|
Name |
Accession |
Description |
Interval |
E-value |
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
179-678 |
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: 526.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 179 FLSEEVEEGDHLQQHYLDLERQLLLLSEEKQNLAQENAALRERVGRSEVESAPG-LTAKKLLLLQSQLEQLQEENFRLES 257
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGtPGGKKYLLLQKQLEQLQEENFRLET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 258 SREDDRLRCLELEREVAELQQRNQALTSLSQEAQALKDEMDELRQSSERA------------------------RQLEER 313
Cdd:pfam05622 81 ARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDKVkkleatvetykkkledlgdlrrqvKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 314 NAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTERDSLREA 393
Cdd:pfam05622 161 NAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRET 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 394 NEELRCAQLQPRGLAQADLSLDPTPSGLENLAAEILPAELRETLVRLQLENKRL-CQQEAADRERQEELQRHLEEANRAR 472
Cdd:pfam05622 241 NEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLrLGQEGSYRERLTELQQLLEDANRRK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 473 HGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDPTLLKRKLEDHLQKLHEADLELQRKREYIEELEPPTDSSTARR 552
Cdd:pfam05622 321 NELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 553 IEELQDSLQKKDADLRAMEERYRRYVDKARTVIQTLEPKQRPptVVSPEFHTLRSQLWERNLRIRQMEMDYEKSRRRQEQ 632
Cdd:pfam05622 401 IDELQEALRKKDEDMKAMEERYKKYVEKAKSVIKTLDPKQNP--ASPPEIQALKNQLLEKDKKIEHLERDFEKSKLQREQ 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1390249220 633 EEKLLISAWYSMGMALEHRAGEEHAP---AHAQSFLAQQRLATNARRGP 678
Cdd:pfam05622 479 EEKLIVTAWYNMGMALHRKAIEERLAglsSPGQSFLARQRQATNARRGL 527
|
|
| HkD_Hook2 |
cd22227 |
Hook domain found in protein Hook 2 (Hook2) and similar proteins; Hook2 is a ... |
7-156 |
1.02e-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: 1.02e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 7 ELCGSLLTWLQTFQVSPPCASPQDLSSGLAIAHVLNQIDPSWFNNEWLQGISEDSSPSWRLKVRKLEKILQSLVEYSKNV 86
Cdd:cd22227 1 ELCDSLLTWLQTFQVPSPCSSYQDLTSGVAIAQVLNRIDPSWFNEAWLGRIKEDTGDNWRLKVSNLKKILQSLLEYYQDV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 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 |
2.54e-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: 2.54e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 7 ELCGSLLTWLQTFQVSPPCASPQDLSSGLAIAHVLNQIDPSWFNNEWLQGISEDSSPSWRLKVRKLEKILQSLVEYSKNV 86
Cdd:pfam19047 1 ELCDSLLTWLQTFNVPAPCATVEDLTDGVAMAQVLHQIDPSWFTEAWLSRIKEDVGDNWRLKVSNLKKILQSVVDYYQDV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390249220 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 |
2.06e-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: 238.68 E-value: 2.06e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 9 CGSLLTWLQTFQVSPPCASPQDLSSGLAIAHVLNQIDPSWFNNEWLQGISEDSSPSWRLKVRKLEKILQSLVEYSKNVLG 88
Cdd:cd22222 1 CDSLLQWLQTFNLIAPHATAEDLSDGVAIAQVLNQIDPEYFSDSWLSKIKPDVGDNWRLKVSNLKKILKGIVDYYSEVLG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249220 89 HPVSDQHLPDVSLIGEFSNPAELGKLLQLVLGCAISCEKKQEYIQRIMTLEESVQHVVMEAIQELMT 155
Cdd:cd22222 81 QQISGFTMPDVNAIAEKEDPKELGRLLQLVLGCAVNCERKEEYIQAIMGLEESVQHVVMEAIQELMS 147
|
|
| HkD_Hook1 |
cd22225 |
Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a ... |
8-157 |
4.31e-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: 4.31e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 8 LCGSLLTWLQTFQVSPPCASPQDLSSGLAIAHVLNQIDPSWFNNEWLQGISEDSSPSWRLKVRKLEKILQSLVEYSKNVL 87
Cdd:cd22225 1 LCDSLIIWLQTFNTAAPCQTVQDLTSGVAMAQVLHQIDSSWFDESWLSRIKEDVGDNWRIKMSNLKKILQGIVDYYHEFL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 88 GHPVSDQHLPDVSLIGEFSNPAELGKLLQLVLGCAISCEKKQEYIQRIMTLEESVQHVVMEAIQELMTKD 157
Cdd:cd22225 81 DQQISEFLLPDLNRIAEHSDPVELGRLLQLILGCAVNCEKKQEHIQNIMTLEESVQHVVMTAIQELMSKE 150
|
|
| HkD_Hook3 |
cd22226 |
Hook domain found in protein Hook 3 (Hook3) and similar proteins; Hook3 is an adaptor protein ... |
4-156 |
4.33e-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: 4.33e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 4 DKAELCGSLLTWLQTFQVSPPCASPQDLSSGLAIAHVLNQIDPSWFNNEWLQGISEDSSPSWRLKVRKLEKILQSLVEYS 83
Cdd:cd22226 1 DRAELCESLLTWIQTFNVDAPCQTVEDLTSGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390249220 84 KNVLGHPVSDQHLPDVSLIGEFSNPAELGKLLQLVLGCAISCEKKQEYIQRIMTLEESVQHVVMEAIQELMTK 156
Cdd:cd22226 81 HEILGQQINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMSK 153
|
|
| HkD_SF |
cd22211 |
Hook domain-containing proteins superfamily; The Hook domain superfamily includes Hook adaptor ... |
11-154 |
4.81e-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: 4.81e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 11 SLLTWLQTFQVSPPCASPQDLSSGLAIAHVLNQIDPSWFNNEWLQgiSEDSSPSWRLKVRKLEKILQSLVEYSKNVLGHP 90
Cdd:cd22211 3 ALLAWINTFPLSSPVESLDDLSDGVVLAEILSQIDPSYFDSEWLE--SRDSSDNWVLKLNNLKKLYRSLSKYYREVLGQQ 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390249220 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 |
6.84e-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: 6.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 8 LCGSLLTWLQTFQVSPPCA-SPQDLSSGLAIAHVLNQIDPSWFNnewlQGISEDSSPSWRLKVRKLEKILQSLVEYSKNV 86
Cdd:cd22223 2 LSSPLVTWAKTFADDGSAElSYTDLVDGVFLNNVMLQIDPRPFS----EVSNRNVDDDVNARIQNLDLLLRNIKSFYQEV 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390249220 87 LGHPVSdQHLPDVSLIGEFSNP----AELGKLLQLVLGCAISCEKKQEYIQRIMTLEESVQHVVMEAIQEL 153
Cdd:cd22223 78 LQQLIV-MKLPDILTIGREPESeqslEELEKLLLLLLGCAVQCERKEEFIERIKNLDLEVQHALVACIQEV 147
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
259-681 |
1.65e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.20 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 259 REDDRLRclELEREVAELQ-QRNQAltslsQEAQALKDEMDElRQSSERARQLEERNAGHAERTRQLEEelrragsLRAQ 337
Cdd:COG1196 190 RLEDILG--ELERQLEPLErQAEKA-----ERYRELKEELKE-LEAELLLLKLRELEAELEELEAELEE-------LEAE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 338 LEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTERDSLREANEELRCAQLQprglaqadlsldpt 417
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE-------------- 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 418 psglenLAAEIlpAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQ 497
Cdd:COG1196 321 ------LEEEL--AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 498 KALQEQGGKTEDPTLLKRKLEDHLQKLHEADLELQRKREYIEELEPPTDSSTARRIEELQDSLQKKDADLRAMEERYRRY 577
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 578 VDKARTVIQTLEPKQRpptvvspefhtLRSQLWERNLRIRQMEMDYEKSRRRQEQEEK--------LLISAWYSMGMALE 649
Cdd:COG1196 473 ALLEAALAELLEELAE-----------AAARLLLLLEAEADYEGFLEGVKAALLLAGLrglagavaVLIGVEAAYEAALE 541
|
410 420 430
....*....|....*....|....*....|..
gi 1390249220 650 HRAGEEHAPAHAQSFLAQQRLATNARRGPLGR 681
Cdd:COG1196 542 AALAAALQNIVVEDDEVAAAAIEYLKAAKAGR 573
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
254-572 |
3.05e-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: 73.55 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 254 RLESSREDDRLR--CLELEREVAELQqrnQALTSLSQEAQALKDEMDELRQSSERARQ----LEERNAGHAERTRQLEEE 327
Cdd:TIGR02168 672 ILERRREIEELEekIEELEEKIAELE---KALAELRKELEELEEELEQLRKELEELSRqisaLRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 328 LRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEkwlfecRNLEEKCDLVTKEKERLLTERDSLREANEELRcaQLQPRGL 407
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAE------AEIEELEAQIEQLKEELKALREALDELRAELT--LLNEEAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 408 AQAdlsldptpSGLENLAAEIlpAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLS 487
Cdd:TIGR02168 821 NLR--------ERLESLERRI--AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 488 ELRAQVEELQKALQEQGGK----TEDPTLLKRKLEDHLQKLHEADLELQRKREY-----------IEELEPPTDSSTA-- 550
Cdd:TIGR02168 891 LLRSELEELSEELRELESKrselRRELEELREKLAQLELRLEGLEVRIDNLQERlseeysltleeAEALENKIEDDEEea 970
|
330 340
....*....|....*....|....
