|
Name |
Accession |
Description |
Interval |
E-value |
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
184-709 |
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: 685.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 184 ELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQEETFRLEA 263
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 264 AKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSLKDEMDVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQVKLLEEK 343
Cdd:pfam05622 81 ARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLGDLRRQVKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 344 NTMYMQNTVSLEEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKET 423
Cdd:pfam05622 161 NAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRET 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 424 IEELRCVQAQEGQLTTSGLMPLGSQESSDSLAAEIVTPEIKEKLIRLQHENKMLKLNQEGSDNEKIALLQSLLDDANLRK 503
Cdd:pfam05622 241 NEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLGQEGSYRERLTELQQLLEDANRRK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 504 NELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDSVLLKKKLEEHLEKLHEANNEIQRKRAIIEDLEPRYN-NSSLK 582
Cdd:pfam05622 321 NELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDsNLAQK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 583 IEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGTAPEIQALKNQLQERDRMFHSLEKEYEKTKTQREMEE 662
Cdd:pfam05622 401 IDELQEALRKKDEDMKAMEERYKKYVEKAKSVIKTLDPKQNPASPPEIQALKNQLLEKDKKIEHLERDFEKSKLQREQEE 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1729156920 663 KFIVSAWYNMGMTLHKKAAEDRLASTGS-GQSFLARQRQATNTRRSYP 709
Cdd:pfam05622 481 KLIVTAWYNMGMALHRKAIEERLAGLSSpGQSFLARQRQATNARRGLS 528
|
|
| HkD_Hook3 |
cd22226 |
Hook domain found in protein Hook 3 (Hook3) and similar proteins; Hook3 is an adaptor protein ... |
8-160 |
4.72e-102 |
|
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: 309.98 E-value: 4.72e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 8 ERAELGESLLTWIQTFNVEAPCQTVEDLTNGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYN 87
Cdd:cd22226 1 DRAELCESLLTWIQTFNVDAPCQTVEDLTSGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1729156920 88 HEILGQQINDFTLPDVNLIGEHSDVAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMSK 160
Cdd:cd22226 81 HEILGQQINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMSK 153
|
|
| HOOK_N |
pfam19047 |
HOOK domain; This domain is found at the N-terminus of HOOK proteins. |
11-161 |
2.16e-94 |
|
HOOK domain; This domain is found at the N-terminus of HOOK proteins.
Pssm-ID: 465958 Cd Length: 151 Bit Score: 290.08 E-value: 2.16e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 11 ELGESLLTWIQTFNVEAPCQTVEDLTNGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEI 90
Cdd:pfam19047 1 ELCDSLLTWLQTFNVPAPCATVEDLTDGVAMAQVLHQIDPSWFTEAWLSRIKEDVGDNWRLKVSNLKKILQSVVDYYQDV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1729156920 91 LGQQINDFTLPDVNLIGEHSDVAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMSKE 161
Cdd:pfam19047 81 LGQQISDFLLPDVNLIGEHSDPAELGRLLQLILGCAVNCEKKQEYIQQIMTLEESVQHVVMTAIQELMSKD 151
|
|
| HkD_Hook |
cd22222 |
Hook domain found in Hook family of microtubule-binding proteins; The Hook family includes ... |
14-159 |
5.70e-90 |
|
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: 278.36 E-value: 5.70e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 14 ESLLTWIQTFNVEAPCQTVEDLTNGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEILGQ 93
Cdd:cd22222 2 DSLLQWLQTFNLIAPHATAEDLSDGVAIAQVLNQIDPEYFSDSWLSKIKPDVGDNWRLKVSNLKKILKGIVDYYSEVLGQ 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1729156920 94 QINDFTLPDVNLIGEHSDVAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMS 159
Cdd:cd22222 82 QISGFTMPDVNAIAEKEDPKELGRLLQLVLGCAVNCERKEEYIQAIMGLEESVQHVVMEAIQELMS 147
|
|
| HkD_Hook1 |
cd22225 |
Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a ... |
12-161 |
1.47e-80 |
|
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: 254.00 E-value: 1.47e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 12 LGESLLTWIQTFNVEAPCQTVEDLTNGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEIL 91
Cdd:cd22225 1 LCDSLIIWLQTFNTAAPCQTVQDLTSGVAMAQVLHQIDSSWFDESWLSRIKEDVGDNWRIKMSNLKKILQGIVDYYHEFL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 92 GQQINDFTLPDVNLIGEHSDVAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMSKE 161
Cdd:cd22225 81 DQQISEFLLPDLNRIAEHSDPVELGRLLQLILGCAVNCEKKQEHIQNIMTLEESVQHVVMTAIQELMSKE 150
|
|
| HkD_Hook2 |
cd22227 |
Hook domain found in protein Hook 2 (Hook2) and similar proteins; Hook2 is a ... |
11-160 |
1.39e-70 |
|
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: 227.45 E-value: 1.39e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 11 ELGESLLTWIQTFNVEAPCQTVEDLTNGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEI 90
Cdd:cd22227 1 ELCDSLLTWLQTFQVPSPCSSYQDLTSGVAIAQVLNRIDPSWFNEAWLGRIKEDTGDNWRLKVSNLKKILQSLLEYYQDV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 91 LGQQINDFTLPDVNLIGEHSDVAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMSK 160
Cdd:cd22227 81 LGHQVSEDHLPDVNLIGEFSDDTELGKLLQLVLGCAISCEKKQEHIQQIMTLEESVQHVVMEAIQELLTK 150
|
|
| HkD_SF |
cd22211 |
Hook domain-containing proteins superfamily; The Hook domain superfamily includes Hook adaptor ... |
13-159 |
4.87e-54 |
|
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: 182.86 E-value: 4.87e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 13 GESLLTWIQTFNVEAPCQTVEDLTNGVVMAQVLQKIDPAYFDENWLNriKTEVGDNWRLKISNLKKILKGILDYNHEILG 92
Cdd:cd22211 1 EAALLAWINTFPLSSPVESLDDLSDGVVLAEILSQIDPSYFDSEWLE--SRDSSDNWVLKLNNLKKLYRSLSKYYREVLG 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1729156920 93 QQINDFTLPDVNLIGEHSDVAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMS 159
Cdd:cd22211 79 QQLSDLPLPDLSAIARDGDEEEIVKLLELVLGAAVQCENKEEYIARIQQLDESTQAELMLIIQEVLE 145
|
|
| HkD_HkRP |
cd22223 |
Hook domain found in the Hook-related protein (HkRP) family; The HkRP family includes Daple, ... |
15-157 |
2.83e-25 |
|
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: 102.28 E-value: 2.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 15 SLLTWIQTFNVEAPCQ-TVEDLTNGVVMAQVLQKIDPAYFDEnwlnRIKTEVGDNWRLKISNLKKILKGILDYNHEILGQ 93
Cdd:cd22223 5 PLVTWAKTFADDGSAElSYTDLVDGVFLNNVMLQIDPRPFSE----VSNRNVDDDVNARIQNLDLLLRNIKSFYQEVLQQ 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1729156920 94 QINdFTLPDVNLIGEHSD----VAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQEL 157
Cdd:cd22223 81 LIV-MKLPDILTIGREPEseqsLEELEKLLLLLLGCAVQCERKEEFIERIKNLDLEVQHALVACIQEV 147
|
|
| HkD_Daple |
cd22228 |
Hook domain found in Daple (Dvl-associating protein with a high frequency of leucine residues) ... |
12-157 |
2.22e-17 |
|
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: 79.58 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 12 LGESLLTWIQTFNV-----EAPCQTVEDLTNGVVMAQVLQKIDPAYFDEnwlnRIKTEVGDNWRLKISNLKKILKGILDY 86
Cdd:cd22228 2 LQSPLVTWVKTFGPlgfgsEDKLSMYMDLVDGVFLNKIMLQIDPRPTNQ----RVNKHVNNDVNLRIQNLTILVRHIKTY 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1729156920 87 NHEILgQQINDFTLPDVNLIGEH----SDVAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQEL 157
Cdd:cd22228 78 YQEVL-QQLIVMNLPNVLMIGKDplsgKSMEEIKKMLLLVLGCAVQCERKEEFIERIKQLDIETQAAIVSHIQEV 151
|
|
| HkD_Girdin |
cd22229 |
Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation ... |
16-157 |
6.09e-13 |
|
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: 67.12 E-value: 6.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 16 LLTWIQTFNVEAPCQTVE-----DLTNGVVMAQVLQKIDPAYFDEnwlnRIKTEVGDNWRLKISNLKKILKGILDYNHEI 90
Cdd:cd22229 9 LVTWVKTFGPLATGNGTPldeyvALVDGVFLNEVMLQINPKSSNQ----RVNKKVNNDASLRIQNLSILVKQIKLYYQET 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1729156920 91 LgQQINDFTLPDVNLIGEH----SDVAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQEL 157
