRLGELQELRRQVRQLEER 337
Cdd:pfam05622 81 ARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLGDLRRQVKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 338 NAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTERDSLREA 417
Cdd:pfam05622 161 NAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRET 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 418 NEELRCAQLQPRGLAQADLSLDPTPSGLENLAAEILPAELRETLVRLQLENKRL-CQQEAADRERQEELQRHLEEANRAR 496
Cdd:pfam05622 241 NEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLrLGQEGSYRERLTELQQLLEDANRRK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 497 HGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDPTLLKRKLEDHLQKLHEADLELQRKREYIEELEPPTDSSTARR 576
Cdd:pfam05622 321 NELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 577 IEELQDSLQKKDADLRAMEERYRRYVDKARTVIQTLEPKQRPptVVSPEFHTLRSQLWERNLRIRQMEMDYEKSRRRQEQ 656
Cdd:pfam05622 401 IDELQEALRKKDEDMKAMEERYKKYVEKAKSVIKTLDPKQNP--ASPPEIQALKNQLLEKDKKIEHLERDFEKSKLQREQ 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 269784731 657 EEKLLISAWYSMGMALEHRAGEEHAP---AHAQSFLAQQRLATNARRGP 702
Cdd:pfam05622 479 EEKLIVTAWYNMGMALHRKAIEERLAglsSPGQSFLARQRQATNARRGL 527
|
|
| HkD_Hook2 |
cd22227 |
Hook domain found in protein Hook 2 (Hook2) and similar proteins; Hook2 is a ... |
7-156 |
1.66e-87 |
|
Hook domain found in protein Hook 2 (Hook2) and similar proteins; Hook2 is a microtubule-binding protein that contributes to the establishment and maintenance of centrosome function. It may function in the positioning or formation of aggresomes, which are pericentriolar accumulations of misfolded proteins, proteasomes and chaperones. Hook2 is a component of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex.
Pssm-ID: 411798 Cd Length: 150 Bit Score: 271.36 E-value: 1.66e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 7 ELCGSLLTWLQTFQVSPPCASPQDLSSGLAIAHVLNQIDPSWFNNEWLQGISEDSSPSWRLKVRKLEKILQSLVEYSKNV 86
Cdd:cd22227 1 ELCDSLLTWLQTFQVPSPCSSYQDLTSGVAIAQVLNRIDPSWFNEAWLGRIKEDTGDNWRLKVSNLKKILQSLLEYYQDV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 87 LGHPVSDQHLPDVSLIGEFSNPAELGKLLQLVLGCAISCEKKQEYIQRIMTLEESVQHVVMEAIQELMTK 156
Cdd:cd22227 81 LGHQVSEDHLPDVNLIGEFSDDTELGKLLQLVLGCAISCEKKQEHIQQIMTLEESVQHVVMEAIQELLTK 150
|
|
| HOOK_N |
pfam19047 |
HOOK domain; This domain is found at the N-terminus of HOOK proteins. |
7-157 |
4.28e-86 |
|
HOOK domain; This domain is found at the N-terminus of HOOK proteins.
Pssm-ID: 465958 Cd Length: 151 Bit Score: 267.74 E-value: 4.28e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 7 ELCGSLLTWLQTFQVSPPCASPQDLSSGLAIAHVLNQIDPSWFNNEWLQGISEDSSPSWRLKVRKLEKILQSLVEYSKNV 86
Cdd:pfam19047 1 ELCDSLLTWLQTFNVPAPCATVEDLTDGVAMAQVLHQIDPSWFTEAWLSRIKEDVGDNWRLKVSNLKKILQSVVDYYQDV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 269784731 87 LGHPVSDQHLPDVSLIGEFSNPAELGKLLQLVLGCAISCEKKQEYIQRIMTLEESVQHVVMEAIQELMTKD 157
Cdd:pfam19047 81 LGQQISDFLLPDVNLIGEHSDPAELGRLLQLILGCAVNCEKKQEYIQQIMTLEESVQHVVMTAIQELMSKD 151
|
|
| HkD_Hook |
cd22222 |
Hook domain found in Hook family of microtubule-binding proteins; The Hook family includes ... |
9-155 |
3.13e-75 |
|
Hook domain found in Hook family of microtubule-binding proteins; The Hook family includes Hook1-3. Hook1 is a microtubule-binding protein required for spermatid differentiation. Hook2, also a microtubule-binding protein, contributes to the establishment and maintenance of centrosome function. It may function in the positioning or formation of aggresomes, which are pericentriolar accumulations of misfolded proteins, proteasomes and chaperones. Hook3 is an adaptor protein for microtubule-dependent intracellular vesicle and protein trafficking. It is involved in Golgi and endosome transport. It acts as a scaffold for the opposite-polarity microtubule-based motors cytoplasmic dynein-1 and the kinesin KIF1C. It may participate in the turnover of the endocytosed scavenger receptor. Hook proteins are components of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex. Hook adaptor proteins share an N-terminal conserved globular Hook domain, which folds as a variant of the helical calponin homology (CH) domain, and contacts the helix alpha1 of dynein light intermediate chain 1 (LIC1) in a hydrophobic groove.
Pssm-ID: 411793 Cd Length: 147 Bit Score: 239.07 E-value: 3.13e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 9 CGSLLTWLQTFQVSPPCASPQDLSSGLAIAHVLNQIDPSWFNNEWLQGISEDSSPSWRLKVRKLEKILQSLVEYSKNVLG 88
Cdd:cd22222 1 CDSLLQWLQTFNLIAPHATAEDLSDGVAIAQVLNQIDPEYFSDSWLSKIKPDVGDNWRLKVSNLKKILKGIVDYYSEVLG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 269784731 89 HPVSDQHLPDVSLIGEFSNPAELGKLLQLVLGCAISCEKKQEYIQRIMTLEESVQHVVMEAIQELMT 155
Cdd:cd22222 81 QQISGFTMPDVNAIAEKEDPKELGRLLQLVLGCAVNCERKEEYIQAIMGLEESVQHVVMEAIQELMS 147
|
|
| HkD_Hook3 |
cd22226 |
Hook domain found in protein Hook 3 (Hook3) and similar proteins; Hook3 is an adaptor protein ... |
4-156 |
6.26e-63 |
|
Hook domain found in protein Hook 3 (Hook3) and similar proteins; Hook3 is an adaptor protein for microtubule-dependent intracellular vesicle and protein trafficking. It is involved in Golgi and endosome transport. It acts as a scaffold for the opposite-polarity microtubule-based motors cytoplasmic dynein-1 and the kinesin KIF1C. It may participate in the turnover of the endocytosed scavenger receptor. Hook3 is a component of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex.
Pssm-ID: 411797 Cd Length: 153 Bit Score: 206.74 E-value: 6.26e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 4 DKAELCGSLLTWLQTFQVSPPCASPQDLSSGLAIAHVLNQIDPSWFNNEWLQGISEDSSPSWRLKVRKLEKILQSLVEYS 83
Cdd:cd22226 1 DRAELCESLLTWIQTFNVDAPCQTVEDLTSGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 269784731 84 KNVLGHPVSDQHLPDVSLIGEFSNPAELGKLLQLVLGCAISCEKKQEYIQRIMTLEESVQHVVMEAIQELMTK 156
Cdd:cd22226 81 HEILGQQINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMSK 153
|
|
| HkD_Hook1 |
cd22225 |
Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a ... |
8-157 |
6.55e-63 |
|
Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a microtubule-binding protein required for spermatid differentiation. It is a component of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex.
Pssm-ID: 411796 Cd Length: 150 Bit Score: 206.63 E-value: 6.55e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 8 LCGSLLTWLQTFQVSPPCASPQDLSSGLAIAHVLNQIDPSWFNNEWLQGISEDSSPSWRLKVRKLEKILQSLVEYSKNVL 87
Cdd:cd22225 1 LCDSLIIWLQTFNTAAPCQTVQDLTSGVAMAQVLHQIDSSWFDESWLSRIKEDVGDNWRIKMSNLKKILQGIVDYYHEFL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 88 GHPVSDQHLPDVSLIGEFSNPAELGKLLQLVLGCAISCEKKQEYIQRIMTLEESVQHVVMEAIQELMTKD 157
Cdd:cd22225 81 DQQISEFLLPDLNRIAEHSDPVELGRLLQLILGCAVNCEKKQEHIQNIMTLEESVQHVVMTAIQELMSKE 150
|
|
| HkD_SF |
cd22211 |
Hook domain-containing proteins superfamily; The Hook domain superfamily includes Hook adaptor ... |
11-154 |
5.65e-50 |
|
Hook domain-containing proteins superfamily; The Hook domain superfamily includes Hook adaptor proteins, Hook-related proteins and nuclear mitotic apparatus protein (NuMA). They share an N-terminal conserved globular Hook domain, which folds as a variant of the helical calponin homology (CH) domain with an extended alpha-helix. The Hook domain is responsible for the binding of microtubule. The Hook family includes microtubule-binding proteins, Hook1-3. Hook1 is required for spermatid differentiation. Hook2 contributes to the establishment and maintenance of centrosome function. Hook3 is an adaptor protein for microtubule-dependent intracellular vesicle and protein trafficking, and is involved in Golgi and endosome transport. Hook proteins are components of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex. The Hook-related protein (HkRP) family includes Daple, Girdin and Gipie. Daple, also called Dvl-associating protein with a high frequency of leucine residues, or coiled-coil domain-containing protein 88C(CCDC88C), or Hook-related protein 2 (HkRP2), is a novel non-receptor nucleotide exchange factor (GEF) required for activation of guanine nucleotide-binding proteins (G-proteins) during non-canonical Wnt signaling. Girdin, also called Akt phosphorylation enhancer (APE), or coiled-coil domain-containing protein 88A (CCDC88A), or G alpha-interacting vesicle-associated protein (GIV), or Girders of actin filament, or Hook-related protein 1 (HkRP1), is a bifunctional modulator of guanine nucleotide-binding proteins (G proteins). Gipie, also called GRP78-interacting protein induced by ER stress, or coiled-coil domain-containing protein 88B(CCDC88B), or brain leucine zipper domain-containing protein, or Hook-related protein 3 (HkRP3), is a novel actin cytoskeleton-binding protein and Akt substrate that regulates cell migratory responses in various biological contexts. NuMA, also called nuclear mitotic apparatus protein 1, or nuclear matrix protein-22 (NMP-22), or SP-H antigen, is a microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignment and the segregation of chromosomes during mitotic cell division.