gi 1390249220 551 -RRIEELQDSLQK-KDADLRAMEE 572
Cdd:TIGR02168 971 rRRLKRLENKIKElGPVNLAAIEE 994
|
|
| HkD_Daple |
cd22228 |
Hook domain found in Daple (Dvl-associating protein with a high frequency of leucine residues) ... |
12-153 |
4.89e-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: 4.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 12 LLTWLQTFQvspPCASPQ--------DLSSGLAIAHVLNQIDPSWFNnewlQGISEDSSPSWRLKVRKLEKILQSLVEYS 83
Cdd:cd22228 6 LVTWVKTFG---PLGFGSedklsmymDLVDGVFLNKIMLQIDPRPTN----QRVNKHVNNDVNLRIQNLTILVRHIKTYY 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249220 84 KNVLGHPVSdQHLPDVSLIGEfsNP------AELGKLLQLVLGCAISCEKKQEYIQRIMTLEESVQHVVMEAIQEL 153
Cdd:cd22228 79 QEVLQQLIV-MNLPNVLMIGK--DPlsgksmEEIKKMLLLVLGCAVQCERKEEFIERIKQLDIETQAAIVSHIQEV 151
|
|
| HkD_Girdin |
cd22229 |
Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation ... |
12-153 |
2.41e-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: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 12 LLTWLQTFQVSPPCASPQ-----DLSSGLAIAHVLNQIDPSWFNNEWLQGISEDSSpswrLKVRKLEKILQSLVEYSKNV 86
Cdd:cd22229 9 LVTWVKTFGPLATGNGTPldeyvALVDGVFLNEVMLQINPKSSNQRVNKKVNNDAS----LRIQNLSILVKQIKLYYQET 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390249220 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 ... |
268-572 |
9.98e-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: 68.56 E-value: 9.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 268 ELEREVAELQQRNQALTSLSQEA-QALKDEMDELRQSSERARQLEERNAGHAERTRQLEEELRragSLRAQLEAQRRQVQ 346
Cdd:TIGR02169 685 GLKRELSSLQSELRRIENRLDELsQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS---SLEQEIENVKSELK 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 347 ELQGQWQEEAMKAEKWLFECRNLEEKCDlvtkeKERLLTERDSLREANEELRCAQLQPRGLAQADLSLDptpsgLENLAA 426
Cdd:TIGR02169 762 ELEARIEELEEDLHKLEEALNDLEARLS-----HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT-----LEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 427 EILPAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGK 506
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ 911
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249220 507 TEDPTLLKRKLEDHLQKLHEADLELQRKREYIEELEPPTDSstarrIEELQDSLQKKDADLRAMEE 572
Cdd:TIGR02169 912 IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS-----LEDVQAELQRVEEEIRALEP 972
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
255-501 |
6.09e-10 |
|
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: 62.78 E-value: 6.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 255 LESSREDDRLRCLELEREVAELQQRNQALTS----------------LSQEAQALKDEMDELRQSSERARQLEERNAGHA 318
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGEeeqlrvkekigeleaeIASLERSIAEKERELEDAEERLAKLEAEIDKLL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 319 ERTRQLEEELRRAGSLRAQLEAQ----RRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTERDSLREAN 394
Cdd:TIGR02169 336 AEIEELEREIEEERKRRDKLTEEyaelKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEEL 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 395 EELRCAQLQPRG-LAQADLSLDPTPSGLENLAAEIlpAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARH 473
Cdd:TIGR02169 416 QRLSEELADLNAaIAGIEAKINELEEEKEDKALEI--KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA 493
|
250 260
....*....|....*....|....*...
gi 1390249220 474 GLEAQQRLNQQQLSELRAQVEELQKALQ 501
Cdd:TIGR02169 494 EAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
268-524 |
1.43e-09 |
|
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: 61.61 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 268 ELEREVAELQQRNQALTSLSQEAQALKDE-MDELRQSSERARQLEERNAGHAERTRQLEEELRRagsLRAQLEAQRRQVQ 346
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEElRLEVSELEEEIEELQKELYALANEISRLEQQKQI---LRERLANLERQLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 347 ELQGQWQEEAMKAEKwlfecrnLEEKCDLVTKEKERLLTERDSLREANEELRcAQLQPRGLAQADLSldptpSGLENLAA 426
Cdd:TIGR02168 320 ELEAQLEELESKLDE-------LAEELAELEEKLEELKEELESLEAELEELE-AELEELESRLEELE-----EQLETLRS 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 427 EILPAELRETLVRLQLEN-------------KRLCQQEAADRERQE----ELQRHLEEANRARHGLEAQQRLNQQQLSEL 489
Cdd:TIGR02168 387 KVAQLELQIASLNNEIERlearlerledrreRLQQEIEELLKKLEEaelkELQAELEELEEELEELQEELERLEEALEEL 466
|
250 260 270
....*....|....*....|....*....|....*
gi 1390249220 490 RAQVEELQKALQEQGGKTEDPTLLKRKLEDHLQKL 524
Cdd:TIGR02168 467 REELEEAEQALDAAERELAQLQARLDSLERLQENL 501
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
256-636 |
8.82e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.00 E-value: 8.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 256 ESSREDDRLRCLELEREVAELQQRNQALTSLSQEAQAlKDEMDELRQSSERARQLEERNAGH---AERTRQLEEELRRAG 332
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE-ARKADELKKAEEKKKADEAKKAEEkkkADEAKKKAEEAKKAD 1318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 333 SLRAQLEAQRRQVQELQGQWQEEAMKAE-------KWLFECRNLEEKCDLVTKEKERLLTERDSLREANEELRCAQLQPR 405
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKKAEEAKKAAEaakaeaeAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKK 1398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 406 GLAQADLSLDPtpsgLENLAAEILPAElretlvrlqlENKRlcqqEAADRERQEELQRHLEEANRA----RHGLEAQQRL 481
Cdd:PTZ00121 1399 KAEEDKKKADE----LKKAAAAKKKAD----------EAKK----KAEEKKKADEAKKKAEEAKKAdeakKKAEEAKKAE 1460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 482 NQQQLSELRAQVEELQKALQEQGGKTEdptlLKRKLEDHLQKlheADlELQRKREYIEELEPPTDSSTARRIEELQDSLQ 561
Cdd:PTZ00121 1461 EAKKKAEEAKKADEAKKKAEEAKKADE----AKKKAEEAKKK---AD-EAKKAAEAKKKADEAKKAEEAKKADEAKKAEE 1532
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249220 562 KKDAD--LRAMEERYRRYVDKARTVIQTLEPKQRPPTVVSPEfhtlrsqlwERNLRIRQMEMDYEKSRRRQEQEEKL 636
Cdd:PTZ00121 1533 AKKADeaKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEE---------DKNMALRKAEEAKKAEEARIEEVMKL 1600
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
381-589 |
2.04e-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: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 381 ERLLTERDSLREANEELRCAQLQPRGLAQadlsldptpsgLENLAAEIlpAELRETLVRLQLENKRLCQQEAadRERQEE 460
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLEP-----------IRELAERY--AAARERLAELEYLRAALRLWFA--QRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 461 LQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDPtlLKRKLEDHLQKLHEADLELQRKREYIEE 540
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ--LEREIERLERELEERERRRARLEALLAA 370
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1390249220 541 LEPPTDSStARRIEELQDSLQKKDADLRAMEERYRRYVDKARTVIQTLE 589
Cdd:COG4913 371 LGLPLPAS-AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR 418
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
181-602 |
3.29e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.46 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 181 SEEVEEGDHLQQHYLDLERQLLLLSEEKQNLAQENAALRERVGRSEVESAPGLTAKKLLLLQSQLEQLQEENFRLESSRE 260
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK 1627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 261 DdrlrclelEREVAELQQRNQALTSLSQEAQALKDEMDELRQSSERARQLEERNAGHAERTRQLEEELRRAGSLRAQLEA 340
Cdd:PTZ00121 1628 A--------EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE 1699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 341 QRRQVQELQGQWQEEAMKAEkwlfECRNLEEKCDLVTKEKERlltERDSLREANEELRCAQLQPRGLAQADLSLDPTPSG 420
Cdd:PTZ00121 1700 EAKKAEELKKKEAEEKKKAE----ELKKAEEENKIKAEEAKK---EAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEE 1772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 421 LENLAAEILPAELRETLVRLQLENKRLCQQEAADRER-QEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKA 499
Cdd:PTZ00121 1773 IRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANiIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKH 1852
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 500 L-------QEQGGKTEDPTLLKRKLEDHLQKLHEADLELQRKREYIEElEPPTDSSTARRIEELQDSLQKkdadlramEE 572
Cdd:PTZ00121 1853 KfnknnenGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIER-EIPNNNMAGKNNDIIDDKLDK--------DE 1923
|
410 420 430
....*....|....*....|....*....|
gi 1390249220 573 RYRRYVDKARTVIQTLEPKQRPPTVVSPEF 602
Cdd:PTZ00121 1924 YIKRDAEETREEIIKISKKDMCINDFSSKF 1953
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
171-571 |
7.04e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 7.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 171 DTQSRRYYFLSEEVEEGDHLQQHYLDLERQLLLLSEEKQNLAQENAALRERvgRSEVESAPGLTAKKLLLLQSQLEQLQE 250
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA--LAELEEEEEEEEEALEEAAEEEAELEE 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 251 ENFRLESSREDDRLRCLELEREVAELQQRNQALTSLSQEAQALKDEMDELRQSSERARQLEERNAGHAE--RTRQLEEEL 328
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAvaVLIGVEAAY 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 329 RRAGSLRAQLEAQRRQVQELqgqwqEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTERDSLREANEELR------CAQL 402
Cdd:COG1196 537 EAALEAALAAALQNIVVEDD-----EVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVdlvasdLREA 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 403 QPRGLAQADLSLDPTPSGLENLAAEILPAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLN 482
Cdd:COG1196 612 DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE 691
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 483 QQQLSELRAQVEELQKALQEQGGKTEDPTLLKRKLEDHLQKLHEADLELQRKREYIEELEPPTDSSTARRIEELQDSLQK 562
Cdd:COG1196 692 ELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER 771
|
....*....