Cdd:cd22229 85 L-QQLIMMSLPNVLVLGRNplseQGTEEMKKLLLLLLGCAVQCERKEEFIERIQTLDFDTKAAVAAHIQEV 154
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
260-591 |
1.46e-12 |
|
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: 71.63 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 260 RLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSLKDEMDVLRHSSDK-VAKLESQVESYKKKLEDLGdlrrqvK 338
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdLARLEAEVEQLEERIAQLS------K 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 339 LLEEKNTMYMQNTVSLEEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLK-------EKVDGLQKEKD 411
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNeeaanlrERLESLERRIA 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 412 RLRTERDSLKETIEELRCVQAQ-EGQLTTSGLMPLGSQESSDSLAAEIVTPEIKEKLIRLQHENKMLKLNQEGSDN---- 486
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESlAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRselr 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 487 EKIALLQSLLDDANLRKNELEtenrlvnQRLLEVQSQV-EELQKSLQEQGSKAEDSVLLKKKLEEHLEKLHEANNEIQR- 564
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLE-------VRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPv 987
|
330 340 350
....*....|....*....|....*....|
gi 1729156920 565 -KRAI--IEDLEPRYNNSSLKIEELQEALR 591
Cdd:TIGR02168 988 nLAAIeeYEELKERYDFLTAQKEDLTEAKE 1017
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
130-664 |
2.86e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.01 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 130 EQKQEYIQTIMMMEESVQHVVMTAIQELMSKESPVSVGNDAYVDLDRQLKKTTEELNEALATKEEIAqrchELDMQVAAL 209
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIE----ELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 210 QEEKSSLLAENQILMERLNQSDS-IEDPNSPAGR---------RHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEI 279
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKeIEELEEKVKElkelkekaeEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 280 AELRQQNEELTTLAEEAQSLKDEMDVLRHSS---DKVAKLESQVESYKKKLEDL--GDLRRQVKLLEEKNTmymqntvSL 354
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEELEERHelyEEAKAKKEELERLKKRLTGLtpEKLEKELEELEKAKE-------EI 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 355 EEELRKAHAARSQLET----YKRQVVELQ-------------------NRLSEESKKADKLEFEYKLLKEKVDGLQKEKD 411
Cdd:PRK03918 404 EEEISKITARIGELKKeikeLKKAIEELKkakgkcpvcgrelteehrkELLEEYTAELKRIEKELKEIEEKERKLRKELR 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 412 RLRTERD------SLKETIEELRCVQAQegqlttsglmpLGSQESSDSLAAEIVTPEIKEKLIRLQHENKMLK--LNQEG 483
Cdd:PRK03918 484 ELEKVLKkeseliKLKELAEQLKELEEK-----------LKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKkeLEKLE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 484 SDNEKIALLQSLLDDANLRKNELETE-NRLVNQRLLEVQSQVEELQK----------SLQEQGSKAEDSVLLKKKLEEHL 552
Cdd:PRK03918 553 ELKKKLAELEKKLDELEEELAELLKElEELGFESVEELEERLKELEPfyneylelkdAEKELEREEKELKKLEEELDKAF 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 553 EKLHEANNEIQRKRAIIEDLEPRYNnsslkiEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLdpkqnqgtAPEIQA 632
Cdd:PRK03918 633 EELAETEKRLEELRKELEELEKKYS------EEEYEELREEYLELSRELAGLRAELEELEKRREEI--------KKTLEK 698
|
570 580 590
....*....|....*....|....*....|..
gi 1729156920 633 LKNQLQERDRMFHSLEKEYEKTKTQREMEEKF 664
Cdd:PRK03918 699 LKEELEEREKAKKELEKLEKALERVEELREKV 730
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
355-659 |
1.93e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.69 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 355 EEELRKAHAARSQLETYKRQVVEL---QNRLSEESKKADKlefeYKLLKEKVDGLQK-----EKDRLRTERDSLKETIEE 426
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELerqLKSLERQAEKAER----YKELKAELRELELallvlRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 427 LrcvqaqegqlttsglmplgsQESSDSLAAEIVTPEIKEKLIRLQHenkmlklnqeGSDNEKIALLQSLLDDANLRKNEL 506
Cdd:TIGR02168 251 A--------------------EEELEELTAELQELEEKLEELRLEV----------SELEEEIEELQKELYALANEISRL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 507 ETENRLVNQRLLEVQSQVEELQKSLQEQGSK----AEDSVLLKKKLEEHLEKLHEANNEIQRKRAIIEDLEPRYNNSSLK 582
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKldelAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1729156920 583 IEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGTAPEIQALKNQLQERDRMFHSLEKEYEKTKTQRE 659
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE 457
|
|
| HkD_Gipie |
cd22230 |
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar ... |
12-157 |
5.67e-10 |
|
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: 59.07 E-value: 5.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 12 LGESLLTWIQTF-------------NVEAPCQTVED-------LTNGVVMAQVLQKIDPAYFDENWLNRikteVGDNWRL 71
Cdd:cd22230 4 MSGALVTWALGFeglvgeeedslgfPEEEEEEGTLDaekrflrLSNGDLLNRVMGIIDPSPRGGPRMRG----DDGPAAH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 72 KISNLKKILKGILDYNHEILgQQINDFTLPDVNLIGEH----SDVAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQ 147
Cdd:cd22230 80 RVQNLHILWGRLRDFYQEEL-QQLILSPPPDLQVMGRDpfteEAVQELEKLLRLLLGAAVQCERRELFIRHIQGLDLDVQ 158
|
170
....*....|
gi 1729156920 148 HVVMTAIQEL 157
Cdd:cd22230 159 AELAEAIQEV 168
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
283-591 |
1.19e-09 |
|
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: 62.01 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 283 RQQNEELTTLAEEAQSLKDEMDVLRhssDKVAKLESQVESYKKKLED----LGDLRRQVKLLEEKNTMYMQNTVSLEEEL 358
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQ---SELRRIENRLDELSQELSDasrkIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 359 ----RKAHAARSQLETYKRQVVELQNRLSEESKKADKLEfeYKLLKEKVDGLQKEKDRLRTERDSLKETIEELrcvqaqE 434
Cdd:TIGR02169 747 ssleQEIENVKSELKELEARIEELEEDLHKLEEALNDLE--ARLSHSRIPEIQAELSKLEEEVSRIEARLREI------E 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 435 GQLTTSGLMPLGSQESSDSLAAEIVTPEIKEKLIRLQHENkmlklnqegsDNEKIALLQSLLDDANLRKNELETENRLVN 514
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN----------LNGKKEELEEELEELEAALRDLESRLGDLK 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 515 QRLLEVQSQVEELQKSLQEQGSKAEDSVLLKKKLEEHLEKLHEANNEIQR-KRAIIED--LEPRYNNSSLKIEELQEALR 591
Cdd:TIGR02169 889 KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDpKGEDEEIpeEELSLEDVQAELQRVEEEIR 968
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
153-575 |
2.85e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.82 E-value: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 153 AIQELMSKESPVSVGNDAYVDLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDS 232
Cdd:PRK02224 207 RLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 233 IEDpnspagrrhlqlqtqleqlqeetfRLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQslkdemDVLRHSSDK 312
Cdd:PRK02224 287 RLE------------------------ELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELR------DRLEECRVA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 313 VAKLESQVESYKKKLEDlgdlrrqvklLEEKNTMYMQNTVSLEEELRkahAARSQLETYKRQVVELQNRLSEESKKADKL 392
Cdd:PRK02224 337 AQAHNEEAESLREDADD----------LEERAEELREEAAELESELE---EAREAVEDRREEIEELEEEIEELRERFGDA 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 393 EFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTSGLMPLGSQESSDSLAAEIVTpEIKEKLIRLQH 472
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIE-EDRERVEELEA 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 473 ENKMLKLNQEgSDNEKIALLQSLLDDANlRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDsvlLKKKLEEHL 552
Cdd:PRK02224 483 ELEDLEEEVE-EVEERLERAEDLVEAED-RIERLEERREDLEELIAERRETIEEKRERAEELRERAAE---LEAEAEEKR 557
|
410 420
....*....|....*....|...