Pssm-ID: 411792 Cd Length: 145 Bit Score: 171.30 E-value: 5.65e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 11 SLLTWLQTFQVSPPCASPQDLSSGLAIAHVLNQIDPSWFNNEWLQgiSEDSSPSWRLKVRKLEKILQSLVEYSKNVLGHP 90
Cdd:cd22211 3 ALLAWINTFPLSSPVESLDDLSDGVVLAEILSQIDPSYFDSEWLE--SRDSSDNWVLKLNNLKKLYRSLSKYYREVLGQQ 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 269784731 91 VSDQHLPDVSLIGEFSNPAELGKLLQLVLGCAISCEKKQEYIQRIMTLEESVQHVVMEAIQELM 154
Cdd:cd22211 81 LSDLPLPDLSAIARDGDEEEIVKLLELVLGAAVQCENKEEYIARIQQLDESTQAELMLIIQEVL 144
|
|
| HkD_HkRP |
cd22223 |
Hook domain found in the Hook-related protein (HkRP) family; The HkRP family includes Daple, ... |
8-153 |
8.39e-24 |
|
Hook domain found in the Hook-related protein (HkRP) family; The HkRP family includes Daple, Girdin and Gipie. Daple, also called Dvl-associating protein with a high frequency of leucine residues, or coiled-coil domain-containing protein 88C (CCDC88C), or Hook-related protein 2 (HkRP2), is a novel non-receptor nucleotide exchange factor (GEF) required for activation of guanine nucleotide-binding proteins (G-proteins) during non-canonical Wnt signaling. Girdin, also called Akt phosphorylation enhancer (APE), or coiled-coil domain-containing protein 88A (CCDC88A), or G alpha-interacting vesicle-associated protein (GIV), or Girders of actin filament, or Hook-related protein 1 (HkRP1), is a bifunctional modulator of guanine nucleotide-binding proteins (G proteins). It acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein G(i) alpha subunits. It also acts as a guanine nucleotide dissociation inhibitor for guanine nucleotide-binding protein G(s) subunit alpha GNAS. In addition, Girdin plays an essential role in cell migration. Gipie, also called GRP78-interacting protein induced by ER stress, or coiled-coil domain-containing protein 88B (CCDC88B), or brain leucine zipper domain-containing protein, or Hook-related protein 3 (HkRP3), is a novel actin cytoskeleton-binding protein and Akt substrate that regulates cell migratory responses in various biological contexts. It acts as a positive regulator of T-cell maturation and inflammatory function. As a microtubule-binding protein, Gipie regulates lytic granule clustering and NK cell killing. All family members contain a conserved globular Hook domain which folds as a variant of the helical calponin homology (CH) domain.
Pssm-ID: 411794 Cd Length: 149 Bit Score: 98.05 E-value: 8.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 8 LCGSLLTWLQTFQVSPPCA-SPQDLSSGLAIAHVLNQIDPSWFNnewlQGISEDSSPSWRLKVRKLEKILQSLVEYSKNV 86
Cdd:cd22223 2 LSSPLVTWAKTFADDGSAElSYTDLVDGVFLNNVMLQIDPRPFS----EVSNRNVDDDVNARIQNLDLLLRNIKSFYQEV 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 269784731 87 LGHPVSdQHLPDVSLIGEFSNP----AELGKLLQLVLGCAISCEKKQEYIQRIMTLEESVQHVVMEAIQEL 153
Cdd:cd22223 78 LQQLIV-MKLPDILTIGREPESeqslEELEKLLLLLLGCAVQCERKEEFIERIKNLDLEVQHALVACIQEV 147
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
324-705 |
5.66e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 75.74 E-value: 5.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 324 LQELRRQVRQLeERNAGHAERTRQLEEEL--RRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKcdlVT 401
Cdd:COG1196 195 LGELERQLEPL-ERQAEKAERYRELKEELkeLEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE---LE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 402 KEKERLLTERDSLREANEELRCA---------QLQPRGLAQADLSLDptpsgLENLAAEIlpAELRETLVRLQLENKRLC 472
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYELlaelarleqDIARLEERRRELEER-----LEELEEEL--AELEEELEELEEELEELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 473 QQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDPTLLKRKLEDHLQKLHEAD 552
Cdd:COG1196 344 EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 553 LELQRKREYIEELEPPTDSSTARRIEELQDSLQKKDADLRAMEERYRRYVDKARTVIQTLEPKQRpptvvspefhtLRSQ 632
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE-----------AAAR 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 633 LWERNLRIRQMEMDYEKSRRRQEQEEK--------LLISAWYSMGMALEHRAGEEHAPAHAQSFLAQQRLATNARRGPLG 704
Cdd:COG1196 493 LLLLLEAEADYEGFLEGVKAALLLAGLrglagavaVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAG 572
|
.
gi 269784731 705 R 705
Cdd:COG1196 573 R 573
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
254-596 |
3.56e-13 |
|
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: 73.17 E-value: 3.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 254 RLESSREDDRLR--CLELEREVAELQQrnqALTSLSQEAQALKDEMDELRQSSERA-RQLEATLNSCRRRLGELQELRRQ 330
Cdd:TIGR02168 672 ILERRREIEELEekIEELEEKIAELEK---ALAELRKELEELEEELEQLRKELEELsRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 331 VRQLEERNAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEkwlfecRNLEEKCDLVTKEKERLLTE 410
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR------EALDELRAELTLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 411 RDSLREANEELRCAQLQPRGLAQ--ADLSLDptpsgLENLAAEIlpAELRETLVRLQLENKRLCQQEAADRERQEELQRH 488
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEqiEELSED-----IESLAAEI--EELEELIEELESELEALLNERASLEEALALLRSE 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 489 LEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEqggktedptlLKRKLEDHLQKLHEadlELQRKREYIEELEPP 568
Cdd:TIGR02168 896 LEELSEELRELESKRSELRRELEELREKLAQLELRLEG----------LEVRIDNLQERLSE---EYSLTLEEAEALENK 962
|
330 340 350
....*....|....*....|....*....|..
gi 269784731 569 TDSSTA---RRIEELQDSLQK-KDADLRAMEE 596
Cdd:TIGR02168 963 IEDDEEearRRLKRLENKIKElGPVNLAAIEE 994
|
|
| HkD_Daple |
cd22228 |
Hook domain found in Daple (Dvl-associating protein with a high frequency of leucine residues) ... |
12-153 |
5.44e-13 |
|
Hook domain found in Daple (Dvl-associating protein with a high frequency of leucine residues) and similar proteins; Protein Daple, also called coiled-coil domain-containing protein 88C (CCDC88C), or Hook-related protein 2 (HkRP2), is a novel non-receptor nucleotide exchange factor (GEF) required for activation of guanine nucleotide-binding proteins (G-proteins) during non-canonical Wnt signaling.
Pssm-ID: 411799 Cd Length: 153 Bit Score: 67.26 E-value: 5.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 12 LLTWLQTFQvspPCASPQ--------DLSSGLAIAHVLNQIDPSWFNnewlQGISEDSSPSWRLKVRKLEKILQSLVEYS 83
Cdd:cd22228 6 LVTWVKTFG---PLGFGSedklsmymDLVDGVFLNKIMLQIDPRPTN----QRVNKHVNNDVNLRIQNLTILVRHIKTYY 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 269784731 84 KNVLGHPVSdQHLPDVSLIGE--FSNPA--ELGKLLQLVLGCAISCEKKQEYIQRIMTLEESVQHVVMEAIQEL 153
Cdd:cd22228 79 QEVLQQLIV-MNLPNVLMIGKdpLSGKSmeEIKKMLLLVLGCAVQCERKEEFIERIKQLDIETQAAIVSHIQEV 151
|
|
| HkD_Girdin |
cd22229 |
Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation ... |
12-153 |
2.90e-12 |
|
Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation enhancer (APE), or coiled-coil domain-containing protein 88A (CCDC88A), or G alpha-interacting vesicle-associated protein (GIV), or Girders of actin filament, or Hook-related protein 1 (HkRP1), is a bifunctional modulator of guanine nucleotide-binding proteins (G proteins). It acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein G(i) alpha subunits. It also acts as a guanine nucleotide dissociation inhibitor for guanine nucleotide-binding protein G(s) subunit alpha GNAS. In addition, Girdin plays an essential role in cell migration.
Pssm-ID: 411800 Cd Length: 156 Bit Score: 65.20 E-value: 2.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 12 LLTWLQTFQVSPPCASPQ-----DLSSGLAIAHVLNQIDPSWFNNEWLQGISEDSSpswrLKVRKLEKILQSLVEYSKNV 86
Cdd:cd22229 9 LVTWVKTFGPLATGNGTPldeyvALVDGVFLNEVMLQINPKSSNQRVNKKVNNDAS----LRIQNLSILVKQIKLYYQET 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 269784731 87 LGHPVSdQHLPDVSLIGE--FSNPA--ELGKLLQLVLGCAISCEKKQEYIQRIMTLEESVQHVVMEAIQEL 153
Cdd:cd22229 85 LQQLIM-MSLPNVLVLGRnpLSEQGteEMKKLLLLLLGCAVQCERKEEFIERIQTLDFDTKAAVAAHIQEV 154
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
255-525 |
3.42e-12 |
|
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: 70.10 E-value: 3.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 255 LESSREDDRLRCLELEREVAELQQRNQALTSlsQEAQALKDEMDELrqSSERArQLEATLNSCRRRLGELQELRRQ-VRQ 333
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGE--EEQLRVKEKIGEL--EAEIA-SLERSIAEKERELEDAEERLAKlEAE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 334 LEERNAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTERDS 413
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 414 LREANEELRCAQLQPRG-LAQADLSLDPTPSGLENLAAEIlpAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEA 492
Cdd:TIGR02169 411 LQEELQRLSEELADLNAaIAGIEAKINELEEEKEDKALEI--KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKL 488
|
250 260 270
....*....|....*....|....*....|...
gi 269784731 493 NRARHGLEAQQRLNQQQLSELRAQVEELQKALQ 525
Cdd:TIGR02169 489 QRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
271-596 |
5.29e-12 |
|
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: 69.71 E-value: 5.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 271 REVAELQQRNQALTSLSQEAQALKDEMDELRQsseRARQLEATLNSCRRRLGELQelrRQVRQLEERNAGHAERTRQLEE 350
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIEN---RLDELSQELSDASRKIGEIE---KEIEQLEQEEEKLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 351 ELRragSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDlvtkeKERLLTERDSLREANEELRCAQLQPRG 430
Cdd:TIGR02169 745 DLS---SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS-----HSRIPEIQAELSKLEEEVSRIEARLRE 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 431 LAQADLSLDptpsgLENLAAEILPAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQL 510
Cdd:TIGR02169 817 IEQKLNRLT-----LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 511 SELRAQVEELQKALQEQGGKTEDPTLLKRKLEDHLQKLHEADLELQRKREYIEELEPPTDSstarrIEELQDSLQKKDAD 590
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS-----LEDVQAELQRVEEE 966
|
....*.
gi 269784731 591 LRAMEE 596
Cdd:TIGR02169 967 IRALEP 972
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
268-533 |
3.51e-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: 67.00 E-value: 3.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 268 ELEREVAELQQRNQALTSLSQEAQALKDE-MDELRQSSERARQLEATLNSCRRRLGEL-QELRRQVRQLEERNAGHAERT 345
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEElRLEVSELEEEIEELQKELYALANEISRLeQQKQILRERLANLERQLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 346 RQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTERDSLREANEELRcAQ 425
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN-NE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 426 LQ--PRGLAQADLSLDPTPSGLENLAAEILPAELRETLVRLQLENKRLCQQEaadrERQEELQRHLEEANRARHGLEAQQ 503
Cdd:TIGR02168 402 IErlEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQ----EELERLEEALEELREELEEAEQAL 477
|
250 260 270
....*....|....*....|....*....|
gi 269784731 504 RLNQQQLSELRAQVEELQKALQEQGGKTED 533
Cdd:TIGR02168 478 DAAERELAQLQARLDSLERLQENLEGFSEG 507
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
180-595 |
9.49e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 9.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 180 LSEEVEEGDHLQQHYLDLERQLLLLSEEKQNLAQENAALRERVGRSEVESApgLTAKKLLLLQSQLEQLQEENFRLESSR 259
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL--EAEAELAEAEEELEELAEELLEALRAA 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 260 EDDRLRCLELEREVAELQQRNQALtsLSQEAQALKDEMDELRQSSERARQLEATLNSCRRRLGELQELRRQVRQLEERNA 339
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERL--EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 340 GHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEK------------WLFECRNLEEKC------DLVT 401
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLrglagavavligVEAAYEAALEAAlaaalqNIVV 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 402 KEKERLLTERDSLREAN----EELRCAQLQPRGLAQADLSLDPTPSGLENLAAEILPAELR----------ETLVRLQLE 467
Cdd:COG1196 554 EDDEVAAAAIEYLKAAKagraTFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARyyvlgdtllgRTLVAARLE 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 468 NKRLCQQEAADRERQEEL------------QRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDPT 535
Cdd:COG1196 634 AALRRAVTLAGRLREVTLegeggsaggsltGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAE 713
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 269784731 536 LLKRKLEDHLQKLHEADLELQRKREYIEELEPPTDSSTAR-------RIEELQDSLQKKDADLRAME 595
Cdd:COG1196 714 EERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALeelpeppDLEELERELERLEREIEALG 780
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
256-660 |
1.43e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.61 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 256 ESSREDDRLRCLELEREVAELQQRNQALTSLSQEAQAlKDEMDELRQSSERARQLEATLNSCRRRLGELQElrrqvrqle 335
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE-ARKADELKKAEEKKKADEAKKAEEKKKADEAKK--------- 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 336 ernagHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTERDSLR 415
Cdd:PTZ00121 1310 -----KAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAK 1384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 416 EANEELRCAQLQPRGLAQADLSLDPtpsgLENLAAEILPAElretlvrlqlENKRlcqqEAADRERQEELQRHLEEANRA 495
Cdd:PTZ00121 1385 KKAEEKKKADEAKKKAEEDKKKADE----LKKAAAAKKKAD----------EAKK----KAEEKKKADEAKKKAEEAKKA 1446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 496 ----RHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEdptlLKRKLEDHLQKlheADlELQRKREYIEELEPPTDS 571
Cdd:PTZ00121 1447 deakKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE----AKKKAEEAKKK---AD-EAKKAAEAKKKADEAKKA 1518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 572 STARRIEELQDSLQKKDAD--LRAMEERYRRYVDKARTVIQTLEPKQRPPTVVSPEfhtlrsqlwERNLRIRQMEMDYEK 649
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKKADeaKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEE---------DKNMALRKAEEAKKA 1589
|
410
....*....|.