gi 1390249220 563 KDADLRAME 571
Cdd:COG1196 772 LEREIEALG 780
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
307-545 |
2.73e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 307 ARQLEERNAGHAERTRQLEEELRRagsLRAQLEAQRRQVQELqgqwqeeamKAEKWLFecrNLEEKCDLVTKEKERLlte 386
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPE---LRKELEEAEAALEEF---------RQKNGLV---DLSEEAKLLLQQLSEL--- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 387 RDSLREANEELRCAQLQPRGL-AQADLSLDPTPSGLENLAAEILPAELRETLVRLQLENKRLC-----------QQEAAD 454
Cdd:COG3206 225 ESQLAEARAELAEAEARLAALrAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTpnhpdvialraQIAALR 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 455 RERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDPTLLKRKLEDHLQKLHEADLELQRK 534
Cdd:COG3206 305 AQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALT 384
|
250
....*....|.
gi 1390249220 535 REYIEELEPPT 545
Cdd:COG3206 385 VGNVRVIDPAV 395
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
268-503 |
4.48e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.42 E-value: 4.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 268 ELEREVAELQQRNQaltSLSQEAQALKDEMDELRQSSERARQLEErnAGHAERTRQLEEELRRA----------GSLRAQ 337
Cdd:PRK04863 848 ELERALADHESQEQ---QQRSQLEQAKEGLSALNRLLPRLNLLAD--ETLADRVEEIREQLDEAeeakrfvqqhGNALAQ 922
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 338 LEAQ--------------RRQVQELQGQWQEEAMK--AEKWLFECRN----------LEEKCDLVTKEKERLLTERDSLR 391
Cdd:PRK04863 923 LEPIvsvlqsdpeqfeqlKQDYQQAQQTQRDAKQQafALTEVVQRRAhfsyedaaemLAKNSDLNEKLRQRLEQAEQERT 1002
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 392 EANEELRCAQLQPRGLAQADLSLDPTPSGLENLAAEiLPAELRETLVRLQLEnkrlcqQEAADRERQEELQRHLEEANRA 471
Cdd:PRK04863 1003 RAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQE-LKQELQDLGVPADSG------AEERARARRDELHARLSANRSR 1075
|
250 260 270
....*....|....*....|....*....|..
gi 1390249220 472 RHGLEAQQRLNQQQLSELRAQVEELQKALQEQ 503
Cdd:PRK04863 1076 RNQLEKQLTFCEAEMDNLTKKLRKLERDYHEM 1107
|
|
| HkD_Gipie |
cd22230 |
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar ... |
8-153 |
4.51e-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: 50.21 E-value: 4.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 8 LCGSLLTWLQTFQ------------------VSPPCASPQ--DLSSGLAIAHVLNQIDPSWFNNEWLQGIseDSSPSWRl 67
Cdd:cd22230 4 MSGALVTWALGFEglvgeeedslgfpeeeeeEGTLDAEKRflRLSNGDLLNRVMGIIDPSPRGGPRMRGD--DGPAAHR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 68 kVRKLEKILQSLVEYSKNVLgHPVSDQHLPDVSLIGE--FSNPA--ELGKLLQLVLGCAISCEKKQEYIQRIMTLEESVQ 143
Cdd:cd22230 81 -VQNLHILWGRLRDFYQEEL-QQLILSPPPDLQVMGRdpFTEEAvqELEKLLRLLLGAAVQCERRELFIRHIQGLDLDVQ 158
|
170
....*....|
gi 1390249220 144 HVVMEAIQEL 153
Cdd:cd22230 159 AELAEAIQEV 168
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
256-586 |
4.71e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 4.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 256 ESSREDDRLRCLELEREVAELQQRNQALTSLSQEAQALKDEMDELRQS-----SERARQLEErnAGHAERTRQLeeELRR 330
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAeelkkAEEKKKAEE--AKKAEEDKNM--ALRK 1582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 331 AGSLRAQLEAQRRQVQELQGqwQEEAMKAEKwlfecrnleekcdLVTKEKERLLTERdsLREANEELRCAQLQPRGLAQa 410
Cdd:PTZ00121 1583 AEEAKKAEEARIEEVMKLYE--EEKKMKAEE-------------AKKAEEAKIKAEE--LKKAEEEKKKVEQLKKKEAE- 1644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 411 dlsldptpsglENLAAEILPAELRETLVRLQLENKRlcqqEAADRERQEELQRHLEEANRARHGL--EAQQRLNQQQLSE 488
Cdd:PTZ00121 1645 -----------EKKKAEELKKAEEENKIKAAEEAKK----AEEDKKKAEEAKKAEEDEKKAAEALkkEAEEAKKAEELKK 1709
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 489 LRAQ----VEELQKALQEQGGKTEDptlLKRKLEDHLQKLHEADLELQRKR---EYIEELEPPTDSSTARRIEELQDSLQ 561
Cdd:PTZ00121 1710 KEAEekkkAEELKKAEEENKIKAEE---AKKEAEEDKKKAEEAKKDEEEKKkiaHLKKEEEKKAEEIRKEKEAVIEEELD 1786
|
330 340
....*....|....*....|....*
gi 1390249220 562 KKDADLRAMEERYRRYVDKARTVIQ 586
Cdd:PTZ00121 1787 EEDEKRRMEVDKKIKDIFDNFANII 1811
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
302-550 |
5.95e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 5.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 302 QSSERARQLEERNAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEeamkaekwlfecrnLEEKCDLVTKEKE 381
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRA--------------LEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 382 RLLTERDSLREANEELRcAQLQPRGLAQADLSLDPTPSGLENlaaeilPAELRETLVRLQLenkrLCQQEAADRERQEEL 461
Cdd:COG4942 87 ELEKEIAELRAELEAQK-EELAELLRALYRLGRQPPLALLLS------PEDFLDAVRRLQY----LKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 462 QRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDPTLLKRKLEDHLQKLHEADLELQRKREYIEEL 541
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
....*....
gi 1390249220 542 EPPTDSSTA 550
Cdd:COG4942 236 AAAAAERTP 244
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
415-640 |
6.62e-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: 6.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 415 DPTPSGLENLAAEIlpAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVE 494
Cdd:TIGR02168 666 AKTNSSILERRREI--EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 495 ELQKALQEQGGKTEDptlLKRKLEDHLQKLHEADLELQRKREYIEELEPptdsstarRIEELQDSLQKKDADLRAMEERY 574
Cdd:TIGR02168 744 QLEERIAQLSKELTE---LEAEIEELEERLEEAEEELAEAEAEIEELEA--------QIEQLKEELKALREALDELRAEL 812
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249220 575 RRYVDKARTVIQTLEPKQRPPTVVSPEFHTLRSQLWERNLRIRQMEMDYEKSRRRQEQEEKLLISA 640
Cdd:TIGR02168 813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL 878
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
254-504 |
6.95e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 6.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 254 RLESSREDDRLRCLELEREVAELQQRNQALTSLSQEAQALKDEMDELRQSSERAR-----QLEERNAGHAERTRQLEEEL 328
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELaeaeeALLEAEAELAEAEEELEELA 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 329 RRAGSLRAQLEAQRRQVQELQGQWQEEAmkaekwlfecrnleekcdlvtKEKERLLTERDSLREANEELRcaqlqprgla 408
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALL---------------------ERLERLEEELEELEEALAELE---------- 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 409 qadlsldptpsgLENLAAEILPAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLSE 488
Cdd:COG1196 435 ------------EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
250
....*....|....*.