gi 1729156920 553 EKLHEANNEIQRKRAIIEDLEPR 575
Cdd:PRK02224 558 EAAAEAEEEAEEAREEVAELNSK 580
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
173-556 |
3.50e-09 |
|
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: 60.47 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 173 DLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLaENQILMERLnqsdsIEDPNSPAGRRHLQLQTQLE 252
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEK-----REYEGYELLKEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 253 QLQEETFRLEAAKDDYRIRCEELEKEIAELRQQNEELTT-----LAEEAQSLKDEMDVLrhsSDKVAKLESQVESYKKKL 327
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKkikdlGEEEQLRVKEKIGEL---EAEIASLERSIAEKEREL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 328 EDLGDLRRQVKLLEEKNTMYMQNtvsLEEELRKAHAARSQLET----YKRQVVELQNRLSEESKKADKLEFEYKLLKEKV 403
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEE---LEREIEEERKRRDKLTEeyaeLKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 404 DGLQKEKDRLRTERDSLKETIEELRCVQAQegqlttsglmplgsqessdsLAAEIvtPEIKEKLIRLQHENKMLKLNQEg 483
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELAD--------------------LNAAI--AGIEAKINELEEEKEDKALEIK- 451
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1729156920 484 SDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDSVLLKKKLEEHLEKLH 556
Cdd:TIGR02169 452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVH 524
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
173-655 |
4.89e-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: 60.07 E-value: 4.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 173 DLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSiedpnspagrrhlqlqtQLE 252
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER-----------------QLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 253 QLQEETFRLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSLKDEM--------DVLRHSSDKVAKLESQVESYK 324
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELesrleeleEQLETLRSKVAQLELQIASLN 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 325 KKLEdlgDLRRQVKLLEEKNTMYMQNTVSLEEELRKA--HAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEK 402
Cdd:TIGR02168 400 NEIE---RLEARLERLEDRRERLQQEIEELLKKLEEAelKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 403 VDGLQKEKDRLRTERDSLKETIEELR-----CVQAQEGQLTTSGLMPLGSQ----ESSDSLAAEIVTPEIKEKLI----- 468
Cdd:TIGR02168 477 LDAAERELAQLQARLDSLERLQENLEgfsegVKALLKNQSGLSGILGVLSElisvDEGYEAAIEAALGGRLQAVVvenln 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 469 ----------------------------RLQHENKMLKLNQEG----------SDNEKIALLQSLL---------DDANL 501
Cdd:TIGR02168 557 aakkaiaflkqnelgrvtflpldsikgtEIQGNDREILKNIEGflgvakdlvkFDPKLRKALSYLLggvlvvddlDNALE 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 502 RKNELETENRLV--------------------NQRLLEVQSQVEELQKSLQEQGSKAEDsvlLKKKLEEHLEKLHEANNE 561
Cdd:TIGR02168 637 LAKKLRPGYRIVtldgdlvrpggvitggsaktNSSILERRREIEELEEKIEELEEKIAE---LEKALAELRKELEELEEE 713
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 562 IQRKRAIIEDLEPRYNNSSLKIEEL---QEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGTA------PEIQA 632
Cdd:TIGR02168 714 LEQLRKELEELSRQISALRKDLARLeaeVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAeieeleAQIEQ 793
|
570 580
....*....|....*....|...
gi 1729156920 633 LKNQLQERDRMFHSLEKEYEKTK 655
Cdd:TIGR02168 794 LKEELKALREALDELRAELTLLN 816
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
213-663 |
9.59e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 9.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 213 KSSLLA-ENQILMERLNQSdsIEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDDYR---IRCEELEKEIAELRQQNEE 288
Cdd:COG4717 36 KSTLLAfIRAMLLERLEKE--ADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAelqEELEELEEELEELEAELEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 289 LTT---LAEEAQSLKDEMDVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEELRkaHAAR 365
Cdd:COG4717 114 LREeleKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLS--LATE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 366 SQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKdrlrtERDSLKETIEELR----------CVQAQEG 435
Cdd:COG4717 192 EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL-----EAAALEERLKEARlllliaaallALLGLGG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 436 QLTTSGLMPLGSQESSDSLAAEIVTPEIKEKLIRLQHENKMLKLN-QEGSDNEKIALLQSLLDDANLRKNELETENRLVN 514
Cdd:COG4717 267 SLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPaLEELEEEELEELLAALGLPPDLSPEELLELLDRI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 515 QRLLEVQSQVEELQKSLQEQGSKAEDSVLLKK---KLEEHLEKLHEANNEIQRKRAIIEDLEPRYNNSSLKIEELQEALr 591
Cdd:COG4717 347 EELQELLREAEELEEELQLEELEQEIAALLAEagvEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL- 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1729156920 592 kkeeemkqMEERYKKYLEKAKSVIRTLDPKQNQGTApEIQALKNQLQ--ERDRMFHSLEKEYEKTKTQREMEEK 663
Cdd:COG4717 426 --------DEEELEEELEELEEELEELEEELEELRE-ELAELEAELEqlEEDGELAELLQELEELKAELRELAE 490
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
174-662 |
1.60e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 174 LDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDPNSpagRRHLQLQTQLEQ 253
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE---ERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 254 LQEETFRLEAAKDDYRIRCEELEKEIAELRQQNEEL---------TTLAEEAQSLKDEMDVLRHSSDKVAKLESQVESYK 324
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAeaelaeaeeALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 325 KKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVD 404
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 405 GLQKEKDRLRTERDSLKETIEE----LRCVQAQEGQLTTSGLMPLGSQESSDSLAAEIVTPEIKEKLIRLQHENKMLKLN 480
Cdd:COG1196 481 ELLEELAEAAARLLLLLEAEADyegfLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 481 QEG----SDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDSVLLKKKLEEHLEKLH 556
Cdd:COG1196 561 AAIeylkAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 557 EANNEIQRKRAIIEDLEPRYNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGTAPEIQALKNQ 636
Cdd:COG1196 641 TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEE 720
|
490 500
....*....|....*....|....*.