gi 269784731 650 SRRRQEQEEKL 660
Cdd:PTZ00121 1590 EEARIEEVMKL 1600
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
268-422 |
2.26e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 268 ELEREVAELQQRNQALTSLSQEAQALKDEMDELRQSSERA-----------------RQLEATLNSCRRRLGELQELRRQ 330
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLaeyswdeidvasaereiAELEAELERLDASSDDLAALEEQ 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 331 VRQLEERNAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKE-KERLLT 409
Cdd:COG4913 694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERElRENLEE 773
|
170
....*....|...
gi 269784731 410 ERDSLREANEELR 422
Cdd:COG4913 774 RIDALRARLNRAE 786
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
405-613 |
3.32e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 3.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 405 ERLLTERDSLREANEELRCAQLQPRGLAQadlsldptpsgLENLAAEIlpAELRETLVRLQLENKRLCQQEAadRERQEE 484
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLEP-----------IRELAERY--AAARERLAELEYLRAALRLWFA--QRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 485 LQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDPtlLKRKLEDHLQKLHEADLELQRKREYIEE 564
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ--LEREIERLERELEERERRRARLEALLAA 370
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 269784731 565 LEPPTDSStARRIEELQDSLQKKDADLRAMEERYRRYVDKARTVIQTLE 613
Cdd:COG4913 371 LGLPLPAS-AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR 418
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
268-534 |
4.75e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 4.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 268 ELEREVAELQQRNQALTSLSQEAQALKDEMDELRQsserARQLEATLNSCRRRLgELQELRRQVRQLEERNAGHAERTRQ 347
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRELAERYAAARERLAE----LEYLRAALRLWFAQR-RLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 348 LEEELRRAGSLRAQLEAQRRQvqelQGQWQEEAmkaekwlfecrnLEEKCDLVTKEKERLLTERDSLREAneelrcaqlq 427
Cdd:COG4913 314 LEARLDALREELDELEAQIRG----NGGDRLEQ------------LEREIERLERELEERERRRARLEAL---------- 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 428 prgLAQADLSLDPTPSGLENLAaeilpAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQrlnq 507
Cdd:COG4913 368 ---LAALGLPLPASAEEFAALR-----AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK---- 435
|
250 260
....*....|....*....|....*..
gi 269784731 508 qqlSELRAQVEELQKALQEQGGKTEDP 534
Cdd:COG4913 436 ---SNIPARLLALRDALAEALGLDEAE 459
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
254-661 |
4.83e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 4.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 254 RLESSREDDRLRCLELEREV--AELQQRNQALTSLSQEAQALKDEMDELRQS--------SERARQLEATLNSCRRRLGE 323
Cdd:COG1196 308 EERRRELEERLEELEEELAEleEELEELEEELEELEEELEEAEEELEEAEAElaeaeealLEAEAELAEAEEELEELAEE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 324 LQELRRQVRQLEERNAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKE 403
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 404 KERLLTE-RDSLREANEELRCAQLQPRGLAQADLSLDPTPSGLENLAAEILPAELRETLVRLQLENKRLcQQEAADRERQ 482
Cdd:COG1196 468 LLEEAALlEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY-EAALEAALAA 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 483 EELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQggKTEDPTLLKRKLEDHLQKLHEADLELQRKREYI 562
Cdd:COG1196 547 ALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAA--LARGAIGAAVDLVASDLREADARYYVLGDTLLG 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 563 EELEPPTDSSTARRIEELQDSLQKKDADLRAMEERYRRYVDKARTVIQTLEPKQRpptvvspefhtLRSQLWERNLRIRQ 642
Cdd:COG1196 625 RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEA-----------ELEELAERLAEEEL 693
|
410
....*....|....*....
gi 269784731 643 MEMDYEKSRRRQEQEEKLL 661
Cdd:COG1196 694 ELEEALLAEEEEERELAEA 712
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
256-659 |
6.77e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.20 E-value: 6.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 256 ESSREDDRLRCLELEREVAELQQRNQALTSLSQ----EAQALKDEMDELrqsSERARQLEATLNSCRRRLGELQE----L 327
Cdd:PRK02224 271 EREREELAEEVRDLRERLEELEEERDDLLAEAGlddaDAEAVEARREEL---EDRDEELRDRLEECRVAAQAHNEeaesL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 328 RRQVRQLEERNAGHAERTRQLEEELRRAgslRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKER- 406
Cdd:PRK02224 348 REDADDLEERAEELREEAAELESELEEA---REAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDEl 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 407 ----------LLTERDSLREAN---EELRCAQL-QPRGLAQADLSLDPTPSGLENLAAEILPAELRETLVRLQLENKRLC 472
Cdd:PRK02224 425 rereaeleatLRTARERVEEAEallEAGKCPECgQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 473 QQEAADRERQEELQRHLEEANRARHGLEAQQRLnqqQLSELRAQVEELQKALQEqggKTEDPTLLKRKLEDHLQKLHEAD 552
Cdd:PRK02224 505 VEAEDRIERLEERREDLEELIAERRETIEEKRE---RAEELRERAAELEAEAEE---KREAAAEAEEEAEEAREEVAELN 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 553 LELQRKREYIEELEpptdsstarRIEELQDSLQKKDADLRAMEERyrryvdkaRTVIQTLEpKQRpptvvspefhtlRSQ 632
Cdd:PRK02224 579 SKLAELKERIESLE---------RIRTLLAAIADAEDEIERLREK--------REALAELN-DER------------RER 628
|
410 420
....*....|....*....|....*..
gi 269784731 633 LWERNLRIRQMEMDYEKSRRRQEQEEK 659
Cdd:PRK02224 629 LAEKRERKRELEAEFDEARIEEAREDK 655
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
268-527 |
1.08e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 55.73 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 268 ELEREVAELQQRNQaltSLSQEAQALKDEMDELRQSSERARQLE-----ATLNSCRRRLGELQELRRQVRQleernagHA 342
Cdd:PRK04863 848 ELERALADHESQEQ---QQRSQLEQAKEGLSALNRLLPRLNLLAdetlaDRVEEIREQLDEAEEAKRFVQQ-------HG 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 343 ERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMK--AEKWLFECRN----------LEEKCDLVTKEKERLLTE 410
Cdd:PRK04863 918 NALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQafALTEVVQRRAhfsyedaaemLAKNSDLNEKLRQRLEQA 997
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 411 RDSLREANEELRCAQLQPRGLAQADLSLDPTPSGLENLAAEiLPAELRETLVRLQLEnkrlcqQEAADRERQEELQRHLE 490
Cdd:PRK04863 998 EQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQE-LKQELQDLGVPADSG------AEERARARRDELHARLS 1070
|
250 260 270
....*....|....*....|....*....|....*..