gi 1390249220 489 LRAQVEELQKALQEQG 504
Cdd:COG1196 503 YEGFLEGVKAALLLAG 518
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
256-635 |
7.70e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 7.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 256 ESSREDDRLRCLELEREVAELQQRnqaLTSLSQEAQALKDEMDELRqssERARQLEERNAGHAERTRQLEEELRRAgslR 335
Cdd:PRK02224 306 DADAEAVEARREELEDRDEELRDR---LEECRVAAQAHNEEAESLR---EDADDLEERAEELREEAAELESELEEA---R 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 336 AQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKER-----------LLTERDSLREAN---EELRCAQ 401
Cdd:PRK02224 377 EAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDElrereaeleatLRTARERVEEAEallEAGKCPE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 402 L-QPRGLAQADLSLDPTPSGLENLAAEILPAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQR 480
Cdd:PRK02224 457 CgQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKR 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 481 LnqqQLSELRAQVEELQKALQEqggKTEDPTLLKRKLEDHLQKLHEADLELQRKREYIEELEpptdsstarRIEELQDSL 560
Cdd:PRK02224 537 E---RAEELRERAAELEAEAEE---KREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE---------RIRTLLAAI 601
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390249220 561 QKKDADLRAMEERyrryvdkaRTVIQTLEpKQRpptvvspefhtlRSQLWERNLRIRQMEMDYEKSRRRQEQEEK 635
Cdd:PRK02224 602 ADAEDEIERLREK--------REALAELN-DER------------RERLAEKRERKRELEAEFDEARIEEAREDK 655
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
265-579 |
1.32e-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: 51.89 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 265 RCLELEREVAELQQRNQA----LTSLSQEAQALKDEMDELRQSSERARQLEERNAGHAERTRQLEEELRRAGSLRAQLEA 340
Cdd:TIGR00618 529 RMQRGEQTYAQLETSEEDvyhqLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAED 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 341 QRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTERDSLREANEELRCAQLQPRGLAQADLSLDPTPSG 420
Cdd:TIGR00618 609 MLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSE 688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 421 LENLAAEILPAELRETLVRLQLE-----NKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEE 495
Cdd:TIGR00618 689 KEQLTYWKEMLAQCQTLLRELEThieeyDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNE 768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 496 LQKALQEQGGKTE----DPTLLKRKLEDHLQKLHEADLELQRKREYIEELEPPTDSSTARRIEELQDSLQKKDADLRAME 571
Cdd:TIGR00618 769 EVTAALQTGAELShlaaEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEIT 848
|
....*...
gi 1390249220 572 ERYRRYVD 579
Cdd:TIGR00618 849 HQLLKYEE 856
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
298-631 |
1.55e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 298 DELRQSSERARqlEERNagHAERTRQLEEELR-RAGSLRA-QLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDl 375
Cdd:TIGR02169 194 DEKRQQLERLR--RERE--KAERYQALLKEKReYEGYELLkEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLE- 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 376 vtkEKERLLTERDSLREANEELRCAQLQPRglaqadlsLDPTPSGLENLAAEIlpAELRETLVRLQLENKRLCQQEAADR 455
Cdd:TIGR02169 269 ---EIEQLLEELNKKIKDLGEEEQLRVKEK--------IGELEAEIASLERSI--AEKERELEDAEERLAKLEAEIDKLL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 456 ERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKT----EDPTLLKRKLEDHLQKLHEADLEL 531
Cdd:TIGR02169 336 AEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELkdyrEKLEKLKREINELKRELDRLQEEL 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 532 QRKREYIEELEPPTDSSTArRIEELQDSLQKKDADLRAMEERYRRYVDKARTVIQTLEPKQRPPTVVSPEFHTLRSQLWE 611
Cdd:TIGR02169 416 QRLSEELADLNAAIAGIEA-KINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
|
330 340
....*....|....*....|
gi 1390249220 612 RNLRIRQMEmDYEKSRRRQE 631
Cdd:TIGR02169 495 AEAQARASE-ERVRGGRAVE 513
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
268-502 |
2.30e-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: 50.53 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 268 ELEREVAELQQR----NQALTSLSQEAQALKDEMDELRQS-SERARQLEERNAGHAERTRQLEEELRRAGSLRAQLEAQR 342
Cdd:COG4942 24 EAEAELEQLQQEiaelEKELAALKKEEKALLKQLAALERRiAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 343 RQVQE-LQGQWQEEAMKAEKWLFecrnleekcdlvtkekerllterdSLREANEELRCAQLQpRGLAQADLSLdptpsgL 421
Cdd:COG4942 104 EELAElLRALYRLGRQPPLALLL------------------------SPEDFLDAVRRLQYL-KYLAPARREQ------A 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 422 ENLAAEIlpAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQ 501
Cdd:COG4942 153 EELRADL--AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
.
gi 1390249220 502 E 502
Cdd:COG4942 231 R 231
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
301-586 |
2.63e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 50.89 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 301 RQSSERARQLEERNAGHAERTRQLEEelrragSLRAQLEAQRRQVQeLQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEK 380
Cdd:pfam17380 295 KMEQERLRQEKEEKAREVERRRKLEE------AEKARQAEMDRQAA-IYAEQERMAMERERELERIRQEERKRELERIRQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 381 ERLLTERDSLREAnEELRCAQLQPRGLAQADLSLDPTPSGLENLAAEILPAELREtlvrlqLENKRLCQQEAadreRQEE 460
Cdd:pfam17380 368 EEIAMEISRMREL-ERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVE------MEQIRAEQEEA----RQRE 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 461 LQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKAL----QEQGGKTEDPTLLKRKLEDHLQKLHEADLELQRKRE 536
Cdd:pfam17380 437 VRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKleleKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRK 516
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1390249220 537 YIEelepptdsstaRRIEELQDSLQKKDADLRAMEERYRRYVDKARTVIQ 586
Cdd:pfam17380 517 LLE-----------KEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQ 555
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
254-495 |
3.11e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 254 RLESSREDDRLRCLELEREVAELQQ----RNQALTSLSQEAQALKDEMDELRQSSERARQLEERNAGHAERTRQLEEELR 329
Cdd:PTZ00121 1547 KADELKKAEELKKAEEKKKAEEAKKaeedKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK 1626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 330 RAgslraqlEAQRRQVQELQGQWQEEAMKAEkwlfECRNLEEKcDLVTKEKERLLTERDslREANEELRCAQLQPRGLAQ 409
Cdd:PTZ00121 1627 KA-------EEEKKKVEQLKKKEAEEKKKAE----ELKKAEEE-NKIKAAEEAKKAEED--KKKAEEAKKAEEDEKKAAE 1692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 410 ADLSLDPTPSGLENL----AAEILPAE-LRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQ 484
Cdd:PTZ00121 1693 ALKKEAEEAKKAEELkkkeAEEKKKAEeLKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEE 1772
|
250
....*....|.