gi 1729156920 637 LQERDRMFHSLEKEYEKTKTQREMEE 662
Cdd:COG1196 721 LEEEALEEQLEAEREELLEELLEEEE 746
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
282-652 |
1.65e-08 |
|
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: 58.21 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 282 LRQQNEELTTLAEEAQSLKDEMDVLRHSSDKvaKLESQVESYKKKLEDL-GDLRRQVKLLEEKNTMYMQNTVSLEEELRK 360
Cdd:pfam15921 226 LRELDTEISYLKGRIFPVEDQLEALKSESQN--KIELLLQQHQDRIEQLiSEHEVEITGLTEKASSARSQANSIQSQLEI 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 361 AH-AARSQLETYKRQVVELQNRLSEESKKadkLEFEYKLLKEKVDGLQK-------EKDRLRTERDSLketieelrcvqa 432
Cdd:pfam15921 304 IQeQARNQNSMYMRQLSDLESTVSQLRSE---LREAKRMYEDKIEELEKqlvlansELTEARTERDQF------------ 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 433 qegqlttsglmplgSQES---SDSLAAEIVTPEIKEKLIRLQHENKMLKLNQEGSDNEKIALLQSLLDDANLRKNELETe 509
Cdd:pfam15921 369 --------------SQESgnlDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEA- 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 510 nrLVNQRLLEVQSQVEELQKSLQEQGSKAEDSVLLKKKLEEHLEKLHEANNEIQRKRAIIEDLEPRYNNSSLKIEELQEA 589
Cdd:pfam15921 434 --LLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERA 511
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1729156920 590 LRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGTapEIQALKNQLQERDRMFHSLEKEYE 652
Cdd:pfam15921 512 IEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQT--ECEALKLQMAEKDKVIEILRQQIE 572
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
304-649 |
2.64e-08 |
|
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: 57.76 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 304 DVLRHSSDKVAKLESQVES---YKKKLEDLGDLRRQVKLLEekntmymqntvsLEEELRKAHAARSQLETYKRQVVELQN 380
Cdd:TIGR02168 193 DILNELERQLKSLERQAEKaerYKELKAELRELELALLVLR------------LEELREELEELQEELKEAEEELEELTA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 381 RLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEELRCVQAQegqlttsglmplgSQESSDSLAAEIVt 460
Cdd:TIGR02168 261 ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN-------------LERQLEELEAQLE- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 461 pEIKEKLIRLQHENKMLKlNQEGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQeqgskaed 540
Cdd:TIGR02168 327 -ELESKLDELAEELAELE-EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA-------- 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 541 svLLKKKLEEHLEKLHEANNEIQRKRAIIEDLEPRYnnSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDP 620
Cdd:TIGR02168 397 --SLNNEIERLEARLERLEDRRERLQQEIEELLKKL--EEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
330 340
....*....|....*....|....*....
gi 1729156920 621 KQNqgtapEIQALKNQLQERDRMFHSLEK 649
Cdd:TIGR02168 473 AEQ-----ALDAAERELAQLQARLDSLER 496
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
318-558 |
3.09e-08 |
|
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: 56.31 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 318 SQVESYKKKLEDLGDLRRQVKLLEEKntmymqntvsLEEELRKAHAARSQLETYKRQVVELQNRLSEeskkadkLEFEYK 397
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKE----------LAALKKEEKALLKQLAALERRIAALARRIRA-------LEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 398 LLKEKVDGLQKEKDRLRTERDSLKETIEELrcVQAQEGQLTTSGLMPLGSQESSDSLAA-----EIVTPEIKEKLIRLQH 472
Cdd:COG4942 80 ALEAELAELEKEIAELRAELEAQKEELAEL--LRALYRLGRQPPLALLLSPEDFLDAVRrlqylKYLAPARREQAEELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 473 ENKMLKLNQEGSDNEKiALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDSVLLKKKLEEHL 552
Cdd:COG4942 158 DLAELAALRAELEAER-AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
....*.
gi 1729156920 553 EKLHEA 558
Cdd:COG4942 237 AAAAER 242
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
260-706 |
3.16e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 260 RLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSLkdemdvLRHSSDKVAKLESQVESYKKKLEDLgdLRRQVKL 339
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAE------EYELLAELARLEQDIARLEERRREL--EERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 340 LEEKNtmymQNTVSLEEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDS 419
Cdd:COG1196 322 EEELA----ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 420 LKETIEELRCVQAQEGQLTTSglmpLGSQESSDSLAAEivtpEIKEKLIRLQHENKMLKLNQEGSDNEKIALLQSLLDDa 499
Cdd:COG1196 398 LAAQLEELEEAEEALLERLER----LEEELEELEEALA----ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL- 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 500 nLRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDSVLLKKKLEEHLEKLHEANNEIQRKRAIIEDLEprynns 579
Cdd:COG1196 469 -LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE------ 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 580 slkiEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQN-QGTAPEIQALKNQLQERDRMFHSLEKEYEKTKTQR 658
Cdd:COG1196 542 ----AALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKiRARAALAAALARGAIGAAVDLVASDLREADARYYV 617
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1729156920 659 EME---EKFIVSAWYNMGMTLHKKAAEDRLASTGSGQSFLARQRQATNTRR 706
Cdd:COG1196 618 LGDtllGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR 668
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
259-519 |
7.35e-08 |
|
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: 56.22 E-value: 7.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 259 FRLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSLKDEMDV-LRHSSDKVAKLESQVESYKKKLEDLG----DL 333
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQqKQILRERLANLERQLEELEAQLEELEskldEL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 334 RRQVKLLEEKNTMYMQNTVSLEEELRKAHA----ARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKE 409
Cdd:TIGR02168 336 AEELAELEEKLEELKEELESLEAELEELEAeleeLESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDR 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 410 KDRLRTERDSLKETIEELRcVQAQEGQLTTSGLMPLGSQESSDSLAAEIvtpEIKEKLIRLQHENKMLKLNQEGSDNEKI 489
Cdd:TIGR02168 416 RERLQQEIEELLKKLEEAE-LKELQAELEELEEELEELQEELERLEEAL---EELREELEEAEQALDAAERELAQLQARL 491
|
250 260 270
....*....|....*....|....*....|
gi 1729156920 490 ALLQSLLddanlrkNELETENRLVNQRLLE 519
Cdd:TIGR02168 492 DSLERLQ-------ENLEGFSEGVKALLKN 514
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
173-427 |
1.41e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.07 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 173 DLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAE-------------NQILMERLNQSDSIEDPNSP 239
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlshsripeiqaelSKLEEEVSRIEARLREIEQK 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 240 AGRRHLQLQTQLEQLQEetfrLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQ-SLKDEMDVLRHSSDKVAKLES 318
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQE----LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEaALRDLESRLGDLKKERDELEA 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 319 QVESYKKKLEDLG----DLRRQVKLLEEKNTMYMQNTVSLEEELRK---AHAARSQLETYKRQVVELQNRLSEESKKADK 391
Cdd:TIGR02169 897 QLRELERKIEELEaqieKKRKRLSELKAKLEALEEELSEIEDPKGEdeeIPEEELSLEDVQAELQRVEEEIRALEPVNML 976
|
250 260 270
....*....|....*....|....*....|....*.
gi 1729156920 392 LEFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEEL 427
Cdd:TIGR02169 977 AIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
179-582 |
1.42e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 179 KKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDsiEDPNSPAGRRHLQLQTQLEQLQEET 258
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE--EKKKAEEAKKAEEDKNMALRKAEEA 1586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 259 FRLEAAKDDYRIRCEELEKEI-AELRQQNEELTTLAEEAQSLKDEMDVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQV 337
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEEKKMkAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 338 KLLEEKNTMYMQNTVSLEEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTER 417
Cdd:PTZ00121 1667 AKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA 1746
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 418 DSLKETIEELRCVQ---------AQEGQLTTSGLMPLGSQESSDSLAAEI--VTPEIKEKLIRLQHENKMLKLNQEGSDN 486
Cdd:PTZ00121 1747 EEAKKDEEEKKKIAhlkkeeekkAEEIRKEKEAVIEEELDEEDEKRRMEVdkKIKDIFDNFANIIEGGKEGNLVINDSKE 1826
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 487 EKIALLQSLLDDANLRKNELEtenrlvnqrllEVQSQVEELQKSLQEQGSKAEDSVLLKKKLEEHLEKLHEANneiQRKR 566
Cdd:PTZ00121 1827 MEDSAIKEVADSKNMQLEEAD-----------AFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEAD---EIEK 1892
|
410
....*....|....*.