gi 269784731 491 EANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQ 527
Cdd:PRK04863 1071 ANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEM 1107
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
180-526 |
1.37e-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: 55.06 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 180 LSEEVEEGDHLQQHYLDLERQLLLLSEEKQnlaQENAALRERVGRSEVESAPGltAKKLLLLQSQLEQLQEENFRLESSR 259
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKELEELS---RQISALRKDLARLEAEVEQL--EERIAQLSKELTELEAEIEELEERL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 260 EDDRLRCLELEREVAELQQR-NQALTSLSQEAQALKDEMDELRQSSERARQLEATLNSCRRRLGELQ-ELRRQVRQLEER 337
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQiEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATErRLEDLEEQIEEL 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 338 NaghaERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKwlfECRNLEEKCDLVTKEKERLLTERDSLREA 417
Cdd:TIGR02168 851 S----EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS---ELEELSEELRELESKRSELRRELEELREK 923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 418 NE---------ELRCAQLQPRGLAQADLSLDPTPSGLENLAAEilPAELRETLVRLQLENKRL-------CQQEAADRER 481
Cdd:TIGR02168 924 LAqlelrleglEVRIDNLQERLSEEYSLTLEEAEALENKIEDD--EEEARRRLKRLENKIKELgpvnlaaIEEYEELKER 1001
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 269784731 482 QEELQRHLEEANRARHGLE-AQQRLNQQQLSELRAQVEELQKALQE 526
Cdd:TIGR02168 1002 YDFLTAQKEDLTEAKETLEeAIEEIDREARERFKDTFDQVNENFQR 1047
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
268-660 |
1.39e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 268 ELEREVAELQQRNQALtslsQEAQALKDEMDELRQSSERARQLEATLNSCRRRLGEL----QELRRQVRQLEERNAGHAE 343
Cdd:COG4717 99 ELEEELEELEAELEEL----REELEKLEKLLQLLPLYQELEALEAELAELPERLEELeerlEELRELEEELEELEAELAE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 344 RTRQLEEELRRAG-SLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERlLTERDSLREANEELR 422
Cdd:COG4717 175 LQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA-AALEERLKEARLLLL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 423 CAQLQPRGLAQADLSLDPTPSGLENLAAEILPAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEaq 502
Cdd:COG4717 254 IAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLP-- 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 503 QRLNQQQLSELRAQVEELQKALQEQGGKTEDPTL--LKRKLEDHLQKLHEADLE-----LQRKREYIEELEpptdsstar 575
Cdd:COG4717 332 PDLSPEELLELLDRIEELQELLREAEELEEELQLeeLEQEIAALLAEAGVEDEEelraaLEQAEEYQELKE--------- 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 576 RIEELQDSLQKKDADLRAMEERYRRyvDKARTVIQTLEPKQRpptVVSPEFHTLRSQLWERNLRIRQMEMDYEKSRRRQE 655
Cdd:COG4717 403 ELEELEEQLEELLGELEELLEALDE--EELEEELEELEEELE---ELEEELEELREELAELEAELEQLEEDGELAELLQE 477
|
....*
gi 269784731 656 QEEKL 660
Cdd:COG4717 478 LEELK 482
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
254-613 |
1.46e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 254 RLESSREDDRLRCLELEREVAELQQRNQALTSLSQEAQALKDEMDELRQSS---ERARQLEATLNSCRRRLGELqELRRQ 330
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHelyEEAKAKKEELERLKKRLTGL-TPEKL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 331 VRQLEERNAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQG-----------------------------QWQEEAM 381
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelteehrkelleeytaelkRIEKELK 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 382 KAEKWLFECRNLEEKCDLVTKEKERLLTER---DSLREANEELRCAQLQPrgLAQADLSLDPTPSGLENLAAEILpaELR 458
Cdd:PRK03918 470 EIEEKERKLRKELRELEKVLKKESELIKLKelaEQLKELEEKLKKYNLEE--LEKKAEEYEKLKEKLIKLKGEIK--SLK 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 459 ETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDPTLLK 538
Cdd:PRK03918 546 KELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLE 625
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269784731 539 RKLEDHLQKLHEADLELQRKREYIEELEPPTDSSTARRIEELQDSLQKKDADLRAMEERYRRYVDKARTVIQTLE 613
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLK 700
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
180-601 |
2.76e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 180 LSEEVEEGDHLQQHYLDLERQLLLLSEEKQNLAQENAALRERVGRSEVESAPGLTAKKLLLLQSQLEQlqeenfrlessr 259
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAE------------ 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 260 EDDRLRclELEREVAELQQRNQALTSLSQEAQALKDEMDELRQ--SSERARQLEATLNSCRRRLGELQELRRQVRQLEER 337
Cdd:COG4717 144 LPERLE--ELEERLEELRELEEELEELEAELAELQEELEELLEqlSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 338 NAGHAERTRQLEEELRRAGSLRAQLEAQRRQ-----VQELQGQWQEEAMKAEKWL-FECRNLEEKCDLVTKEKERLLTER 411
Cdd:COG4717 222 LEELEEELEQLENELEAAALEERLKEARLLLliaaaLLALLGLGGSLLSLILTIAgVLFLVLGLLALLFLLLAREKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 412 DSLREANEELRCAQLQPRGLAQ--ADLSLDPTPSGLENLAAEILPAELRETLVRLQLENKRLCQQEAADRERQEELQRHL 489
Cdd:COG4717 302 KEAEELQALPALEELEEEELEEllAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGV 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 490 EEANRARHGLEAQQRLNQ--QQLSELRAQVEELQKALQEQgGKTEDPTLLKRKLEDHLQKLHEADLELQRKREYIEELEP 567
Cdd:COG4717 382 EDEEELRAALEQAEEYQElkEELEELEEQLEELLGELEEL-LEALDEEELEEELEELEEELEELEEELEELREELAELEA 460
|
410 420 430
....*....|....*....|....*....|....*
gi 269784731 568 PTDS-STARRIEELQDSLQKKDADLRAMEERYRRY 601
Cdd:COG4717 461 ELEQlEEDGELAELLQELEELKAELRELAEEWAAL 495
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
332-569 |
5.90e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 5.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 332 RQLEERNAGHAERTRQLEEELRRagsLRAQLEAQRRQVQELQGQWQEEAMKAEKwlfecRNLEEKCDLVTKEKERLLTER 411
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPE---LRKELEEAEAALEEFRQKNGLVDLSEEA-----KLLLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 412 DSLREANEELRcAQLQPRGLAQADLSLDPTPSGLENLAAEiLPAELRETLVRLQLENKRLC----QQEAADRERQEELQR 487
Cdd:COG3206 236 AEAEARLAALR-AQLGSGPDALPELLQSPVIQQLRAQLAE-LEAELAELSARYTPNHPDVIalraQIAALRAQLQQEAQR 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 488 HLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDPTLLKRKLEDHLQKLHEADLELQRKREYIEELEP 567
Cdd:COG3206 314 ILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVIDP 393
|
..
gi 269784731 568 PT 569
Cdd:COG3206 394 AV 395
|
|
| HkD_Gipie |
cd22230 |
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar ... |
8-153 |
6.18e-07 |
|
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar proteins; Gipie, also called coiled-coil domain-containing protein 88B (CCDC88B), or brain leucine zipper domain-containing protein, or Hook-related protein 3 (HkRP3), is a novel actin cytoskeleton-binding protein and Akt substrate that regulates cell migratory responses in various biological contexts. It acts as a positive regulator of T-cell maturation and inflammatory function. As a microtubule-binding protein, Gipie regulates lytic granule clustering and NK cell killing.
Pssm-ID: 411801 Cd Length: 170 Bit Score: 49.83 E-value: 6.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 8 LCGSLLTWLQTFQ------------------VSPPCASPQ--DLSSGLAIAHVLNQIDPSWFNNEWLQGIseDSSPSWRl 67
Cdd:cd22230 4 MSGALVTWALGFEglvgeeedslgfpeeeeeEGTLDAEKRflRLSNGDLLNRVMGIIDPSPRGGPRMRGD--DGPAAHR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 68 kVRKLEKILQSLVEYSKNVLgHPVSDQHLPDVSLIGE--FSNPA--ELGKLLQLVLGCAISCEKKQEYIQRIMTLEESVQ 143
Cdd:cd22230 81 -VQNLHILWGRLRDFYQEEL-QQLILSPPPDLQVMGRdpFTEEAvqELEKLLRLLLGAAVQCERRELFIRHIQGLDLDVQ 158
|
170
....*....|
gi 269784731 144 HVVMEAIQEL 153
Cdd:cd22230 159 AELAEAIQEV 168
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
439-664 |
7.76e-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: 52.75 E-value: 7.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 439 DPTPSGLENLAAEIlpAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVE 518
Cdd:TIGR02168 666 AKTNSSILERRREI--EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 519 ELQKALQEQGGKTEDptlLKRKLEDHLQKLHEADLELQRKREYIEELEPptdsstarRIEELQDSLQKKDADLRAMEERY 598
Cdd:TIGR02168 744 QLEERIAQLSKELTE---LEAEIEELEERLEEAEEELAEAEAEIEELEA--------QIEQLKEELKALREALDELRAEL 812
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 269784731 599 RRYVDKARTVIQTLEPKQRPPTVVSPEFHTLRSQLWERNLRIRQMEMDYEKSRRRQEQEEKLLISA 664
Cdd:TIGR02168 813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL 878
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
259-613 |
8.27e-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: 8.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 259 REDDRLRCLELEREVAELQQRnqaLTSLSQEAQALKDEMDELRQSSERARQLEATLNSCRRRLG--ELQELRRQVRQLEE 336
Cdd:COG4913 276 YLRAALRLWFAQRRLELLEAE---LEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgdRLEQLEREIERLER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 337 RNAGHAERTRQLEEELRRAG----SLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKcdlVTKEKERLLTERD 412
Cdd:COG4913 353 ELEERERRRARLEALLAALGlplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRD---LRRELRELEAEIA 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 413 SLREANEELRCAQLQPRGLAQADLSLDPT-----------------------------------PSGLENLAAEI---LP 454
Cdd:COG4913 430 SLERRKSNIPARLLALRDALAEALGLDEAelpfvgelievrpeeerwrgaiervlggfaltllvPPEHYAAALRWvnrLH 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 455 AELRETLVRLQLENKRLCQQEAADR------------------------------ERQEELQRH--------LEEANRAR 496
Cdd:COG4913 510 LRGRLVYERVRTGLPDPERPRLDPDslagkldfkphpfrawleaelgrrfdyvcvDSPEELRRHpraitragQVKGNGTR 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 497 HGLEAQQRL---------NQQQLSELRAQVEELQKALQEQGGKTEDPTLLKRKLEDHLQKLH-------------EADLE 554
Cdd:COG4913 590 HEKDDRRRIrsryvlgfdNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQrlaeyswdeidvaSAERE 669
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 269784731 555 LQRKREYIEELEpptdsSTARRIEELQDSLQKKDADLRAMEERYRRYVDKARTVIQTLE 613
Cdd:COG4913 670 IAELEAELERLD-----ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELE 723
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
181-519 |
8.89e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 8.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 181 SEEVEEGDHLQQhyldlERQLLLLSEEKQNLAQENAALRERVGRSEVESAPGLTAKKLLLLQSQLEQLqeenfRLESSRE 260
Cdd:PTZ00121 1466 AEEAKKADEAKK-----KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK-----KAEEAKK 1535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 261 DDRLRCLELEREVAELQQ-----RNQALTSLSQEAQALKDEMDELRQSSERARQLEATLNSCRRRLGELQELRRQVRQLE 335
Cdd:PTZ00121 1536 ADEAKKAEEKKKADELKKaeelkKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 336 ERNAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTERDSLR 415
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALK 1695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 416 EANEELRCAQLQPRGLAQadlsldptpsglENLAAEILPAELRETLVRLQlenkRLCQQEAADRERQEELQRHLEEANRA 495
Cdd:PTZ00121 1696 KEAEEAKKAEELKKKEAE------------EKKKAEELKKAEEENKIKAE----EAKKEAEEDKKKAEEAKKDEEEKKKI 1759
|
330 340
....*....|....*....|....
gi 269784731 496 RHGLEAQQRLNQQQLSELRAQVEE 519
Cdd:PTZ00121 1760 AHLKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
287-655 |
9.03e-07 |
|
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: 52.38 E-value: 9.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 287 SQEAQALKDEMDELRQSSERARQLEATLNSCRRRLGELQ----ELRRQVRQLE-ERNagHAERTRQLEEELR-RAGSLRA 360
Cdd:TIGR02169 152 PVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDliidEKRQQLERLRrERE--KAERYQALLKEKReYEGYELL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 361 -QLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDlvtkEKERLLTERDSLREANEELRCAQLQPRglaqadlsLD 439
Cdd:TIGR02169 230 kEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLE----EIEQLLEELNKKIKDLGEEEQLRVKEK--------IG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 440 PTPSGLENLAAEIlpAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEE 519
Cdd:TIGR02169 298 ELEAEIASLERSI--AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 520 LQKALQEQGGKT----EDPTLLKRKLEDHLQKLHEADLELQRKREYIEELEPPTDSSTArRIEELQDSLQKKDADLRAME 595
Cdd:TIGR02169 376 VDKEFAETRDELkdyrEKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEA-KINELEEEKEDKALEIKKQE 454
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 596 ERYRRYVDKARTVIQTLEPKQRPPTVVSPEFHTLRSQLWERNLRIRQMEmDYEKSRRRQE 655
Cdd:TIGR02169 455 WKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASE-ERVRGGRAVE 513
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
268-608 |
9.92e-07 |
|
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: 52.38 E-value: 9.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 268 ELEREVAELQQRNQALTSLSQEAQALKDEMDELR----QSSERARQLEATLNSCRRRLGE--LQELRRQVRQLEERNAGH 341
Cdd:TIGR02169 731 EEEKLKERLEELEEDLSSLEQEIENVKSELKELEarieELEEDLHKLEEALNDLEARLSHsrIPEIQAELSKLEEEVSRI 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 342 AERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEamKAEkwlfecrnLEEKCDLVTKEKERLLTErdslreaneel 421
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ--IKS--------IEKEIENLNGKKEELEEE----------- 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 422 rcaqlqprglaqadlsldptpsgLENLAAEIlpAELRETLVRLQlenkrlcqqeaadRERqEELQRHLEEANRARHGLEA 501
Cdd:TIGR02169 870 -----------------------LEELEAAL--RDLESRLGDLK-------------KER-DELEAQLRELERKIEELEA 910
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 502 QQRLNQQQLSELRAQVEELQKALQEQGgktedpTLLKRKLEDHLQKLHEADLELQRKR--EYIEELEPPTD------SST 573
Cdd:TIGR02169 911 QIEKKRKRLSELKAKLEALEEELSEIE------DPKGEDEEIPEEELSLEDVQAELQRveEEIRALEPVNMlaiqeyEEV 984
|
330 340 350
....*....|....*....|....*....|....*
gi 269784731 574 ARRIEELQDSLQKKDADLRAMEERYRRYVDKARTV 608
Cdd:TIGR02169 985 LKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
282-526 |
1.86e-06 |
|
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: 50.92 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 282 ALTSLSQEAQALKDEMDELRQSSERARQLEATLNSCRRRL-GELQELRRQVRQLEERNAGHAERTRQLEEELRRagsLRA 360
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALlKQLAALERRIAALARRIRALEQELAALEAELAE---LEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 361 QLEAQRRQVQELQGQWQEEAMKAEKwlfecrnleekcdLVTKEKERLLTERDSLREANEELRCAqlqpRGLAQADLSLdp 440
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYR-------------LGRQPPLALLLSPEDFLDAVRRLQYL----KYLAPARREQ-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 441 tpsgLENLAAEIlpAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEEL 520
Cdd:COG4942 152 ----AEELRADL--AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
....*.