gi 1390249220 485 QLSELRAQVEE 495
Cdd:PTZ00121 1773 IRKEKEAVIEE 1783
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
260-569 |
9.02e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 9.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 260 EDDRLRCLELEREVAELQQRNQALTSLSQEAQALKDEMDELRQSSERARQLEERNAGHAERtrqLEEELRRAGSLRAQLE 339
Cdd:PRK02224 471 EEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRET---IEEKRERAEELRERAA 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 340 AQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTERDSLREaneelrcaqlqprglaqadlsldptps 419
Cdd:PRK02224 548 ELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAA--------------------------- 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 420 gLENLAAEIlpAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANrarhgleaqqrlnqqqLSELRAQVEELQKA 499
Cdd:PRK02224 601 -IADAEDEI--ERLREKREALAELNDERRERLAEKRERKRELEAEFDEAR----------------IEEAREDKERAEEY 661
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390249220 500 LQEQGGKTEDPTLLKRKLEDHLQKLHEADLELQRKREYIEELEPPTDS--STARRIEELQDSLQKKDADLRA 569
Cdd:PRK02224 662 LEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEAleALYDEAEELESMYGDLRAELRQ 733
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
268-589 |
1.26e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 268 ELEREVAELQQRNQALtslsQEAQALKDEMDELRQS------SERARQLEERNAGHAERTRQLEEELRRAGSLRAQLEAQ 341
Cdd:PRK03918 349 ELEKRLEELEERHELY----EEAKAKKEELERLKKRltgltpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 342 RRQVQELQG-----------------------------QWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTER---DS 389
Cdd:PRK03918 425 KKAIEELKKakgkcpvcgrelteehrkelleeytaelkRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKelaEQ 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 390 LREANEELRCAQLQPrgLAQADLSLDPTPSGLENLAAEILpaELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEAN 469
Cdd:PRK03918 505 LKELEEKLKKYNLEE--LEKKAEEYEKLKEKLIKLKGEIK--SLKKELEKLEELKKKLAELEKKLDELEEELAELLKELE 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 470 RARHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDPTLLKRKLEDHLQKLHEADLELQRKREYIEELEPPTDSST 549
Cdd:PRK03918 581 ELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEE 660
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1390249220 550 ARRIEELQDSLQKKDADLRAMEERYRRYVDKARTVIQTLE 589
Cdd:PRK03918 661 YEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLK 700
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
261-636 |
1.30e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 261 DDRLRCLELEREVAELQQRNQALTS-LSQEAQALKDEMDELRQSSERARQLEERNAGHAERTRQLEEELRRAG-SLRAQL 338
Cdd:COG4717 115 REELEKLEKLLQLLPLYQELEALEAeLAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEEL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 339 EAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLlTERDSLREANEELRCAQLQPRGLAQADLSLDPTP 418
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA-ALEERLKEARLLLLIAAALLALLGLGGSLLSLIL 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 419 SGLENLAAEILPAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEaqQRLNQQQLSELRAQVEELQK 498
Cdd:COG4717 274 TIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLP--PDLSPEELLELLDRIEELQE 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 499 ALQEQGGKTEDPTL--LKRKLEDHLQKLHEADLE-----LQRKREYIEELEpptdsstarRIEELQDSLQKKDADLRAME 571
Cdd:COG4717 352 LLREAEELEEELQLeeLEQEIAALLAEAGVEDEEelraaLEQAEEYQELKE---------ELEELEEQLEELLGELEELL 422
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390249220 572 ERYRRyvDKARTVIQTLEPKQRpptVVSPEFHTLRSQLWERNLRIRQMEMDYEKSRRRQEQEEKL 636
Cdd:COG4717 423 EALDE--EELEEELEELEEELE---ELEEELEELREELAELEAELEQLEEDGELAELLQELEELK 482
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
432-634 |
1.38e-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: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 432 ELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDPT 511
Cdd:TIGR02169 713 DASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR 792
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 512 LlkRKLEDHLQKLHEadlELQRKREYIEELEPPTDSSTARRiEELQDSLQKKDADLRAMEERYRRYVDKARTVIQTLEPK 591
Cdd:TIGR02169 793 I--PEIQAELSKLEE---EVSRIEARLREIEQKLNRLTLEK-EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL 866
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1390249220 592 QRPPTVVSPEFHTLRSQLWERNLRIRQMEMDYEKSRRRQEQEE 634
Cdd:TIGR02169 867 EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
256-560 |
1.98e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 256 ESSREDDRLRCLELEREVAELQQRN--QALTSLSQEAQALKDEMDELRQSSERARQ----LEERNAGHAERTRQLEEELR 329
Cdd:PRK02224 179 ERVLSDQRGSLDQLKAQIEEKEEKDlhERLNGLESELAELDEEIERYEEQREQAREtrdeADEVLEEHEERREELETLEA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 330 RAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTERDSLREANEELRcaqlqpRGLAQ 409
Cdd:PRK02224 259 EIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELR------DRLEE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 410 ADLSLDPTPSGLENLaaeilpaelRETLVRLQLENKRLcqqeaadRERQEELQRHLEEANRArhgleaqqrlnqqqLSEL 489
Cdd:PRK02224 333 CRVAAQAHNEEAESL---------REDADDLEERAEEL-------REEAAELESELEEAREA--------------VEDR 382
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390249220 490 RAQVEELQKALQEQGGKTEDPTLLKRKLEDHLQKLHEadlELQRKREYIEELEppTDSSTAR-RIEELQDSL 560
Cdd:PRK02224 383 REEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE---ERDELREREAELE--ATLRTAReRVEEAEALL 449
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
357-570 |
2.37e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 357 MKAEKWLFECRNLEEKCDLVTKEKERLLTERDSLREANEELRCAQLQPRGLAQADLSLDPTPSGLENLAAEILPAELRET 436
Cdd:COG4717 40 LAFIRAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 437 LVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRlnqqQLSELRAQVEELQKALQEQGGKTEDPTL---- 512
Cdd:COG4717 120 KLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEE----ELEELEAELAELQEELEELLEQLSLATEeelq 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 513 -LKRKLEDHLQKLHEADLELQRKREYIEELEPPTDS-STARRIEELQDSLQKKDADLRAM 570
Cdd:COG4717 196 dLAEELEELQQRLAELEEELEEAQEELEELEEELEQlENELEAAALEERLKEARLLLLIA 255
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
260-510 |
2.76e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 260 EDDRLRCLELEREVAELQQRNQALTS--LSQEAQALKDEMDELRQSSERARQLEERnaghaertrqleeelrragsLRAQ 337
Cdd:COG4913 258 RELAERYAAARERLAELEYLRAALRLwfAQRRLELLEAELEELRAELARLEAELER--------------------LEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 338 LEAQRRQVQELQGQWQEEAMKAEKwlfecrNLEEKCDLVTKEKERLLTERDSLREAneelrcaqlqprgLAQADLSLDPT 417
Cdd:COG4913 318 LDALREELDELEAQIRGNGGDRLE------QLEREIERLERELEERERRRARLEAL-------------LAALGLPLPAS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 418 PSGLENLAaeilpAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQrlnqqqlSELRAQVEELQ 497
Cdd:COG4913 379 AEEFAALR-----AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK-------SNIPARLLALR 446
|
250
....*....|...
gi 1390249220 498 KALQEQGGKTEDP 510
Cdd:COG4913 447 DALAEALGLDEAE 459
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
459-572 |
4.15e-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: 47.25 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 459 EELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKaLQEQGGKTEDPTLLKR--KLEDHLQKLHEADLELQRKRE 536
Cdd:COG3096 839 AALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNK-LLPQANLLADETLADRleELREELDAAQEAQAFIQQHGK 917
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1390249220 537 YIEELEPPTDS---------STARRIEELQDSLQKKDADLRAMEE 572
Cdd:COG3096 918 ALAQLEPLVAVlqsdpeqfeQLQADYLQAKEQQRRLKQQIFALSE 962
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
268-398 |
5.01e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 268 ELEREVAELQQRNQALTSLSQEAQALKDEMDELRQSSERARqleernaghaERTRQLEEELRRAGSLRAQLEAQRRQVQE 347
Cdd:COG4913 665 SAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELE----------EELDELKGEIGRLEKELEQAEEELDELQD 734
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1390249220 348 LQGQWQEEAMKAEKWLFECRNLEEKCDLVTKE-KERLLTERDSLREANEELR 398
Cdd:COG4913 735 RLEAAEDLARLELRALLEERFAAALGDAVERElRENLEERIDALRARLNRAE 786
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
268-585 |
9.22e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 9.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 268 ELEREVAELQQRNQALTSLSQEAQALKDEMDELRQSSERARQLEERNAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQE 347
Cdd:PRK03918 201 ELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 348 LQGQWQEEAMKAEKWlfecRNLEEKCDLVTKEKERLLTERDSLREANEELRcAQLQPRGLAQADLS-LDPTPSGLENLAA 426
Cdd:PRK03918 281 KVKELKELKEKAEEY----IKLSEFYEEYLDELREIEKRLSRLEEEINGIE-ERIKELEEKEERLEeLKKKLKELEKRLE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 427 EILPAELRETLVRLQLENKRLCQQEAADRErQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGK 506
Cdd:PRK03918 356 ELEERHELYEEAKAKKEELERLKKRLTGLT-PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKA 434
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249220 507 TEDPTLLKRKLEDHlqklHEADLelqrKREYIEELEpptdsstarRIEELQDSLQKKDADLRAMEERYRRYVDKARTVI 585
Cdd:PRK03918 435 KGKCPVCGRELTEE----HRKEL----LEEYTAELK---------RIEKELKEIEEKERKLRKELRELEKVLKKESELI 496
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
172-610 |
1.07e-04 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 45.73 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 172 TQSRRYYFLSEEVEEGDHLQQHYLDLERQLLLLSEEKQNLAQENAALRERVGRSEVESAPGLTAKKLLLLQSQLEQLQEE 251
Cdd:COG4995 8 ALLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAALAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 252 NFRLESSREDDRLRCLELEREVAELQQRNQALTSLSQEAQALKDEMDELRQSSERARQLEERNAGHAERTRQLEEELRRA 331
Cdd:COG4995 88 ALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAALLA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 332 GSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTERDSLREANEELRCAQLQPRGLAQAD 411
Cdd:COG4995 168 LALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAAAA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 412 LSLDPTPSGLENLAAEILPAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRA 491
Cdd:COG4995 248 AALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLLLL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 492 QVEELQKALQEQGGKTEDPTLLKRKLEDHLQKLHEADLELQRKREYIEELEPPTDSSTARRIEELQDSLQKKDADLRAME 571
Cdd:COG4995 328 AALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAALLALAAAQ 407
|
410 420 430
....*....|....*....|....*....|....*....