gi 1729156920 567 AIIEDLEPRYNNSSLK 582
Cdd:PTZ00121 1893 IDKDDIEREIPNNNMA 1908
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
260-662 |
2.69e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 260 RLEAAKDDYRIRCEELEKEIAEL----RQQNEELTTLAEEAQSLKDEMDVLRHSSDKVAKLESQVESYKKKLED-LGDLR 334
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREELaeevRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDrLEECR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 335 RQVKLLEEKNTMYMQNTVSLEEELRKAH-----------AARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKV 403
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDLEERAEELReeaaeleseleEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 404 DGLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTSGLMPLGSQESSDSLAAEIvtpeikeklirlqhenkmlklnqeg 483
Cdd:PRK02224 415 EELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVET------------------------- 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 484 sdnekiallqslLDDANLRKNELETEnrlvnqrLLEVQSQVEELQKSLQEqgskAEDSVLLKKKLEEHLEKLHEANNEIQ 563
Cdd:PRK02224 470 ------------IEEDRERVEELEAE-------LEDLEEEVEEVEERLER----AEDLVEAEDRIERLEERREDLEELIA 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 564 RKRAIIEDLEPRYNNSSLKIEELQEALRKKEEEMKQMEERykkyLEKAKSVIRTLDPKQNQGTApEIQALKN---QLQER 640
Cdd:PRK02224 527 ERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEE----AEEAREEVAELNSKLAELKE-RIESLERirtLLAAI 601
|
410 420
....*....|....*....|..
gi 1729156920 641 DRMFHSLEKEYEKTKTQREMEE 662
Cdd:PRK02224 602 ADAEDEIERLREKREALAELND 623
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
174-471 |
2.89e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 174 LDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDsiedpnspagRRHLQLQTQLEQ 253
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK----------ERLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 254 LQEETFRLEAAKDDYRIRCEELEKEIAELRQQNEEL--TTLAEEAQSLKDEMDVLRhssDKVAKLESQVESYKKKLEDLg 331
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLeaRLSHSRIPEIQAELSKLE---EEVSRIEARLREIEQKLNRL- 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 332 DLRRQvkLLEEKntmyMQNTVSLEEELRKAHAARSQ-LETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEK 410
Cdd:TIGR02169 825 TLEKE--YLEKE----IQELQEQRIDLKEQIKSIEKeIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL 898
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 411 DRLRTERDSLKETIEELRC--------VQAQEGQLTTSG-LMPLGSQESSDSLAAEIVTPEIKEKLIRLQ 471
Cdd:TIGR02169 899 RELERKIEELEAQIEKKRKrlselkakLEALEEELSEIEdPKGEDEEIPEEELSLEDVQAELQRVEEEIR 968
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
260-665 |
3.21e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 260 RLEAAKDDYRIRCEELEKEIAE-------LRQQNEELTTLAEEAQSLkdeMDVLRHSSDKVAKLESQVESYKKKLEDLGD 332
Cdd:PRK03918 166 NLGEVIKEIKRRIERLEKFIKRtenieelIKEKEKELEEVLREINEI---SSELPELREELEKLEKEVKELEELKEEIEE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 333 LRRQVKLLEEKNTMYMQNTVSLEEELRKAHAARSQLETYKRQVVELQnrlsEESKKADKLEFEYKLLKEKVDGLQKEKDR 412
Cdd:PRK03918 243 LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK----EKAEEYIKLSEFYEEYLDELREIEKRLSR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 413 LRTERDSLKETIEELRCVQAQEGQLTTSglmplgSQESSDSLAAEIVTPEIKEKLIRLQHENKMLKLNQEGSDNEKIAll 492
Cdd:PRK03918 319 LEEEINGIEERIKELEEKEERLEELKKK------LKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLE-- 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 493 qSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDSVLLKKKLEEHLEKlheanNEIQRKRAIIEDL 572
Cdd:PRK03918 391 -KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRK-----ELLEEYTAELKRI 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 573 EPRYNNSSLKIEELQEALRkkeeemkqmeeRYKKYLEKAKSVIRTLDpkqnqgTAPEIQALKNQLQErdrmfHSLEKEYE 652
Cdd:PRK03918 465 EKELKEIEEKERKLRKELR-----------ELEKVLKKESELIKLKE------LAEQLKELEEKLKK-----YNLEELEK 522
|
410
....*....|...
gi 1729156920 653 KTKTQREMEEKFI 665
Cdd:PRK03918 523 KAEEYEKLKEKLI 535
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
271-665 |
8.60e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 8.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 271 RCEELEKEIAELRQQNEELTTLAEE---AQSLKDEMDVLRHSSD--KVAKLESQVESYKKKLEDLGDLRRQVKLLEEKNT 345
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKAAAAkkkADEAKKKAEEKKKADEakKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 346 MymQNTVSLEEELRKAHAARSQLETYKRQVVELQNRlSEESKKADKL----------EFEYKLLKEKVDGLQKEKDRLRT 415
Cdd:PTZ00121 1472 A--DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA-AEAKKKADEAkkaeeakkadEAKKAEEAKKADEAKKAEEKKKA 1548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 416 ERDSLKETIEELRCVQAQEGQLTTSGLMPLGSQESSDSLAAEIVTPEIKEKLIRLQHENKMLKLNQEGSDNEKIALLQsl 495
Cdd:PTZ00121 1549 DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK-- 1626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 496 lddanlRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDsvlLKKKLEEHLEKLHEANNEIQRKRAIIEDLEpR 575
Cdd:PTZ00121 1627 ------KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE---EAKKAEEDKKKAEEAKKAEEDEKKAAEALK-K 1696
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 576 YNNSSLKIEELqealRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQgTAPEIQALKNQLQERDRMFHSLEKEYEKTK 655
Cdd:PTZ00121 1697 EAEEAKKAEEL----KKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE-DKKKAEEAKKDEEEKKKIAHLKKEEEKKAE 1771
|
410
....*....|
gi 1729156920 656 TQREMEEKFI 665
Cdd:PTZ00121 1772 EIRKEKEAVI 1781
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
173-639 |
9.84e-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: 9.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 173 DLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDpnsPAGRRHLQLQTQLE 252
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA---EAEEELEELAEELL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 253 QLQEETFRLEAAKDDYRIRCEELEKEIAELRQQNEEL-TTLAEEAQSLKDEMDVLRHSSDKVAKLESQVESYKKKLEDLG 331
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELeEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 332 DLRRQVKLLEEKNTMYMQNTVSLEEELRKAHAARSQLE--TYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKE 409
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLegVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 410 KDRLRTERDsLKETIEELRcvQAQEGQLTtsgLMPLGSQESSDSLAAEIVTPEIKEKLIRLQHENKML--KLNQEGSDNE 487
Cdd:COG1196 550 NIVVEDDEV-AAAAIEYLK--AAKAGRAT---FLPLDKIRARAALAAALARGAIGAAVDLVASDLREAdaRYYVLGDTLL 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 488 KIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGS----KAEDSVLLKKKLEEHLEKLHEANNEIQ 563
Cdd:COG1196 624 GRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAalleAEAELEELAERLAEEELELEEALLAEE 703
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1729156920 564 RKRAIIEDLEPRYNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGTApEIQALKNQLQE 639
Cdd:COG1196 704 EEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER-ELERLEREIEA 778
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
273-591 |
1.10e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 52.28 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 273 EELEKEIAELRQQNEELTTLAEEAQSLKDEMDV----LRHSSDKVAKLESQVESYKKKLEDLGDLRRQVKLLEEKNTMYM 348
Cdd:pfam02463 202 LKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLneerIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEK 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 349 QNTVSLEEELRKAHA-ARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEEL 427
Cdd:pfam02463 282 KLQEEELKLLAKEEEeLKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEEL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 428 RCVQAQEgqlttsglmplgSQESSDSLAAEIVTPEIKEKLIRLQHENKMLKLNQEGSDNEKIALLQSLLDDANLRKNELE 507
Cdd:pfam02463 362 EKLQEKL------------EQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEEL 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 508 TENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDSVLLKKKLEEHLEKLHEANNEIQRKRAIIEDLEPRYNNSSLKIEELQ 587
Cdd:pfam02463 430 EILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGL 509
|
....