gi 269784731 521 QKALQE 526
Cdd:COG4942 226 EALIAR 231
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
288-453 |
2.96e-06 |
|
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: 50.72 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 288 QEAQALKDEMDELRQSSERARQLEATLNSCRRRLGELQELRRQVRQLEERNAGHAERTRQLEEELRRAGSLRAQLEAQ-- 365
Cdd:COG3096 495 QTARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQaa 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 366 ---------RRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLV----------------TKEKERLLT-ERDSLREANE 419
Cdd:COG3096 575 eaveqrselRQQLEQLRARIKELAARAPAWLAAQDALERLREQSgealadsqevtaamqqLLEREREATvERDELAARKQ 654
|
170 180 190
....*....|....*....|....*....|....*
gi 269784731 420 ELrcaQLQPRGLAQADLSLDPTPSGL-ENLAAEIL 453
Cdd:COG3096 655 AL---ESQIERLSQPGGAEDPRLLALaERLGGVLL 686
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
206-606 |
4.13e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 4.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 206 EEKQNLAQEnaALRERVGRSEVESAPGLTAKKLLLLQSQLEQLQEENFR-LESSREDDRLRCLELEREVAELQQRNQALT 284
Cdd:PTZ00121 1094 EEAFGKAEE--AKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARkAEEARKAEDAKRVEIARKAEDARKAEEARK 1171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 285 SLSQEAQALKDEMDELRQSSERARQLEATLNSCRRRLGELQELRRQVRQLEERNA---GHAERTRQLEEELRRAGSLRAQ 361
Cdd:PTZ00121 1172 AEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAeavKKAEEAKKDAEEAKKAEEERNN 1251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 362 LEAQRRQVQELQGQWQ-------EEAMKAEkwlfECRNLEEKCDLVTKEKERLLTERDSLREANEELRCAQLQPRGLAQA 434
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARrqaaikaEEARKAD----ELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA 1327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 435 DLSLDPTPSGLENL--AAEILPAELRETLVRLQLENKRLCQQE---AADRERQEELQRHLEEANRARHgLEAQQRLNQQQ 509
Cdd:PTZ00121 1328 KKKADAAKKKAEEAkkAAEAAKAEAEAAADEAEAAEEKAEAAEkkkEEAKKKADAAKKKAEEKKKADE-AKKKAEEDKKK 1406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 510 LSELRAQVEELQKAlQEQGGKTEDptllKRKLEDHLQKLHEADL--ELQRKREYIEELEP-PTDSSTARRIEELQDSLQ- 585
Cdd:PTZ00121 1407 ADELKKAAAAKKKA-DEAKKKAEE----KKKADEAKKKAEEAKKadEAKKKAEEAKKAEEaKKKAEEAKKADEAKKKAEe 1481
|
410 420
....*....|....*....|..
gi 269784731 586 -KKDADLRAMEERYRRYVDKAR 606
Cdd:PTZ00121 1482 aKKADEAKKKAEEAKKKADEAK 1503
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
286-660 |
5.13e-06 |
|
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: 49.97 E-value: 5.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 286 LSQEAQALKDEMDELRQSSERARQLEATLNSCRRRLGELQELRRQVRQLE-------------------ERNAGHAERTR 346
Cdd:TIGR00618 224 LEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRaqeavleetqerinrarkaAPLAAHIKAVT 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 347 QLEE-------ELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLE---EKCDLVTKEKERLLTERDSLRE 416
Cdd:TIGR00618 304 QIEQqaqrihtELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRdahEVATSIREISCQQHTLTQHIHT 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 417 ANEELRCAQLQPRGLAQADLSLDptpsgleNLAAEILPAELRETLVRLQLenKRLCQQEAADRERQEELQRHLEEANRAR 496
Cdd:TIGR00618 384 LQQQKTTLTQKLQSLCKELDILQ-------REQATIDTRTSAFRDLQGQL--AHAKKQQELQQRYAELCAAAITCTAQCE 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 497 HGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDPTLLKRKLEDHLQKLHEADLELQRKREYIEELEPPTDSSTA-- 574
Cdd:TIGR00618 455 KLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRge 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 575 RRIEELQDSLQKKDADLRAMEERYRRYVDKARTVIQTLEPKQRPPTVVSPEFHTLRsQLWERNLRIRQMEMDYEKSRRRQ 654
Cdd:TIGR00618 535 QTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQ-NITVRLQDLTEKLSEAEDMLACE 613
|
....*.
gi 269784731 655 EQEEKL 660
Cdd:TIGR00618 614 QHALLR 619
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
265-597 |
5.79e-06 |
|
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: 49.95 E-value: 5.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 265 RCLELEREVAELQQRNQALTslsQEAQALKDEMDELRQsserARQLEATLNSCRRRLGELQE-LRRQVRQLEERNAGHAE 343
Cdd:COG3096 307 RLVEMARELEELSARESDLE---QDYQAASDHLNLVQT----ALRQQEKIERYQEDLEELTErLEEQEEVVEEAAEQLAE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 344 RTRQLEEELRRAGSLRAQLEAQRRQVQELQ---GQWQEeAMKAekwLFECRNLEEKCDL-VTKEKERLLTERDSLREANE 419
Cdd:COG3096 380 AEARLEAAEEEVDSLKSQLADYQQALDVQQtraIQYQQ-AVQA---LEKARALCGLPDLtPENAEDYLAAFRAKEQQATE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 420 ELRCAQlQPRGLAQADLS------------LDPTPSG---------------LENLA--AEILPAELRETLVRLQLEN-- 468
Cdd:COG3096 456 EVLELE-QKLSVADAARRqfekayelvckiAGEVERSqawqtarellrryrsQQALAqrLQQLRAQLAELEQRLRQQQna 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 469 ----KRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQ--------------------KAL 524
Cdd:COG3096 535 erllEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRarikelaarapawlaaqdalERL 614
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 269784731 525 QEQGGKT-EDPTLLKRKLEDHLQKLHEADLELQRKREYIEELEpptdsstaRRIEELQDSLQKKDADLRAMEER 597
Cdd:COG3096 615 REQSGEAlADSQEVTAAMQQLLEREREATVERDELAARKQALE--------SQIERLSQPGGAEDPRLLALAER 680
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
322-584 |
1.27e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 322 GELQELRRQVRQLEERNAghAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVT 401
Cdd:PRK02224 187 GSLDQLKAQIEEKEEKDL--HERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLR 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 402 KEKERLLTERDSLREANEELRcAQLQPRGLAQADLSLDptpSGLENLAAEILPAEL-----RETLVRLQLENKRLCQQEA 476
Cdd:PRK02224 265 ETIAETEREREELAEEVRDLR-ERLEELEEERDDLLAE---AGLDDADAEAVEARReeledRDEELRDRLEECRVAAQAH 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 477 -----ADRERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDPTLLKRKLEDHLQKLHEa 551
Cdd:PRK02224 341 neeaeSLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE- 419
|
250 260 270
....*....|....*....|....*....|....
gi 269784731 552 dlELQRKREYIEELEppTDSSTAR-RIEELQDSL 584
Cdd:PRK02224 420 --ERDELREREAELE--ATLRTAReRVEEAEALL 449
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
456-658 |
1.71e-05 |
|
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: 48.53 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 456 ELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDPT 535
Cdd:TIGR02169 713 DASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR 792
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 536 LlkRKLEDHLQKLHEadlELQRKREYIEELEPPTDSSTARRiEELQDSLQKKDADLRAMEERYRRYVDKARTVIQTLEPK 615
Cdd:TIGR02169 793 I--PEIQAELSKLEE---EVSRIEARLREIEQKLNRLTLEK-EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL 866
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 269784731 616 QRPPTVVSPEFHTLRSQLWERNLRIRQMEMDYEKSRRRQEQEE 658
Cdd:TIGR02169 867 EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
254-658 |
2.92e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 254 RLESSREDDRLRCLELEREVAELQQRNQALTSLSQEAQALKDEMDElrqsSERARQ-LEATLNSCRRRLGELQELRRQVR 332
Cdd:PRK02224 224 RYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAE----TEREREeLAEEVRDLRERLEELEEERDDLL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 333 QLEERNAGHAERTRQLEEEL-RRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTER 411
Cdd:PRK02224 300 AEAGLDDADAEAVEARREELeDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAV 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 412 DSLREANEELRCAqlqprgLAQADLSLDPTPSGLENLAAEIlpAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEE 491
Cdd:PRK02224 380 EDRREEIEELEEE------IEELRERFGDAPVDLGNAEDFL--EELREERDELREREAELEATLRTARERVEEAEALLEA 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 492 ANRARHGLE----------AQQRLNQQQLSELRAQVEELQKALQEQGGKTEDPTLLKRKLEDHLQKLHEADLELQRKREY 561
Cdd:PRK02224 452 GKCPECGQPvegsphvetiEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRET 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 562 IEELEPPTDSSTARRiEELQDSLQKKDADLRAMEERyrryVDKARTVIQTLEPKQRPPTVVSPEFHTLRSQLWERNLRIR 641
Cdd:PRK02224 532 IEEKRERAEELRERA-AELEAEAEEKREAAAEAEEE----AEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAED 606
|
410
....*....|....*..