gi 1390249220 572 ERYRRYVDKARTVIQTLEPKQRPPTVVSPEFHTLRSQLW 610
Cdd:COG4995 408 LLRLLLAALALLLALAAYAAARLALLALIEYIILPDRLY 446
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
425-589 |
1.67e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 425 AAEILPAELRETLVRLQLENKRLCQQEAADRERQEELQRH---LEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQ 501
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALerrIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 502 EQGGKTED--PTLLKRKLEDHLQKLHEAD--LELQRKREYIEELEpPTDSSTARRIEELQDSLQKKDADLRAMEERYRRY 577
Cdd:COG4942 101 AQKEELAEllRALYRLGRQPPLALLLSPEdfLDAVRRLQYLKYLA-PARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170
....*....|..
gi 1390249220 578 VDKARTVIQTLE 589
Cdd:COG4942 180 LAELEEERAALE 191
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
268-634 |
1.70e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 268 ELEREVAELQQRNQAL----TSLSQEAQALKDEMDELRQSSERARQLEERNAGHAERTRQLEEEL-RRAGSLRAQLEAQR 342
Cdd:PRK02224 255 TLEAEIEDLRETIAETererEELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELeDRDEELRDRLEECR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 343 RQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTERDSLREANEELRCAqlqprgLAQADLSLDPTPSGLE 422
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEE------IEELRERFGDAPVDLG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 423 NLAAEIlpAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLE----------AQQRLNQQQLSELRAQ 492
Cdd:PRK02224 409 NAEDFL--EELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPvegsphvetiEEDRERVEELEAELED 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 493 VEELQKALQEQGGKTEDPTLLKRKLEDHLQKLHEADLELQRKREYIEELEPPTDSSTARRiEELQDSLQKKDADLRAMEE 572
Cdd:PRK02224 487 LEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERA-AELEAEAEEKREAAAEAEE 565
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390249220 573 RyrryVDKARTVIQTLEPKQRPPTVVSPEFHTLRSQLWERNLRIRQMEMDYEKSRRRQEQEE 634
Cdd:PRK02224 566 E----AEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELND 623
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
268-682 |
2.17e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 268 ELEREVAELQQRNQALTSLSQEAQALKDEMDELRQSSERA---------RQLEERNAGHAERTR---QLEEELRRAG--- 332
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrleqleREIERLERELEERERrraRLEALLAALGlpl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 333 -SLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKcdlVTKEKERLLTERDSLREANEELRCAQLQPRGLAQAD 411
Cdd:COG4913 376 pASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRD---LRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 412 LSLDPT-----------------------------------PSGLENLAAEILPAELRETLVRLQL--ENKRLCQQEAAD 454
Cdd:COG4913 453 LGLDEAelpfvgelievrpeeerwrgaiervlggfaltllvPPEHYAAALRWVNRLHLRGRLVYERvrTGLPDPERPRLD 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 455 R-------------------------------ERQEELQRH--------LEEANRARHGLEAQQRL---------NQQQL 486
Cdd:COG4913 533 PdslagkldfkphpfrawleaelgrrfdyvcvDSPEELRRHpraitragQVKGNGTRHEKDDRRRIrsryvlgfdNRAKL 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 487 SELRAQVEELQKALQEQGGKTEDptllKRKLEDHLQKLHEADLELQRKREYIEELEpptdsSTARRIEELQD---SLQKK 563
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEA----LEAELDALQERREALQRLAEYSWDEIDVA-----SAEREIAELEAeleRLDAS 683
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 564 DADLRAMEERyrryVDKARTVIQTLEpkqrpptvvsPEFHTLRSQLWERNLRIRQMEMDYEKSRRRQEQEEKLLISAWYS 643
Cdd:COG4913 684 SDDLAALEEQ----LEELEAELEELE----------EELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA 749
|
490 500 510
....*....|....*....|....*....|....*....
gi 1390249220 644 MGMALEHRAGEEHAPAHAQSFLAQQRLATNARRGPLGRQ 682
Cdd:COG4913 750 LLEERFAAALGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
254-633 |
3.14e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.34 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 254 RLESSREDDRLRCL-ELEREVAELQQRNQALTSLSQEAQALKDEMDELrqsserarqleernaghaertRQLEEELRrag 332
Cdd:pfam15921 430 RLEALLKAMKSECQgQMERQMAAIQGKNESLEKVSSLTAQLESTKEML---------------------RKVVEELT--- 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 333 SLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTERDSLREANEELRCAQLQprgLAQADL 412
Cdd:pfam15921 486 AKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQ---MAEKDK 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 413 SLDPTPSGLENL------------AAEILPAELRETL--VRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQ 478
Cdd:pfam15921 563 VIEILRQQIENMtqlvgqhgrtagAMQVEKAQLEKEIndRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGS 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 479 QRLNQ-QQLSELRAQ-VEELQKALQEQGGKTEDPTLLKRKLEDHLQ-----------KLHEADLELQRKREYIEELEPPT 545
Cdd:pfam15921 643 ERLRAvKDIKQERDQlLNEVKTSRNELNSLSEDYEVLKRNFRNKSEemetttnklkmQLKSAQSELEQTRNTLKSMEGSD 722
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 546 DSS-----------TARR--IEELQDSLQ-KKDADLRAMEERYRRYVDKARtVIQTLEPKQRPPTVVSPEFHTLRSQLWE 611
Cdd:pfam15921 723 GHAmkvamgmqkqiTAKRgqIDALQSKIQfLEEAMTNANKEKHFLKEEKNK-LSQELSTVATEKNKMAGELEVLRSQERR 801
|
410 420 430
....*....|....*....|....*....|..
gi 1390249220 612 RNLRIRQMEMDYEKSR----------RRQEQE 633
Cdd:pfam15921 802 LKEKVANMEVALDKASlqfaecqdiiQRQEQE 833
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
205-584 |
3.35e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 205 SEEKQNLAQENAALRERVGR-----SEVESAPGLTAKKLLLLQSQLEQLQEenfrlessreddrlrclELEREVAELQQR 279
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRienrlDELSQELSDASRKIGEIEKEIEQLEQ-----------------EEEKLKERLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 280 NQALTSLSQEAQALKDEMDELRqssERARQLEERNAGHAERTRQLEEELRRAG--SLRAQLEAQRRQVQELQGQWQEEAM 357
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELKELE---ARIEELEEDLHKLEEALNDLEARLSHSRipEIQAELSKLEEEVSRIEARLREIEQ 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 358 KAEKWLFECRNLEekcdlvtKEKERLLTERDSLrEANEELRCAQlqprglaqadlsldptpsgLENLAAEIlpAELRETL 437
Cdd:TIGR02169 820 KLNRLTLEKEYLE-------KEIQELQEQRIDL-KEQIKSIEKE-------------------IENLNGKK--EELEEEL 870
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 438 VRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQGgktedpTLLKRKL 517
Cdd:TIGR02169 871 EELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE------DPKGEDE 944
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390249220 518 EDHLQKLHEADLELQRKR--EYIEELEPPTD------SSTARRIEELQDSLQKKDADLRAMEERYRRYVDKARTV 584
Cdd:TIGR02169 945 EIPEEELSLEDVQAELQRveEEIRALEPVNMlaiqeyEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
207-512 |
3.90e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.57 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 207 EKQNLAQENAAL-RERVGRSEVESAPglTAKKLLLLQSQLEQLQEENFRLESSREDDRLRCLELEREVAELQQRNQALTs 285
Cdd:pfam17380 297 EQERLRQEKEEKaREVERRRKLEEAE--KARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAME- 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 286 lSQEAQALKDEMDELRQSSERARQLEE----RNAGHAERTRQLEEELRRAGSLRA-QLEAQRRQVQELQgqwQEEAMKAE 360
Cdd:pfam17380 374 -ISRMRELERLQMERQQKNERVRQELEaarkVKILEEERQRKIQQQKVEMEQIRAeQEEARQREVRRLE---EERAREME 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 361 KWLFECRNLEEKCDLVTKEKERLLTERDSLREANEELRCAQLQPRGLAQADLSLDPTPSGLENLAAEILPAELRETLVRL 440
Cdd:pfam17380 450 RVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAI 529
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249220 441 QLENKRLCQQEAADRERQEELQRHLEE----ANRARHGLEAQQRLNqqqlsELRAQVEELQKALQEQGGKTEDPTL 512
Cdd:pfam17380 530 YEEERRREAEEERRKQQEMEERRRIQEqmrkATEERSRLEAMERER-----EMMRQIVESEKARAEYEATTPITTI 600
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
268-637 |
4.67e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 268 ELEREVAELQQRNQALTSLSQEAQA-------LKDEMDELRQSSERARQLEERNAGHAERTRQLEEELRRAGSLRAQLEA 340
Cdd:PRK03918 270 ELKKEIEELEEKVKELKELKEKAEEyiklsefYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 341 QRRQVQELQGQWQE-----------EAMKAEKWLFECRNLEEKCDLVTKEKE--------------RLLTERDSLREANE 395
Cdd:PRK03918 350 LEKRLEELEERHELyeeakakkeelERLKKRLTGLTPEKLEKELEELEKAKEeieeeiskitarigELKKEIKELKKAIE 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 396 ELRCAQLQPRgLAQADLSLDPTPSGLENLAAEI--LPAELRETLVRLQLENKRLCQQEAAdRERQEELQRHLEEANRARh 473
Cdd:PRK03918 430 ELKKAKGKCP-VCGRELTEEHRKELLEEYTAELkrIEKELKEIEEKERKLRKELRELEKV-LKKESELIKLKELAEQLK- 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 474 glEAQQRLNQQQLSELRAQVEELQKALQEQGG----------KTEDPTLLKRKLEDHLQKLHEADLELQRKREYIEELEP 543
Cdd:PRK03918 507 --ELEEKLKKYNLEELEKKAEEYEKLKEKLIKlkgeikslkkELEKLEELKKKLAELEKKLDELEEELAELLKELEELGF 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 544 PTDSSTARRIEELQdSLQKKDADLRAMEERYRRYVDKARTVIQTLEPKQRPPTVVSPEFHTLRSQLWErnLRIRQMEMDY 623
Cdd:PRK03918 585 ESVEELEERLKELE-PFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE--LEKKYSEEEY 661
|
410
....*....|....