gi 1729156920 588 EALR 591
Cdd:pfam02463 510 KVLL 513
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
304-591 |
1.72e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 304 DVLRHSSDKVAKLESQVESYKkkleDLGDLRRQVK--LLEEKNTM--------YMQNTVSLEEELRKAHAARSQLEtykr 373
Cdd:COG4913 184 RRLGIGSEKALRLLHKTQSFK----PIGDLDDFVReyMLEEPDTFeaadalveHFDDLERAHEALEDAREQIELLE---- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 374 QVVELQNRLSEESKKADKLEF------------EYKLLKEKVDGLQKEKDRLRTERDSLKETIEELRcvqaqegqlttsg 441
Cdd:COG4913 256 PIRELAERYAAARERLAELEYlraalrlwfaqrRLELLEAELEELRAELARLEAELERLEARLDALR------------- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 442 lmplgsqessdslaaeivtpeikEKLIRLQHEnkmlklnQEGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQ 521
Cdd:COG4913 323 -----------------------EELDELEAQ-------IRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALG 372
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1729156920 522 SQVEELQKSLQEQGSKAEDSV--------LLKKKLEEHLEKLHEANNEIQRKRAIIEDLEPRYNNSSLKIEELQEALR 591
Cdd:COG4913 373 LPLPASAEEFAALRAEAAALLealeeeleALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
260-499 |
1.87e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 260 RLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAE-------------EAQSLKDEMDVLRHSSDKVAKLESQVESYKKK 326
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeidvasaerEIAELEAELERLDASSDDLAALEEQLEELEAE 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 327 LEDL----GDLRRQVKLLEEKNTmymqntvSLEEELRKAHAARSQLETYKRQVV--ELQNRLSEESKKAdklefeykLLK 400
Cdd:COG4913 701 LEELeeelDELKGEIGRLEKELE-------QAEEELDELQDRLEAAEDLARLELraLLEERFAAALGDA--------VER 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 401 EKVDGLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTSGLMP-LGSQESSDSLAAEIVT---PEIKEKLIRLQHENKm 476
Cdd:COG4913 766 ELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDAdLESLPEYLALLDRLEEdglPEYEERFKELLNENS- 844
|
250 260
....*....|....*....|...
gi 1729156920 477 lklnqegsdNEKIALLQSLLDDA 499
Cdd:COG4913 845 ---------IEFVADLLSKLRRA 858
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
384-659 |
1.98e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 384 EESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTSGLMPLGSQESSDSLAAEIVTpei 463
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA--- 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 464 kekliRLQHENKMLKlNQEGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDSVL 543
Cdd:TIGR02168 751 -----QLSKELTELE-AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 544 LKKKLEEHLE----KLHEANNEIQRKRAIIEDLEPRYNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLD 619
Cdd:TIGR02168 825 RLESLERRIAaterRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1729156920 620 PKQNqgtapEIQALKNQLQERDRMFHSLEKEYEKTKTQRE 659
Cdd:TIGR02168 905 ELES-----KRSELRRELEELREKLAQLELRLEGLEVRID 939
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
327-663 |
2.69e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 327 LEDL-GDLRRQVKlleekntmymqntvSLEEELRKAHAARsqleTYKRQVVELQNRLSeeSKKADKLEFEYKLLKEKVDG 405
Cdd:COG1196 191 LEDIlGELERQLE--------------PLERQAEKAERYR----ELKEELKELEAELL--LLKLRELEAELEELEAELEE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 406 LQKEKDRLRTERDSLKETIEELRCVQAQEgqlttsglmplgSQESSDSLAAEIvtpEIKEKLIRLQHENKMLKlnqegsd 485
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEEL------------ELELEEAQAEEY---ELLAELARLEQDIARLE------- 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 486 nEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDsvlLKKKLEEHLEKLHEANNEIQRK 565
Cdd:COG1196 309 -ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE---AEEALLEAEAELAEAEEELEEL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 566 RAIIEDLEPRYNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQgtapEIQALKNQLQERDRMFH 645
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA----LEEAAEEEAELEEEEEA 460
|
330
....*....|....*...
gi 1729156920 646 SLEKEYEKTKTQREMEEK 663
Cdd:COG1196 461 LLELLAELLEEAALLEAA 478
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
266-658 |
2.76e-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: 51.22 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 266 DDYRIRCEELEKEIAELRQQNEELTTLAEEaqsLKDEMDVLRHSSDKVaklesqvESYKKKLEDLGDLRRQVKLLEEKNT 345
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDE---KRQQLERLRREREKA-------ERYQALLKEKREYEGYELLKEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 346 MYMQNTV-----SLEEELRKAHAARSQLEtykRQVVELQNRLSEESKKADKL-EFEYKLLKEKVDGLQKEKDRLRterDS 419
Cdd:TIGR02169 236 ERQKEAIerqlaSLEEELEKLTEEISELE---KRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLE---RS 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 420 LKETIEELRCVQAQEGQLttsglmplgsQESSDSLAAEIvtPEIKEKLIRLQHENKMLKlnqegsdnEKIALLQSLLDDA 499
Cdd:TIGR02169 310 IAEKERELEDAEERLAKL----------EAEIDKLLAEI--EELEREIEEERKRRDKLT--------EEYAELKEELEDL 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 500 NLRKNELETENRLVNQRLLEVQSQVEELQKSLQEqgSKAEDSVLLKKKLEEHlEKLHEANNEIQRKRAIIEDLEPRYNNS 579
Cdd:TIGR02169 370 RAELEEVDKEFAETRDELKDYREKLEKLKREINE--LKRELDRLQEELQRLS-EELADLNAAIAGIEAKINELEEEKEDK 446
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1729156920 580 SLKIEELQEALrkkeeemkqmeERYKKYLEKAKSvirtldpkqnqgtapEIQALKNQLQERDRMFHSLEKEYEKTKTQR 658
Cdd:TIGR02169 447 ALEIKKQEWKL-----------EQLAADLSKYEQ---------------ELYDLKEEYDRVEKELSKLQRELAEAEAQA 499
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
273-427 |
2.89e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 273 EELEKEIAELRqqnEELTTLAEEAQSLKDEMDVLRHSSDKVAKLESQVESykkkLEDLGDLRRQVklleekntmymqntV 352
Cdd:COG4913 613 AALEAELAELE---EELAEAEERLEALEAELDALQERREALQRLAEYSWD----EIDVASAEREI--------------A 671
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1729156920 353 SLEEELRKAHAARSQLETYKRQVVELQNRLseeskkaDKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEEL 427
Cdd:COG4913 672 ELEAELERLDASSDDLAALEEQLEELEAEL-------EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
260-426 |
3.18e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.15 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 260 RLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSLKDEMDV-LRHSSDKVAKLESQVESYKKKLEDLGDLRRQVK 338
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKeIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 339 LLEEKNTMYMQNTVsLEEELRKAHAarsQLETYKRQVVELQNRLSEESKKADKLEFEyklLKEKVDGLQKEKDRLRTERD 418
Cdd:COG1579 94 LQKEIESLKRRISD-LEDEILELME---RIEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAERE 166
|
....*...
gi 1729156920 419 SLKETIEE 426
Cdd:COG1579 167 ELAAKIPP 174
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
262-659 |
5.95e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 5.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 262 EAAKDDYRIRCEELEKEiAELRQQNEELTTLAEEAQSLKDEMDvlrhssdKVAKLESQVESYKKKLEDLGDLRRQVKLLE 341
Cdd:PTZ00121 1370 EKKKEEAKKKADAAKKK-AEEKKKADEAKKKAEEDKKKADELK-------KAAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 342 EKNTMymQNTVSLEEELRKAHAARSQLETyKRQVVELQNRlSEESKKADKLEFEYKLLKEKVDGLQKeKDRLRTERDSLK 421
Cdd:PTZ00121 1442 EAKKA--DEAKKKAEEAKKAEEAKKKAEE-AKKADEAKKK-AEEAKKADEAKKKAEEAKKKADEAKK-AAEAKKKADEAK 1516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 422 ETIEELRCVQAQEGQLTTSglmplgsqessdslAAEIVTPEIKEKLIRLQHENKMLKLNQEGSDNEKiallQSLLDDANL 501
Cdd:PTZ00121 1517 KAEEAKKADEAKKAEEAKK--------------ADEAKKAEEKKKADELKKAEELKKAEEKKKAEEA----KKAEEDKNM 1578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 502 RKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDSVLLK---KKLEEHLEKLHEANNEIQRKRAIIEDLEPRYNN 578
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAeelKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 579 SSLKIEELQ----------EALRKKEEEMKQMEERYKKYLEKAKSVIRTldPKQNQGTAPEIQALKNQLQERDRMFHSLE 648
Cdd:PTZ00121 1659 NKIKAAEEAkkaeedkkkaEEAKKAEEDEKKAAEALKKEAEEAKKAEEL--KKKEAEEKKKAEELKKAEEENKIKAEEAK 1736
|
410
....*....|.