gi 269784731 642 QMEMDYEKSRRRQEQEE 658
Cdd:PRK02224 607 EIERLREKREALAELND 623
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
381-594 |
3.68e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 381 MKAEKWLFECRNLEEKCDLVTKEKERLLTERDSLREANEELRCAQLQPRGLAQADLSLDPTPSGLENLAAEILPAELRET 460
Cdd:COG4717 40 LAFIRAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 461 LVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRlnqqQLSELRAQVEELQKALQEQGGKTEDPTL---- 536
Cdd:COG4717 120 KLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEE----ELEELEAELAELQEELEELLEQLSLATEeelq 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 537 -LKRKLEDHLQKLHEADLELQRKREYIEELEPPTDS-STARRIEELQDSLQKKDADLRAM 594
Cdd:COG4717 196 dLAEELEELQQRLAELEEELEEAQEELEELEEELEQlENELEAAALEERLKEARLLLLIA 255
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
267-634 |
4.00e-05 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 46.89 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 267 LELEREVAELQQRNQALTSLSQEAQALKDEMDELRQSSERARQLEATLNSCRRRLGELQELRRQVRQLEERNAGHAERTR 346
Cdd:COG4995 79 ALALAALALALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 347 QLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTERDSLREANEELRCAQL 426
Cdd:COG4995 159 AAAAAALLALALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 427 QPRGLAQADLSLDPTPSGLENLAAEILPAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLN 506
Cdd:COG4995 239 ALLALAAAAAALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALL 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 507 QQQLSELRAQVEELQKALQEQGGKTEDPTLLKRKLEDHLQKLHEADLELQRKREYIEELEPPTDSSTARRIEELQDSLQK 586
Cdd:COG4995 319 LLAALLLLLAALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAA 398
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 269784731 587 KDADLRAMEERYRRYVDKARTVIQTLEPKQRPPTVVSPEFHTLRSQLW 634
Cdd:COG4995 399 ALLALAAAQLLRLLLAALALLLALAAYAAARLALLALIEYIILPDRLY 446
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
328-610 |
4.26e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.04 E-value: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 328 RRQVRQLEERNAGHAERTRQLEEelrragSLRAQLEAQRRQVQeLQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERL 407
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEE------AEKARQAEMDRQAA-IYAEQERMAMERERELERIRQEERKRELERIRQEEI 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 408 LTERDSLREAnEELRCAQLQPRGLAQADLSLDPTPSGLENLAAEILPAELREtlvrlqLENKRLCQQEAadreRQEELQR 487
Cdd:pfam17380 371 AMEISRMREL-ERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVE------MEQIRAEQEEA----RQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 488 HLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKAL----QEQGGKTEDPTLLKRKLEDHLQKLHEADLELQRKREYIE 563
Cdd:pfam17380 440 LEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKleleKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLE 519
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 269784731 564 elepptdsstaRRIEELQDSLQKKDADLRAMEERYRRYVDKARTVIQ 610
Cdd:pfam17380 520 -----------KEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQ 555
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
483-596 |
5.51e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.87 E-value: 5.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 483 EELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKaLQEQGGKTEDPTLLKR--KLEDHLQKLHEADLELQRKRE 560
Cdd:COG3096 839 AALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNK-LLPQANLLADETLADRleELREELDAAQEAQAFIQQHGK 917
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 269784731 561 YIEELEPPTDS---------STARRIEELQDSLQKKDADLRAMEE 596
Cdd:COG3096 918 ALAQLEPLVAVlqsdpeqfeQLQADYLQAKEQQRRLKQQIFALSE 962
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
323-422 |
7.17e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 46.23 E-value: 7.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 323 ELQELRRQVRQLE-ERNAGHAERTRQLEEelrRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVT 401
Cdd:COG0542 412 ELDELERRLEQLEiEKEALKKEQDEASFE---RLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIP 488
|
90 100
....*....|....*....|.
gi 269784731 402 KEKERLLTERDSLREANEELR 422
Cdd:COG0542 489 ELEKELAELEEELAELAPLLR 509
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
253-600 |
1.02e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 253 FRLESSREDDRLRCLELEREVAELqqrNQALTSLSQEAQALKDEMdelrQSSERARQLEATLNSCRRRLGELQE-LRRQV 331
Cdd:PRK04863 296 YTSRRQLAAEQYRLVEMARELAEL---NEAESDLEQDYQAASDHL----NLVQTALRQQEKIERYQADLEELEErLEEQN 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 332 RQLEERNAGHAERTRQLEEELRRAGSLRAQL--------EAQRRQVQELQGQWQEEamKAEKWL----FECRNLEEKCD- 398
Cdd:PRK04863 369 EVVEEADEQQEENEARAEAAEEEVDELKSQLadyqqaldVQQTRAIQYQQAVQALE--RAKQLCglpdLTADNAEDWLEe 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 399 LVTKEKErlLTERdsLREANEELRCAQLQPRGLAQAdLSLdptpsgLENLAAEILPAE----LRETLVRLQlENKRLCQQ 474
Cdd:PRK04863 447 FQAKEQE--ATEE--LLSLEQKLSVAQAAHSQFEQA-YQL------VRKIAGEVSRSEawdvARELLRRLR-EQRHLAEQ 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 475 EAADRERQEELQRHLEEANRARHGL-EAQQRLN---------QQQLSELRAQVEELQKALQEQGgktEDPTLLKRKLED- 543
Cdd:PRK04863 515 LQQLRMRLSELEQRLRQQQRAERLLaEFCKRLGknlddedelEQLQEELEARLESLSESVSEAR---ERRMALRQQLEQl 591
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 269784731 544 -----HLQKLHEADLELQRKREYIEELEPPTDsSTARRIEELQDSLQKKDADLRAMEERYRR 600
Cdd:PRK04863 592 qariqRLAARAPAWLAAQDALARLREQSGEEF-EDSQDVTEYMQQLLERERELTVERDELAA 652
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
298-597 |
1.79e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 298 DELRQSSERARQLEATLnSCRRrlgelqELRRQVRQLEERNAGHAERTRQLEEELRRAGSLRAQLEAQR---------RQ 368
Cdd:PRK04863 273 DYMRHANERRVHLEEAL-ELRR------ELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASdhlnlvqtaLR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 369 VQELQGQWQEEAMKAEKwlfecrNLEEKCDLVTKEKERLLTERDSLREANEELRCAQ------------LQPRGL----- 431
Cdd:PRK04863 346 QQEKIERYQADLEELEE------RLEEQNEVVEEADEQQEENEARAEAAEEEVDELKsqladyqqaldvQQTRAIqyqqa 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 432 ------AQADLSLDP-TPSGLENLAAEILPAELRETLVRLQLENKRLCQQEAADR-ERQEELQRHL------EEANRARH 497
Cdd:PRK04863 420 vqalerAKQLCGLPDlTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQfEQAYQLVRKIagevsrSEAWDVAR 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 498 GLEAQ---QRLNQQQLSELRAQVEELQKALQEQGGKTEDPTLLKRKLEDHLQKLHEADLELQRKREYIEELEPPTDSSTA 574
Cdd:PRK04863 500 ELLRRlreQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARE 579
|
330 340
....*....|....*....|...
gi 269784731 575 RRiEELQDSLQKKDADLRAMEER 597
Cdd:PRK04863 580 RR-MALRQQLEQLQARIQRLAAR 601
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
268-564 |
1.89e-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: 44.78 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 268 ELEREVAELQQRNQALTSLSQEAQALKDEmdELRQS---SERARQLEATLNSCRRRLGELQELRRQV-RQLEERNAGHAE 343
Cdd:pfam01576 451 EAEGKNIKLSKDVSSLESQLQDTQELLQE--ETRQKlnlSTRLRQLEDERNSLQEQLEEEEEAKRNVeRQLSTLQAQLSD 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 344 RTRQLEEElrrAGSLRAQLEAQRRQVQELQGQWQEEAMKAEkwlfECRNLEEKCDLVTKEKERLLTERDSLREANEELRC 423
Cdd:pfam01576 529 MKKKLEED---AGTLEALEEGKKRLQRELEALTQQLEEKAA----AYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEK 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 424 AQ------LQPRGLAQADLSLDPTPSGLENLAAEILPAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARH 497
Cdd:pfam01576 602 KQkkfdqmLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVH 681
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 269784731 498 GLEAQQRLNQQQLSELRAQVEELQKALQEqggkTEDPTLlkrKLEDHLQKLH-EADLELQRKREYIEE 564
Cdd:pfam01576 682 ELERSKRALEQQVEEMKTQLEELEDELQA----TEDAKL---RLEVNMQALKaQFERDLQARDEQGEE 742
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
253-422 |
2.13e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.73 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 253 FRLESSREDDRLRC-LELEREVAELQQRNQaltslsQEAQALKDEMDELRQSSERARQLEAtlnscrRRLGELQELR-RQ 330
Cdd:pfam17380 383 LQMERQQKNERVRQeLEAARKVKILEEERQ------RKIQQQKVEMEQIRAEQEEARQREV------RRLEEERAREmER 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 331 VRQLEERNAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKW-LFECRNLEEKCDLVTKEKERLLT 409
Cdd:pfam17380 451 VRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQaMIEEERKRKLLEKEMEERQKAIY 530
|
170
....*....|...
gi 269784731 410 ERDSLREANEELR 422
Cdd:pfam17380 531 EEERRREAEEERR 543
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
254-608 |
2.17e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 254 RLESSREDDRLRCLELEREVAELQQRNQALTSLSQEAQALKDEMDELRQSSERARQLEATLNSCRRRLGELQELRRQVRQ 333
Cdd:PRK03918 218 ELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIK 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 334 LEERNAGHAERTRQLEEELrraGSLRAQLEAQRRQVQELQgqwqeeamkaekwlfecrNLEEKCDLVTKEKERLLTERDS 413
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRL---SRLEEEINGIEERIKELE------------------EKEERLEELKKKLKELEKRLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 414 LREANEELRCAQLQPRGLAQadLSLDPTPSGLENLAAEILPAELRETLVRLQLENkrLCQQEAADRERQEELQRHLEEAN 493
Cdd:PRK03918 357 LEERHELYEEAKAKKEELER--LKKRLTGLTPEKLEKELEELEKAKEEIEEEISK--ITARIGELKKEIKELKKAIEELK 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 494 RARH-----GLEAQQRLNQQQLSELRAQVEELQKALQEqggktedptlLKRKLEDHLQKLHEADLELQRKREYIEELEpp 568
Cdd:PRK03918 433 KAKGkcpvcGRELTEEHRKELLEEYTAELKRIEKELKE----------IEEKERKLRKELRELEKVLKKESELIKLKE-- 500
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 269784731 569 tdssTARRIEELQDSLQKKDA-DLRAMEERYRRYVDKARTV 608
Cdd:PRK03918 501 ----LAEQLKELEEKLKKYNLeELEKKAEEYEKLKEKLIKL 537
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
449-613 |
2.22e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 449 AAEILPAELRETLVRLQLENKRLCQQEAADRERQEELQRH---LEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQ 525
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALerrIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 526 EQGGKTED--PTLLKRKLEDHLQKLHEAD--LELQRKREYIEELEpPTDSSTARRIEELQDSLQKKDADLRAMEERYRRY 601
Cdd:COG4942 101 AQKEELAEllRALYRLGRQPPLALLLSPEdfLDAVRRLQYLKYLA-PARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170
....*....|..
gi 269784731 602 VDKARTVIQTLE 613
Cdd:COG4942 180 LAELEEERAALE 191
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
260-593 |
2.59e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 260 EDDRLRCLELEREVAElqqrnqaltslsqeaqaLKDEMDELRQSSERARQLEATlnscRRRLGELQELRRQVRQL-EERN 338
Cdd:PRK02224 471 EEDRERVEELEAELED-----------------LEEEVEEVEERLERAEDLVEA----EDRIERLEERREDLEELiAERR 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 339 AGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKwlfecrnLEEKCDLVTKEKERLLTERDSLREan 418
Cdd:PRK02224 530 ETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAE-------LNSKLAELKERIESLERIRTLLAA-- 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 419 eelrcaqlqprglaqadlsldptpsgLENLAAEIlpAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANrarhg 498
Cdd:PRK02224 601 --------------------------IADAEDEI--ERLREKREALAELNDERRERLAEKRERKRELEAEFDEAR----- 647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 499 leaqqrlnqqqLSELRAQVEELQKALQEQGGKTEDPTLLKRKLEDHLQKLHEADLELQRKREYIEELEPPTDS--STARR 576
Cdd:PRK02224 648 -----------IEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEAleALYDE 716
|
330
....*....|....*..