gi 1390249220 624 EKSRRRQEQEEKLL 637
Cdd:PRK03918 662 EELREEYLELSREL 675
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
265-573 |
5.05e-04 |
|
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: 43.40 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 265 RCLELEREVAELQQRNQALTS----------LSQEAQALKDEMD----ELRQSSERARQLEERNAGHAERTRQLEEELRR 330
Cdd:COG3096 307 RLVEMARELEELSARESDLEQdyqaasdhlnLVQTALRQQEKIEryqeDLEELTERLEEQEEVVEEAAEQLAEAEARLEA 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 331 A----GSLRAQLEAQRRQVQELQ---GQWQEeAMKAekwLFECRNLEEKCDL-VTKEKERLLTERDSLREANEELRCAQl 402
Cdd:COG3096 387 AeeevDSLKSQLADYQQALDVQQtraIQYQQ-AVQA---LEKARALCGLPDLtPENAEDYLAAFRAKEQQATEEVLELE- 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 403 QPRGLAQADLS------------LDPTPSG---------------LENLA--AEILPAELRETLVRLQLEN------KRL 447
Cdd:COG3096 462 QKLSVADAARRqfekayelvckiAGEVERSqawqtarellrryrsQQALAqrLQQLRAQLAELEQRLRQQQnaerllEEF 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 448 CQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQ--------------------KALQEQGGKT 507
Cdd:COG3096 542 CQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRarikelaarapawlaaqdalERLREQSGEA 621
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390249220 508 -EDPTLLKRKLEDHLQKLHEADLELQRKREYIEELEpptdsstaRRIEELQDSLQKKDADLRAMEER 573
Cdd:COG3096 622 lADSQEVTAAMQQLLEREREATVERDELAARKQALE--------SQIERLSQPGGAEDPRLLALAER 680
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
261-526 |
5.45e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 43.25 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 261 DDRLRCLELEREVA------------------ELQQRNQALTSLSQEAQALKDEMDELRQSSERARQLEERNAG---HAE 319
Cdd:PRK10246 527 VNQSRLDALEKEVKklgeegaalrgqldaltkQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQPwldAQE 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 320 RTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFEC-----RNLEEKCDLVTKEKERLLTERDSLREAN 394
Cdd:PRK10246 607 EHERQLRLLSQRHELQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYaltlpQEDEEASWLATRQQEAQSWQQRQNELTA 686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 395 EELRCAQLQPRglaqadLSLDPTPSGLENLAAEILPAELRET---LVRLQLENKRLCQQEAADRERQEELQRHLEEA--- 468
Cdd:PRK10246 687 LQNRIQQLTPL------LETLPQSDDLPHSEETVALDNWRQVheqCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTAlqa 760
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249220 469 ---------------NRARHGLEAQ-QRLNQ--QQLSELRAQVEELQKALQEQGGKTEDPTLLKRKLEDHLQKLHE 526
Cdd:PRK10246 761 svfddqqaflaalldEETLTQLEQLkQNLENqrQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQLAQ 836
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
267-573 |
6.29e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 267 LELEREVA----ELQQRNQALTSLSQEAQALKDEMDELRQSSERAR---QLEERNAGHAERTRQLEEELrraGSLRAQLE 339
Cdd:PRK04863 289 LELRRELYtsrrQLAAEQYRLVEMARELAELNEAESDLEQDYQAASdhlNLVQTALRQQEKIERYQADL---EELEERLE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 340 AQRRQVQELQGQWQEeamkaekwlfecrnLEEKCDLVTKEKERLLTERDSLREANEELRCAQLQPRGL------AQADLS 413
Cdd:PRK04863 366 EQNEVVEEADEQQEE--------------NEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAvqalerAKQLCG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 414 LDP-TPSGLENLAAEILPAELRETLVRLQLENKRLCQQEAADR-ERQEELQRHL------EEANRARHGLEAQ---QRLN 482
Cdd:PRK04863 432 LPDlTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQfEQAYQLVRKIagevsrSEAWDVARELLRRlreQRHL 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 483 QQQLSELRAQVEELQKALQEQGGKTEDPTLLKRKLEDHLQKLHEADLELQRKREYIEELEPPTDSSTARRiEELQDSLQK 562
Cdd:PRK04863 512 AEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERR-MALRQQLEQ 590
|
330
....*....|.
gi 1390249220 563 KDADLRAMEER 573
Cdd:PRK04863 591 LQARIQRLAAR 601
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
253-576 |
7.14e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 253 FRLESSREDDRLRCLELEREVAELqqrNQALTSLSQEAQALKDE----MDELRQSS--ERAR--------QLEERNAGHA 318
Cdd:PRK04863 296 YTSRRQLAAEQYRLVEMARELAEL---NEAESDLEQDYQAASDHlnlvQTALRQQEkiERYQadleeleeRLEEQNEVVE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 319 ERTRQLEEELRRAG-------SLRAQL--------EAQRRQVQELQGQWQEEamKAEKWL----FECRNLEEKCD-LVTK 378
Cdd:PRK04863 373 EADEQQEENEARAEaaeeevdELKSQLadyqqaldVQQTRAIQYQQAVQALE--RAKQLCglpdLTADNAEDWLEeFQAK 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 379 EKErlLTERdsLREANEELRCAQLQPRGLAQAdLSLdptpsgLENLAAEILPAE----LRETLVRLQlENKRLCQQEAAD 454
Cdd:PRK04863 451 EQE--ATEE--LLSLEQKLSVAQAAHSQFEQA-YQL------VRKIAGEVSRSEawdvARELLRRLR-EQRHLAEQLQQL 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 455 RERQEELQRHLEEANRARHGL-EAQQRLN---------QQQLSELRAQVEELQKALQEQGgktEDPTLLKRKLED----- 519
Cdd:PRK04863 519 RMRLSELEQRLRQQQRAERLLaEFCKRLGknlddedelEQLQEELEARLESLSESVSEAR---ERRMALRQQLEQlqari 595
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1390249220 520 -HLQKLHEADLELQRKREYIEELEPPTDsSTARRIEELQDSLQKKDADLRAMEERYRR 576
Cdd:PRK04863 596 qRLAARAPAWLAAQDALARLREQSGEEF-EDSQDVTEYMQQLLERERELTVERDELAA 652
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
254-585 |
1.30e-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: 42.02 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 254 RLESSREDDRLRCLELEREVAELQQRNQALTSLSQEAQALKDEMDE----LRQSSERARQLEERNAGHAERTRQLEEELR 329
Cdd:pfam05483 371 RLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEdeklLDEKKQFEKIAEELKGKEQELIFLLQAREK 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 330 RAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTERD----SLREANEEL-RCAQLQP 404
Cdd:pfam05483 451 EIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASdmtlELKKHQEDIiNCKKQEE 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 405 RGLAQadlsldptpsgLENLaaEILPAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARhglEAQQRLNQQ 484
Cdd:pfam05483 531 RMLKQ-----------IENL--EEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKK---EKQMKILEN 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 485 QLSELRAQVEELQKALQEQggkTEDPTLLKRKLEDHLQKLHEADLELQRKreyieELEPptdSSTARRIEELQDSLQKKD 564
Cdd:pfam05483 595 KCNNLKKQIENKNKNIEEL---HQENKALKKKGSAENKQLNAYEIKVNKL-----ELEL---ASAKQKFEEIIDNYQKEI 663
|
330 340
....*....|....*....|.