gi 1729156920 649 KEYEKTKTQRE 659
Cdd:PTZ00121 1737 KEAEEDKKKAE 1747
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
191-439 |
6.94e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 6.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 191 TKEEIAQRCHELDMQVAALQEEKSSL---LAENQILMERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDD 267
Cdd:PRK02224 469 TIEEDRERVEELEAELEDLEEEVEEVeerLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAE 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 268 YRIRCEELEKEIAELRQQNEE----LTTLAEEAQSLKDEMDVL---RHSSDKVAKLESQVESYKKKLEDLGDLRRQVK-L 339
Cdd:PRK02224 549 LEAEAEEKREAAAEAEEEAEEareeVAELNSKLAELKERIESLeriRTLLAAIADAEDEIERLREKREALAELNDERReR 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 340 LEEKNTMYMQNTVSLEEE-LRKAHAARSQLETYKRQVVElqnRLSEESKKADKLEFEYKLLKEKVDGLqkekDRLRTERD 418
Cdd:PRK02224 629 LAEKRERKRELEAEFDEArIEEAREDKERAEEYLEQVEE---KLDELREERDDLQAEIGAVENELEEL----EELRERRE 701
|
250 260
....*....|....*....|.
gi 1729156920 419 SLKETIEELRCVQAQEGQLTT 439
Cdd:PRK02224 702 ALENRVEALEALYDEAEELES 722
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
169-709 |
7.17e-06 |
|
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: 49.73 E-value: 7.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 169 DAYVDLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAAL-----QEEKSSLLAENQilMERLNQSDSIEDPNSPAGRR 243
Cdd:pfam15921 342 DKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLladlhKREKELSLEKEQ--NKRLWDRDTGNSITIDHLRR 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 244 HLQLQTQLEQlqeetfRLEAAKDDYRIRCE-ELEKEIAELRQQNEELTTLAEEAQSLKDEMDVLRHSSDKVAKLESQVES 322
Cdd:pfam15921 420 ELDDRNMEVQ------RLEALLKAMKSECQgQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLES 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 323 YKKKLEDL-GDLRRQVKLLEEKNT-------------MYMQNTVSLEEELRKAHAARSQL-----------ETYKRQVVE 377
Cdd:pfam15921 494 SERTVSDLtASLQEKERAIEATNAeitklrsrvdlklQELQHLKNEGDHLRNVQTECEALklqmaekdkviEILRQQIEN 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 378 LQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEELRcVQAQEGQLTTSGLMPLGSQESSdslaae 457
Cdd:pfam15921 574 MTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELE-ARVSDLELEKVKLVNAGSERLR------ 646
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 458 iVTPEIKEKLIRLQHENKMLKlNQEGSDNEKIALLQSLLDDanlRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSK 537
Cdd:pfam15921 647 -AVKDIKQERDQLLNEVKTSR-NELNSLSEDYEVLKRNFRN---KSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGS 721
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 538 AEDSVLLKKKLEEHLEKLHEANNEIQRKRAIIEDLEPRYNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRT 617
Cdd:pfam15921 722 DGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERR 801
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 618 LDPK-QNQGTAPEIQALknQLQERDRMFHSLEKEYEKTKTQREMEEKFIVSAWY----NMGMTLHKKAAEDR----LAST 688
Cdd:pfam15921 802 LKEKvANMEVALDKASL--QFAECQDIIQRQEQESVRLKLQHTLDVKELQGPGYtsnsSMKPRLLQPASFTRthsnVPSS 879
|
570 580
....*....|....*....|.
gi 1729156920 689 GSGQSFLARQRQATNTRRSYP 709
Cdd:pfam15921 880 QSTASFLSHHSRKTNALKEDP 900
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
173-427 |
7.73e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 7.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 173 DLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAE----NQILMERLNQSDSIEDPNSPAGRRHLQLQ 248
Cdd:TIGR02168 723 ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERleeaEEELAEAEAEIEELEAQIEQLKEELKALR 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 249 TQLEQLQEETFRLEAAKDDYRIRCEELEKEIAELRQQNEElttLAEEAQSLKDEMDVLRHSsdkVAKLESQVESYKKKLE 328
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLED---LEEQIEELSEDIESLAAE---IEELEELIEELESELE 876
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 329 DLGDLRRQVK-LLEEKNTMYMQNTVSLEEELRKAHAARSQLETYKRQVVELQNRLSE--------ESKKADKLEFEYKLL 399
Cdd:TIGR02168 877 ALLNERASLEeALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGlevridnlQERLSEEYSLTLEEA 956
|
250 260
....*....|....*....|....*...
gi 1729156920 400 KEKVDGLQKEKDRLRTERDSLKETIEEL 427
Cdd:TIGR02168 957 EALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
173-594 |
1.42e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 173 DLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDPnspAGRRHLQLQTQLE 252
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE---EEEALEEAAEEEA 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 253 QLQEETFRLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSLKDEMDVLRHSSDKVAKLESQVESYKKKLEDLGD 332
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 333 LRRQVKLLEEKNTMYMQNTV--------SLEEELRKAHAAR------------SQLETYKRQVVELQNRLSEESKKADKL 392
Cdd:COG1196 533 EAAYEAALEAALAAALQNIVveddevaaAAIEYLKAAKAGRatflpldkirarAALAAALARGAIGAAVDLVASDLREAD 612
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 393 EFEYKLLKEKVdGLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTSGLMPLGSQESSDSLAAEIVTpEIKEKLIRLQH 472
Cdd:COG1196 613 ARYYVLGDTLL-GRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEA-ELEELAERLAE 690
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 473 ENKMLKLNQEgsdnEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDSVLLKKKLEEHL 552
Cdd:COG1196 691 EELELEEALL----AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1729156920 553 EKLHEANNEIQRK-----RAIIE--DLEPRYNNSSLKIEELQEALRKKE 594
Cdd:COG1196 767 RELERLEREIEALgpvnlLAIEEyeELEERYDFLSEQREDLEEARETLE 815
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
309-591 |
1.56e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 309 SSDKVAKLESQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEELRkahAARSQLETYKRQVVELQNRLSEESKK 388
Cdd:PRK03918 146 SREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIK---EKEKELEEVLREINEISSELPELREE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 389 ADKLEFEYKLL---KEKVDGLQKEKDRLRTERDSLKETIEELRcvqaqegqlttsglmplgsqessDSLAaeivtpEIKE 465
Cdd:PRK03918 223 LEKLEKEVKELeelKEEIEELEKELESLEGSKRKLEEKIRELE-----------------------ERIE------ELKK 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 466 KLIRLqhENKMLKLNQEGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDSVLLK 545
Cdd:PRK03918 274 EIEEL--EEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELE 351
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1729156920 546 KKLEEhLEKLHEANNEIQRKRAIIEDLEPRYNNSSL-KIEELQEALR 591
Cdd:PRK03918 352 KRLEE-LEERHELYEEAKAKKEELERLKKRLTGLTPeKLEKELEELE 397
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
260-663 |
1.61e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 260 RLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSLKDEMDVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQVKL 339
Cdd:PTZ00121 1225 KAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKA 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 340 LEEKNTmymqntvslEEELRKAHAARSQLETYKRQVVELQNRlSEESKKAD--------KLEFEYKLLKEKVDGLQKEKD 411
Cdd:PTZ00121 1305 DEAKKK---------AEEAKKADEAKKKAEEAKKKADAAKKK-AEEAKKAAeaakaeaeAAADEAEAAEEKAEAAEKKKE 1374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 412 RLRTERDSLKETIEELRcvQAQEGQLTTSGLMPlGSQESSDSLAAEIVTPEIKEKLIRLQHENKMLKLNQEGSDNEKIAL 491
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEKK--KADEAKKKAEEDKK-KADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKK 1451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 492 LQSLLDDA-NLRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDSvllkKKLEEHLEKLHEANNEIQRKRAIie 570
Cdd:PTZ00121 1452 KAEEAKKAeEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEA----KKAAEAKKKADEAKKAEEAKKAD-- 1525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 571 dlEPRYNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGTAPEIQALKNQLQERDRMFHSLEKE 650
Cdd:PTZ00121 1526 --EAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE 1603
|
410
....*....|....*.