gi 269784731 577 IEELQDSLQKKDADLRA 593
Cdd:PRK02224 717 AEELESMYGDLRAELRQ 733
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
253-609 |
3.65e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.94 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 253 FRLESSRedDRLRCLElerEVAELQQRNqaLTSLSQEAQALKDEMDELRQSSERA----RQLEATLNSCRRRLGELQELR 328
Cdd:pfam05483 261 FLLEESR--DKANQLE---EKTKLQDEN--LKELIEKKDHLTKELEDIKMSLQRSmstqKALEEDLQIATKTICQLTEEK 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 329 R-QVRQLEERNAGHAERTRQLE------EELRRAGSLRaqLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLE---EKCD 398
Cdd:pfam05483 334 EaQMEELNKAKAAHSFVVTEFEattcslEELLRTEQQR--LEKNEDQLKIITMELQKKSSELEEMTKFKNNKEvelEELK 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 399 LVTKEKERLLTERDSLREANEELRCAQLQPRGLAQA------DLSLDPTPSG---------LENLAAEILPAELRETLV- 462
Cdd:pfam05483 412 KILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQArekeihDLEIQLTAIKtseehylkeVEDLKTELEKEKLKNIELt 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 463 ----RLQLENKRLCQqEAAD-----RERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQK----------A 523
Cdd:pfam05483 492 ahcdKLLLENKELTQ-EASDmtlelKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQkgdevkckldK 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 524 LQEQGGKTEDPTLLKRKLEDHLQ-KLHEADLELQRKREYIEELEPPTDS---------------------------STAR 575
Cdd:pfam05483 571 SEENARSIEYEVLKKEKQMKILEnKCNNLKKQIENKNKNIEELHQENKAlkkkgsaenkqlnayeikvnklelelaSAKQ 650
|
410 420 430
....*....|....*....|....*....|....
gi 269784731 576 RIEELQDSLQKKDADLRAMEERYRRYVDKARTVI 609
Cdd:pfam05483 651 KFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIA 684
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
181-626 |
4.29e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 181 SEEVEEGDHLQQHYLDLERQLLLLSEEKQNlAQENAALRERVGRSEVESAPGLT----AKKLLLLQSQLEQLQEENFRLE 256
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEAKKADEAKKAEEAKK-ADEAKKAEEKKKADELKKAEELKkaeeKKKAEEAKKAEEDKNMALRKAE 1584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 257 SSREDDRLRCLELEREVAELQQRNQALTSLSQEAQALKDEMDELRQSSERARQLEATLNSCRRRLGELQELRRQVRQLEE 336
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAA 1664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 337 RNAGHAERTRQLEEELRRAGSLRAQLEAQ-------RRQVQELQGQWQEEAMKAEkwlfECRNLEEKCDLVTKEKERllt 409
Cdd:PTZ00121 1665 EEAKKAEEDKKKAEEAKKAEEDEKKAAEAlkkeaeeAKKAEELKKKEAEEKKKAE----ELKKAEEENKIKAEEAKK--- 1737
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 410 ERDSLREANEELRCAQLQPRGLAQADLSLDPTPSGLENLAAEILPAELRETLVRLQLENKRLCQQEAADRER-QEELQRH 488
Cdd:PTZ00121 1738 EAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANiIEGGKEG 1817
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 489 LEEANRARHGLEAQQRLNQQQLSELRAQVEELQKAL-------QEQGGKTEDPTLLKRKLEDHLQKLHEADLELQRKREY 561
Cdd:PTZ00121 1818 NLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKfnknnenGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDD 1897
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269784731 562 IEElEPPTDSSTARRIEELQDSLQKkdadlramEERYRRYVDKARTVIQTLEPKQRPPTVVSPEF 626
Cdd:PTZ00121 1898 IER-EIPNNNMAGKNNDIIDDKLDK--------DEYIKRDAEETREEIIKISKKDMCINDFSSKF 1953
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
268-386 |
4.67e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 268 ELEREVAELQQRnqaLTSLSQEAQALKDEMDELRQS-SERARQLEATLNSCRRRL-GELQELRRQVRQLEERNAGHAERT 345
Cdd:COG3206 274 ELEAELAELSAR---YTPNHPDVIALRAQIAALRAQlQQEAQRILASLEAELEALqAREASLQAQLAQLEARLAELPELE 350
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 269784731 346 RQLEEELRRAGSLRAQLEAQRRQVQELQgqwQEEAMKAEKW 386
Cdd:COG3206 351 AELRRLEREVEVARELYESLLQRLEEAR---LAEALTVGNV 388
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
267-441 |
5.14e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 267 LELEREVAELQQRNQAltslSQEAQALKDEMDELRQSSERARQLEATLNSCRRRLGELQELRRQVRQLEERN-------- 338
Cdd:PRK04863 479 YQLVRKIAGEVSRSEA----WDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLgknldded 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 339 ---AGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWL----------------FECRNLEEKCDL 399
Cdd:PRK04863 555 eleQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLaaqdalarlreqsgeeFEDSQDVTEYMQ 634
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 269784731 400 VTKEKERLLT-ERDSLREANEELrcaQLQPRGLAQADLSLDPT 441
Cdd:PRK04863 635 QLLERERELTvERDELAARKQAL---DEEIERLSQPGGSEDPR 674
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
263-378 |
6.01e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.15 E-value: 6.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 263 RLRcLELEREVAELQQRNQALTSLSQEAQALKDEMDELrqSSERARQLEAtlnscrrrlgELQELRRQVRQLEERNagHA 342
Cdd:COG0542 401 RVR-MEIDSKPEELDELERRLEQLEIEKEALKKEQDEA--SFERLAELRD----------ELAELEEELEALKARW--EA 465
|
90 100 110
....*....|....*....|....*....|....*.
gi 269784731 343 ERtrqleEELRRAGSLRAQLEAQRRQVQELQGQWQE 378
Cdd:COG0542 466 EK-----ELIEEIQELKEELEQRYGKIPELEKELAE 496
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
206-706 |
1.25e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 206 EEKQNLAQENAALRERVGRSEVESApgltAKKLLLLQSQLEQLQEENFRLESSREDDRLRCLELEREVAELQQR-----N 280
Cdd:COG4913 262 ERYAAARERLAELEYLRAALRLWFA----QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgngG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 281 QALTSLSQEAQALKDEMDELRQSSERARQLEATLNScrRRLGELQELRRQVRQLEERNAGHAERTRQLEEELRRAGSLRA 360
Cdd:COG4913 338 DRLEQLEREIERLERELEERERRRARLEALLAALGL--PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 361 QLEAQRRQVQ-ELQGQWQ------EEAMKAEKWLfeCRNLEEK-------CDLV---TKEKE--------------RLLT 409
Cdd:COG4913 416 DLRRELRELEaEIASLERrksnipARLLALRDAL--AEALGLDeaelpfvGELIevrPEEERwrgaiervlggfalTLLV 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 410 ERDSLREANEELRCAQLQPR---GLAQADLSLDPTPSGLENLAAEIL---PAELRETLvrlqlenkrlcQQEAADR---- 479
Cdd:COG4913 494 PPEHYAAALRWVNRLHLRGRlvyERVRTGLPDPERPRLDPDSLAGKLdfkPHPFRAWL-----------EAELGRRfdyv 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 480 --ERQEELQRH--------LEEANRARHGLEAQQRL---------NQQQLSELRAQVEELQKALQEQGGKTEDptllKRK 540
Cdd:COG4913 563 cvDSPEELRRHpraitragQVKGNGTRHEKDDRRRIrsryvlgfdNRAKLAALEAELAELEEELAEAEERLEA----LEA 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 541 LEDHLQKLHEADLELQRKREYIEELEpptdsSTARRIEELQD---SLQKKDADLRAMEERyrryVDKARTVIQTLEpkqr 617
Cdd:COG4913 639 ELDALQERREALQRLAEYSWDEIDVA-----SAEREIAELEAeleRLDASSDDLAALEEQ----LEELEAELEELE---- 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 618 pptvvsPEFHTLRSQLWERNLRIRQMEMDYEKSRRRQEQEEKLLISAWYSMGMALEHRAGEEHAPAHAQSFLAQQRLATN 697
Cdd:COG4913 706 ------EELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALR 779
|
....*....
gi 269784731 698 ARRGPLGRQ 706
Cdd:COG4913 780 ARLNRAEEE 788
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
323-599 |
1.27e-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: 42.25 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 323 ELQELRRQVRQLEERNAGHAERTRQleeelrragsLRAQLEAQRRQVQELQGqwqeeaMKAEKWLFECRNLEEKCDLVTK 402
Cdd:COG3096 837 ELAALRQRRSELERELAQHRAQEQQ----------LRQQLDQLKEQLQLLNK------LLPQANLLADETLADRLEELRE 900
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 403 EKERLLTERDSLREANEelRCAQLQPrglaQADlSLDPTPSGLENLAAEILPAELRETLVRLQLE------NKRL----- 471
Cdd:COG3096 901 ELDAAQEAQAFIQQHGK--ALAQLEP----LVA-VLQSDPEQFEQLQADYLQAKEQQRRLKQQIFalsevvQRRPhfsye 973
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 472 --CQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLSE-----------LRAQVEELQKALQE--QGGKTEDPTL 536
Cdd:COG3096 974 daVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQynqvlaslkssRDAKQQTLQELEQEleELGVQADAEA 1053
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 269784731 537 LKRKlEDHLQKLHEadlELQRKREYIEELEpptdsSTARRIEELQDSLQKKdadLRAMEERYR 599
Cdd:COG3096 1054 EERA-RIRRDELHE---ELSQNRSRRSQLE-----KQLTRCEAEMDSLQKR---LRKAERDYK 1104
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
268-588 |
1.42e-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: 42.26 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 268 ELEREVAELQQRNQALTSLSQEaqaLKDEMDELRQSSERARQLEATLNSCRRRLGELQELRRQVRQLEERNAGHAERTRQ 347
Cdd:TIGR00618 560 SLKEQMQEIQQSFSILTQCDNR---SKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQ 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 348 LEEELRRAGSLRAQLE---AQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTERDSLREANEELRCA 424
Cdd:TIGR00618 637 CSQELALKLTALHALQltlTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEY 716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 425 QLQPRGLAQADLSLDPTPSGLENLAAEILP---AELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEA 501
Cdd:TIGR00618 717 DREFNEIENASSSLGSDLAAREDALNQSLKelmHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREE 796
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 502 QQRLNQQQLSELRAQV-EELQKALQEQGGKTEDPTLLKRKLEDHLQKLHEADLELQRKREYIEELEPPTDSStaRRIEEL 580
Cdd:TIGR00618 797 DTHLLKTLEAEIGQEIpSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQ--AKIIQL 874
|
....*...
gi 269784731 581 QDSLQKKD 588
Cdd:TIGR00618 875 SDKLNGIN 882
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
261-550 |
2.62e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 41.32 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 261 DDRLRCLELEREVA------------------ELQQRNQALTSLSQEAQALKDEMDELRQSSERARQLEATLNSCrrrLG 322
Cdd:PRK10246 527 VNQSRLDALEKEVKklgeegaalrgqldaltkQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQPW---LD 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 323 ELQELRRQVRQLEERNAghaertrqleeelrragsLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFEC-----RNLEEKC 397
Cdd:PRK10246 604 AQEEHERQLRLLSQRHE------------------LQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYaltlpQEDEEAS 665
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 398 DLVTKEKERLLTERDSLREANEELRCAQLQPRglaqadLSLDPTPSGLENLAAEILPAELRET---LVRLQLENKRLCQQ 474
Cdd:PRK10246 666 WLATRQQEAQSWQQRQNELTALQNRIQQLTPL------LETLPQSDDLPHSEETVALDNWRQVheqCLSLHSQLQTLQQQ 739
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 475 EAADRERQEELQRHLEEA------------------NRARHGLEAQ-QRLNQ--QQLSELRAQVEELQKALQEQGGKTED 533
Cdd:PRK10246 740 DVLEAQRLQKAQAQFDTAlqasvfddqqaflaalldEETLTQLEQLkQNLENqrQQAQTLVTQTAQALAQHQQHRPDGLD 819
|
330
....*....|....*..