gi 1390249220 565 ADLRAMEERYRRYVDKARTVI 585
Cdd:pfam05483 664 EDKKISEEKLLEEVEKAKAIA 684
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
260-635 |
1.54e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.86 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 260 EDDRLRCLELEREVAELQQRNQaltsLSQEAQALKDEMDELRQSSERARQLEE------------RNA-GHAERTRQLEE 326
Cdd:COG3096 279 ERRELSERALELRRELFGARRQ----LAEEQYRLVEMARELEELSARESDLEQdyqaasdhlnlvQTAlRQQEKIERYQE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 327 ELrraGSLRAQLEAQRRQVQELQGQWQEeamkaekwlfecrnLEEKCDLVTKEKERLLTERDSLREANEEL--RCAQ--- 401
Cdd:COG3096 355 DL---EELTERLEEQEEVVEEAAEQLAE--------------AEARLEAAEEEVDSLKSQLADYQQALDVQqtRAIQyqq 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 402 -LQPRGLAQADLSLDP-TPSGLENLAAEILPAELRETLVRLQLENKRLCQQEAADRERQ--EELQRHLEEANRARHGLEA 477
Cdd:COG3096 418 aVQALEKARALCGLPDlTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKayELVCKIAGEVERSQAWQTA 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 478 QQRLNQ--------QQLSELRAQVEELQKALQEQGGKTEDPTLLKRKLEDHLQKLHEADLELQRKREYIEELEPPTDSST 549
Cdd:COG3096 498 RELLRRyrsqqalaQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAV 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 550 ARRIEELQ--DSLQKKDADLRAMEERYRryvdKARTVIQTLEPKQRPPTVVSPEFHTLRSQLWERNlriRQMEMDYEKSR 627
Cdd:COG3096 578 EQRSELRQqlEQLRARIKELAARAPAWL----AAQDALERLREQSGEALADSQEVTAAMQQLLERE---REATVERDELA 650
|
....*...
gi 1390249220 628 RRQEQEEK 635
Cdd:COG3096 651 ARKQALES 658
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
256-372 |
1.68e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 41.62 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 256 ESSREDDRLRCLELEREVAELQQRNQALTSLSQEAQALKDEMDelrqssERARQLEERNAGHAERTRQLEEELRRAGSLR 335
Cdd:PRK12705 66 NQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLE------EREKALSARELELEELEKQLDNELYRVAGLT 139
|
90 100 110
....*....|....*....|....*....|....*..
gi 1390249220 336 AQlEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEK 372
Cdd:PRK12705 140 PE-QARKLLLKLLDAELEEEKAQRVKKIEEEADLEAE 175
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
206-636 |
1.80e-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: 41.88 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 206 EEKQNLAQENAALRErVGRSEVESAPGLTAKkllllqsqleqlqeenfrlessreddrlrcLELEREVAELQQRNQALTS 285
Cdd:TIGR00618 219 ERKQVLEKELKHLRE-ALQQTQQSHAYLTQK------------------------------REAQEEQLKKQQLLKQLRA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 286 LSQEAQALKDEMDELRQSSERARQLeERNAGHAERTRQLEE-------ELRRAGSLRAQLEAQRRQVQELQGQWQEEAMK 358
Cdd:TIGR00618 268 RIEELRAQEAVLEETQERINRARKA-APLAAHIKAVTQIEQqaqrihtELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 359 AEKWLFECRNLE---EKCDLVTKEKERLLTERDSLREANEELRCAQLQPRGLAQADLSLDptpsgleNLAAEILPAELRE 435
Cdd:TIGR00618 347 LQTLHSQEIHIRdahEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQ-------REQATIDTRTSAF 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 436 TLVRLQLenKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDPTLLKR 515
Cdd:TIGR00618 420 RDLQGQL--AHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 516 KLEDHLQKLHEADLELQRKREYIEELEPPTDSSTA--RRIEELQDSLQKKDADLRAMEERYRRYVDKARTVIQTLEPKQR 593
Cdd:TIGR00618 498 ELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRgeQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQ 577
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1390249220 594 PPTVVSPEFHTLRsQLWERNLRIRQMEMDYEKSRRRQEQEEKL 636
Cdd:TIGR00618 578 CDNRSKEDIPNLQ-NITVRLQDLTEKLSEAEDMLACEQHALLR 619
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
268-522 |
5.70e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.89 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 268 ELEREVAELQQR-NQALTSLSQeAQALKDEMDELRQSSERA-RQLEERNAGHAERTRQLEEELR---RAGSLRaQLEAQR 342
Cdd:PRK11281 53 LLEAEDKLVQQDlEQTLALLDK-IDRQKEETEQLKQQLAQApAKLRQAQAELEALKDDNDEETRetlSTLSLR-QLESRL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 343 RQVQELQGQWQEEAMKAEKwlfecrnleekcDLVTKEK--ERLLTERDSLREANEELRcAQLQPRGLAQADLSldptPSG 420
Cdd:PRK11281 131 AQTLDQLQNAQNDLAEYNS------------QLVSLQTqpERAQAALYANSQRLQQIR-NLLKGGKVGGKALR----PSQ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 421 LENLAAEILPAELRETLVRLQLENKRLCQqeAADRERQEELQrhlEEANRARHGLEA-QQRLNQQQLSELRAQVEELQKa 499
Cdd:PRK11281 194 RVLLQAEQALLNAQNDLQRKSLEGNTQLQ--DLLQKQRDYLT---ARIQRLEHQLQLlQEAINSKRLTLSEKTVQEAQS- 267
|
250 260
....*....|....*....|...
gi 1390249220 500 lQEQGGKTEDPTLLKRKLEDHLQ 522
Cdd:PRK11281 268 -QDEAARIQANPLVAQELEINLQ 289
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
260-362 |
6.29e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 39.78 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 260 EDDRLRCLELEREVAElQQRNQALTSLSQEAQALKDEMDELRQSSERARQLEERNAGHAERTRQLEEELRRAGSLRAQL- 338
Cdd:PRK10246 775 DEETLTQLEQLKQNLE-NQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQLAQQLRENTTRQGEIRQQLk 853
|
90 100
....*....|....*....|....*.
gi 1390249220 339 --EAQRRQVQELQGQWQEEAMKAEKW 362
Cdd:PRK10246 854 qdADNRQQQQALMQQIAQATQQVEDW 879
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
288-359 |
6.54e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 39.40 E-value: 6.54e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390249220 288 QEAQALKDEMDELRQSSERARQLEERNAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKA 359
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKA 141
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
269-417 |
6.85e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 6.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 269 LEREVAELQQRNQaltsLSQEAQALKDEMDE-LRQSSERARQLEERNAGHAERTRQLEEELRRAGSLRAQLeaqRRQVQE 347
Cdd:PRK04863 518 LRMRLSELEQRLR----QQQRAERLLAEFCKrLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMAL---RQQLEQ 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 348 LQGQWQEEAMKAEKWL----------------FECRNLEEKCDLVTKEKERLLT-ERDSLREANEELrcaQLQPRGLAQA 410
Cdd:PRK04863 591 LQARIQRLAARAPAWLaaqdalarlreqsgeeFEDSQDVTEYMQQLLERERELTvERDELAARKQAL---DEEIERLSQP 667
|
....*..
gi 1390249220 411 DLSLDPT 417
Cdd:PRK04863 668 GGSEDPR 674
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
315-542 |
7.53e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 39.29 E-value: 7.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 315 AGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQgqwQEEAMkaekWLFECRNLEEkCDLVTKEKERLLTERDSLREAn 394
Cdd:COG0497 151 AGLEELLEEYREAYRAWRALKKELEELRADEAERA---RELDL----LRFQLEELEA-AALQPGEEEELEEERRRLSNA- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 395 EELRcaqlqpRGLAQADLSLDPTPSGLENLAAEI---------LPAELRETLVRL-----QLEnkrlcqqEAADrerqeE 460
Cdd:COG0497 222 EKLR------EALQEALEALSGGEGGALDLLGQAlralerlaeYDPSLAELAERLesaliELE-------EAAS-----E 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 461 LQRHLE--EANRARhgLEA-QQRLNQ---------QQLSELRAQVEELQKALQEQGGKTEDPTLLKRKLEDHLQKLHEAD 528
Cdd:COG0497 284 LRRYLDslEFDPER--LEEvEERLALlrrlarkygVTVEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAA 361
|
250
....*....|....*
gi 1390249220 529 LELQRKR-EYIEELE 542
Cdd:COG0497 362 EKLSAARkKAAKKLE 376
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
273-487 |
9.49e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 9.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 273 VAELQQRNQALTSLS-QEAQALKDEMDELRQSSERARQLEERNAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQ 351
Cdd:COG4717 48 LERLEKEADELFKPQgRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249220 352 WQEEAmkaekwlfECRNLEEKCDLVTKEKERLLTERDSLREANEELRCAQLQprgLAQADLSLDPTPSGLENLAAEILpA 431
Cdd:COG4717 128 LPLYQ--------ELEALEAELAELPERLEELEERLEELRELEEELEELEAE---LAELQEELEELLEQLSLATEEEL-Q 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1390249220 432 ELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLS 487
Cdd:COG4717 196 DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL 251
|
|
| |