gi 269784731 534 PTLLKRKLEDHLQKLHE 550
Cdd:PRK10246 820 LTVTVEQIQQELAQLAQ 836
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
260-597 |
2.97e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.88 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 260 EDDRLRCLELEREVAELQQRNQALTSLSQEAQALKDEMDELRQSSERARQLEATLNScrrrlgELQELRRQVRQLEERNA 339
Cdd:pfam05557 76 ELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNS------ELEELQERLDLLKAKAS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 340 GHAERTRQLEEELRRAGSLRAQLEAQRRQVQeLQGQWQEEAMKAEKWLFECRNLEekcdlvtKEKERLLTERDSLREANE 419
Cdd:pfam05557 150 EAEQLRQNLEKQQSSLAEAEQRIKELEFEIQ-SQEQDSEIVKNSKSELARIPELE-------KELERLREHNKHLNENIE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 420 -----ELRCAQLQPRGLAQADLSLDPTPSGLENlaaEILPAELRETLVRLQLENKRLCQQEAADRERQEELQR---HLEE 491
Cdd:pfam05557 222 nklllKEEVEDLKRKLEREEKYREEAATLELEK---EKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQReivLKEE 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 492 ----ANRARHgLEAQQRLNQQQLSELRAQVEELQKALQEQGGktedptlLKRKLEDHLQKL-HEADLELQRKREYIEELE 566
Cdd:pfam05557 299 nsslTSSARQ-LEKARRELEQELAQYLKKIEDLNKKLKRHKA-------LVRRLQRRVLLLtKERDGYRAILESYDKELT 370
|
330 340 350
....*....|....*....|....*....|..
gi 269784731 567 PP-TDSSTARRIEELQDSLQKKDADLRAMEER 597
Cdd:pfam05557 371 MSnYSPQLLERIEEAEDMTQKMQAHNEEMEAQ 402
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
281-453 |
3.70e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.61 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 281 QALTSLSQEAQALKDEmDELRQSSERARQLEATLNSCRRRLGELQELRRQVRQLEERNAGHAERTRQLEEELRRAGS--- 357
Cdd:COG2433 380 EALEELIEKELPEEEP-EAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSeer 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 358 --LRAQLEAQRRQ--VQELQGQWQEEAMKAEKW------LFECRNLEEKCDLVTKEKERLLTeRDSLREANEELrcaqlq 427
Cdd:COG2433 459 reIRKDREISRLDreIERLERELEEERERIEELkrklerLKELWKLEHSGELVPVKVVEKFT-KEAIRRLEEEY------ 531
|
170 180
....*....|....*....|....*.
gi 269784731 428 prGLAQADLSLDPTPSGLENLAAEIL 453
Cdd:COG2433 532 --GLKEGDVVYLRDASGAGRSTAELL 555
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
319-566 |
4.35e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.44 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 319 RRLGEL----------QELRRQVRQLE--ERNAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQgqwQEEAMkaekW 386
Cdd:COG0497 119 RELGELlvdihgqhehQSLLDPDAQREllDAFAGLEELLEEYREAYRAWRALKKELEELRADEAERA---RELDL----L 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 387 LFECRNLEEkCDLVTKEKERLLTERDSLREAnEELRcaqlqpRGLAQADLSLDPTPSGLENLAAEI---------LPAEL 457
Cdd:COG0497 192 RFQLEELEA-AALQPGEEEELEEERRRLSNA-EKLR------EALQEALEALSGGEGGALDLLGQAlralerlaeYDPSL 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 458 RETLVRL-----QLEnkrlcqqEAADrerqeELQRHLE--EANRARhgLEA-QQRLNQ---------QQLSELRAQVEEL 520
Cdd:COG0497 264 AELAERLesaliELE-------EAAS-----ELRRYLDslEFDPER--LEEvEERLALlrrlarkygVTVEELLAYAEEL 329
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 269784731 521 QKALQEQGGKTEDPTLLKRKLEDHLQKLHEADLELQRKR-EYIEELE 566
Cdd:COG0497 330 RAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARkKAAKKLE 376
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
268-612 |
4.41e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.59 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 268 ELEREVAELQQRNQALTSLSQEAQ----ALKDEMDELRQSSERARQ-LEATLNSCRRRLGELQELRRQVrqleernagha 342
Cdd:pfam12128 601 ELRERLDKAEEALQSAREKQAAAEeqlvQANGELEKASREETFARTaLKNARLDLRRLFDEKQSEKDKK----------- 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 343 erTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEE---------AMKAEKWLFECRNLEEKCDLVTKEKERLLTERDS 413
Cdd:pfam12128 670 --NKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEqkeqkrearTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKA 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 414 LREANEELRCAQLQprglaqadlSLDPTPSGLENLAAEIlpaelrETLVRlQLENKRLCQQEAADRERQEELQRHLEEAN 493
Cdd:pfam12128 748 ELKALETWYKRDLA---------SLGVDPDVIAKLKREI------RTLER-KIERIAVRRQEVLRYFDWYQETWLQRRPR 811
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 494 RArhgleaqqrlnqQQLSELRAQVEELQkalQEQGGKTEDPTLLKRKLEDHL----QKLHEADLELQRKREYIEEL---- 565
Cdd:pfam12128 812 LA------------TQLSNIERAISELQ---QQLARLIADTKLRRAKLEMERkaseKQQVRLSENLRGLRCEMSKLatlk 876
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 269784731 566 EPPTDSSTARRIEELQDSLQKKDADLRAMEERYRRYVDKARTVIQTL 612
Cdd:pfam12128 877 EDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVIADH 923
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
310-659 |
4.69e-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: 40.32 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 310 LEATLNSCRRRLGELQELRRQ-------------------VRQLEERNaGHAERTRQLEEELrrAGSLRAQLEAQRRQV- 369
Cdd:COG3096 234 MEAALRENRMTLEAIRVTQSDrdlfkhliteatnyvaadyMRHANERR-ELSERALELRREL--FGARRQLAEEQYRLVe 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 370 --QELQGQWQEEAM------KAEKWLFECRN---------------------LEEKCDLVTKEKERLLTERDSLREANEE 420
Cdd:COG3096 311 maRELEELSARESDleqdyqAASDHLNLVQTalrqqekieryqedleelterLEEQEEVVEEAAEQLAEAEARLEAAEEE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 421 LRCAQ------------LQPRGL-----------AQADLSLDP-TPSGLENLAAEILPAELRETLVRLQLENKRLCQQEA 476
Cdd:COG3096 391 VDSLKsqladyqqaldvQQTRAIqyqqavqalekARALCGLPDlTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAA 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 477 ADRERQ--EELQRHLEEANRARHGLEAQQRLNQ--------QQLSELRAQVEELQKALQEQGGKTEDPTLLKRKLEDHLQ 546
Cdd:COG3096 471 RRQFEKayELVCKIAGEVERSQAWQTARELLRRyrsqqalaQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLD 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 547 KLHEADLELQRKREYIEELEPPTDSSTARRIEELQ--DSLQKKDADLRAMEERYRryvdKARTVIQTLEPKQRPPTVVSP 624
Cdd:COG3096 551 AAEELEELLAELEAQLEELEEQAAEAVEQRSELRQqlEQLRARIKELAARAPAWL----AAQDALERLREQSGEALADSQ 626
|
410 420 430
....*....|....*....|....*....|....*
gi 269784731 625 EFHTLRSQLWERNlriRQMEMDYEKSRRRQEQEEK 659
Cdd:COG3096 627 EVTAAMQQLLERE---REATVERDELAARKQALES 658
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
185-422 |
6.06e-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: 6.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 185 EEGDHLQQHYldlerqlLLLSEEKQNLAQENAALRERVGRSEVESApgltakkllllqsqleqlqeenfRLESSREDDRL 264
Cdd:TIGR02168 281 EEIEELQKEL-------YALANEISRLEQQKQILRERLANLERQLE-----------------------ELEAQLEELES 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 265 RCLELEREVAELQQRnqaLTSLSQEAQALKDEMDELRQSSERARQLEATLNScrrrlgELQELRRQVRQLEERNAGHAER 344
Cdd:TIGR02168 331 KLDELAEELAELEEK---LEELKEELESLEAELEELEAELEELESRLEELEE------QLETLRSKVAQLELQIASLNNE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 345 TRQLEEELRRAGSLRAQLEAQRR---------QVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTERDSLR 415
Cdd:TIGR02168 402 IERLEARLERLEDRRERLQQEIEellkkleeaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
....*..
gi 269784731 416 EANEELR 422
Cdd:TIGR02168 482 RELAQLQ 488
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
274-526 |
7.05e-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: 39.94 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 274 AELQQRNQALTSLSQEAQALKDEMDELRQSSERARQLEATLN-------------------SCRRRLGELQELRRQVRQl 334
Cdd:COG3096 836 AELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNkllpqanlladetladrleELREELDAAQEAQAFIQQ- 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 335 eernagHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAE------------KWLFECRNLEEKCDLVTK 402
Cdd:COG3096 915 ------HGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFalsevvqrrphfSYEDAVGLLGENSDLNEK 988
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 403 EKERLLTERDSLREANEELRCAQLQPRGLAQADLSLDptpSGLENlAAEILpAELRETLVRLQLENkrlcQQEAADRERQ 482
Cdd:COG3096 989 LRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLK---SSRDA-KQQTL-QELEQELEELGVQA----DAEAEERARI 1059
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 269784731 483 EELQRHlEEANRARhgleaqQRLNQ--QQLSELRAQVEELQKALQE 526
Cdd:COG3096 1060 RRDELH-EELSQNR------SRRSQleKQLTRCEAEMDSLQKRLRK 1098
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
247-564 |
7.32e-03 |
|
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: 39.49 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 247 QLQEENFRLESSREDDRLRCLELEREVAELQQRnqaLTSLSQEAQALKDEMDELRQSSERARQLEATLNSCRRRLGELQE 326
Cdd:pfam07888 49 AQEAANRQREKEKERYKRDREQWERQRRELESR---VAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 327 LRRQ-VRQLEERNAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQElqgqwqeeamkaekwlfECRNLEEKCDLVTKEKE 405
Cdd:pfam07888 126 AHEArIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEA-----------------ERKQLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 406 RLLTERDSLREANEElRCAQLQPRGLAQADLSLDPTPSGLENLAAEILPAELRETLVRLqlenkrlcqqeAADRERQEEL 485
Cdd:pfam07888 189 SLSKEFQELRNSLAQ-RDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERL-----------NASERKVEGL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 486 QRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQE-QGGKTEDPTLLKRKLEDHLQKLHEADLELQRKREYIEE 564
Cdd:pfam07888 257 GEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREgRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQE 336
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
254-604 |
8.10e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 39.70 E-value: 8.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 254 RLESSREDDRLRCLELEREVAELQQRN----------QALTSLSQEAQALKDEMDELRQSSERARQLEATLNS-CRRRLG 322
Cdd:pfam05483 371 RLEKNEDQLKIITMELQKKSSELEEMTkfknnkevelEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFlLQAREK 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 323 ELQELRRQVRQLEERNAGHAERTRQLEEELRRAGSLRAQLEAqrrQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTK 402
Cdd:pfam05483 451 EIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTA---HCDKLLLENKELTQEASDMTLELKKHQEDIINCKK 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 403 EKERLLTERDSLREANEELR--CAQLQPRGLAQAD---LSLDPTPSGLENLAAEILPAELRETLVRLQLENKrlcqqeaa 477
Cdd:pfam05483 528 QEERMLKQIENLEEKEMNLRdeLESVREEFIQKGDevkCKLDKSEENARSIEYEVLKKEKQMKILENKCNNL-------- 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784731 478 dRERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDPTLLKRKlEDHLQKLHEADL--EL 555
Cdd:pfam05483 600 -KKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQK-EIEDKKISEEKLleEV 677
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 269784731 556 QRKREYIEElepptdssTARRIEELQDSLQKKDADLRAMEERYRRYVDK 604
Cdd:pfam05483 678 EKAKAIADE--------AVKLQKEIDKRCQHKIAEMVALMEKHKHQYDK 718
|
|
| |