gi 1729156920 651 YEKTKTQ---REMEEK 663
Cdd:PTZ00121 1604 EKKMKAEeakKAEEAK 1619
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
360-567 |
1.72e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 360 KAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEEL------RCVQAQ 433
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERreelgeRARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 434 EGQLTTSGLMPLGSQESSDSLAaeivtpeikeklirlqheNKMLKLNQ-EGSDNEKIALLQSLLDDANLRKNELETENRL 512
Cdd:COG3883 97 RSGGSVSYLDVLLGSESFSDFL------------------DRLSALSKiADADADLLEELKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1729156920 513 VNQRLLEVQSQVEELQKSLQEQGSKAEDSVLLKKKLEEHLEKLHEANNEIQRKRA 567
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
144-666 |
1.83e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 144 ESVQHVVMTAIQELMSKESPVSVGNDAYVDLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQIL 223
Cdd:TIGR02168 284 EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 224 -MERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAkddyRIRCEELEKEIAELRQQNEELTTLAEEAQSLKDE 302
Cdd:TIGR02168 364 eAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL----EARLERLEDRRERLQQEIEELLKKLEEAELKELQ 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 303 M----------DVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQVKLLEEKNTMymqnTVSLEEELRKAHAARSQLETYK 372
Cdd:TIGR02168 440 AeleeleeeleELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS----LERLQENLEGFSEGVKALLKNQ 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 373 RQVVELQNRLSeeskkaDKLEFE--YKLLKEK----------VDGLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTS 440
Cdd:TIGR02168 516 SGLSGILGVLS------ELISVDegYEAAIEAalggrlqavvVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGN 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 441 GLMPLGSQESSDSLAAEIVTPEIK----------------------EKLIRLQHENKMLKLNQE---------GSDNEKI 489
Cdd:TIGR02168 590 DREILKNIEGFLGVAKDLVKFDPKlrkalsyllggvlvvddldnalELAKKLRPGYRIVTLDGDlvrpggvitGGSAKTN 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 490 ALLQSllddanlRKNELETenrlVNQRLLEVQSQVEELQKSLQ----EQGSKAEDSVLLKKKLEEHLEKLHEANNEIQRK 565
Cdd:TIGR02168 670 SSILE-------RRREIEE----LEEKIEELEEKIAELEKALAelrkELEELEEELEQLRKELEELSRQISALRKDLARL 738
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 566 RAIIEDLEPRYNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGTAPE--IQALKNQLQERDRM 643
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALReaLDELRAELTLLNEE 818
|
570 580
....*....|....*....|...
gi 1729156920 644 FHSLEKEYEKTKTQREMEEKFIV 666
Cdd:TIGR02168 819 AANLRERLESLERRIAATERRLE 841
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
360-591 |
2.58e-05 |
|
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: 47.07 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 360 KAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEELrcvQAQEGQLTT 439
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL---EKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 440 SglmplgSQESSDSLAAEIVTpeikekLIRL-QHENKMLKLNQEGSD--NEKIALLQSLLDDANLRKNELETENRLVNQR 516
Cdd:COG4942 98 E------LEAQKEELAELLRA------LYRLgRQPPLALLLSPEDFLdaVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1729156920 517 LLEVQSQVEELQKSLQEQGSKAEDsvlLKKKLEEHLEKLHEANNEIQRKRAIIEDLEPRYNNSSLKIEELQEALR 591
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAA---LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
298-567 |
4.22e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.84 E-value: 4.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 298 SLKDEMD-VLR--HSSDKVaklesQVESYKKKLEDLgdlrrQVKLLEEKNTMYMQNTVSLEEELRKAHAARSQLETYKrq 374
Cdd:PRK05771 13 TLKSYKDeVLEalHELGVV-----HIEDLKEELSNE-----RLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVS-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 375 VVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLK--ETIE-ELRCVQAQEGQLTTSGLMPLGSQESS 451
Cdd:PRK05771 81 VKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwGNFDlDLSLLLGFKYVSVFVGTVPEDKLEEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 452 DSLAAEIVTPEIKEKlirlqHENKMLKLNQEGSDNEKIAllqSLLDDANLRKNELETEnRLVNQRLLEVQSQVEELQKSL 531
Cdd:PRK05771 161 KLESDVENVEYISTD-----KGYVYVVVVVLKELSDEVE---EELKKLGFERLELEEE-GTPSELIREIKEELEEIEKER 231
|
250 260 270
....*....|....*....|....*....|....*.
gi 1729156920 532 QEQGSKAEDsvlLKKKLEEHLEKLHEAnNEIQRKRA 567
Cdd:PRK05771 232 ESLLEELKE---LAKKYLEELLALYEY-LEIELERA 263
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
261-428 |
4.27e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 261 LEAAKDDYRIRCEELEKEIAELRQQNEeLTTLAEEAQSLKDEMDVLRhssDKVAKLESQVESYKKKLEDLgdlRRQVKLL 340
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNG-LVDLSEEAKLLLQQLSELE---SQLAEARAELAEAEARLAAL---RAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 341 EEKNTMYMQNTV--SLEEELRKAHAARSQLET-----------YKRQVVELQNRLSEESKKA-DKLEFEYKLLKEKVDGL 406
Cdd:COG3206 253 PDALPELLQSPViqQLRAQLAELEAELAELSArytpnhpdviaLRAQIAALRAQLQQEAQRIlASLEAELEALQAREASL 332
|
170 180
....*....|....*....|..
gi 1729156920 407 QKEKDRLRTERDSLKETIEELR 428
Cdd:COG3206 333 QAQLAQLEARLAELPELEAELR 354
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
261-554 |
5.54e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.76 E-value: 5.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 261 LEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEA-QSLKDEMDVLR-----HSSDKVAKLESQVESYKKKLEDLGDLR 334
Cdd:pfam12128 609 AEEALQSAREKQAAAEEQLVQANGELEKASREETFArTALKNARLDLRrlfdeKQSEKDKKNKALAERKDSANERLNSLE 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 335 RQVKLLEEKNTMYMQNTvslEEELRKAHAARSQletyKRQVVELQNRLSEESKKADKLEfEYKLLKEKVDGLQKEKDR-- 412
Cdd:pfam12128 689 AQLKQLDKKHQAWLEEQ---KEQKREARTEKQA----YWQVVEGALDAQLALLKAAIAA-RRSGAKAELKALETWYKRdl 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 413 ------------LRTERDSLKETIEELrcvqAQEGQLTTSGLMPLGSQESSDSLAAEIVTPEIKEKLIRLQHENKMLKLN 480
Cdd:pfam12128 761 aslgvdpdviakLKREIRTLERKIERI----AVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIAD 836
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1729156920 481 QEgSDNEKIALLQSLLDDANLRKNELETENRLVNQRL--LEVQSQVEELQKSLQEQGSKAEDSVLLKKKLEEHLEK 554
Cdd:pfam12128 837 TK-LRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLatLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKK 911
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
173-427 |
6.27e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.59 E-value: 6.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 173 DLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQ-----------SDSIEDPNSPAG 241
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaanlrerLESLERRIAATE 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 242 RRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEIAELrqqNEELTTLAEEAQSLKDEMDVLrhsSDKVAKLESQVE 321
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL---LNERASLEEALALLRSELEEL---SEELRELESKRS 911
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 322 SYKKKLEDLGDLRRQVKLLEEKNTMYMQNT---------VSLEEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKL 392
Cdd:TIGR02168 912 ELRRELEELREKLAQLELRLEGLEVRIDNLqerlseeysLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAA 991
|
250 260 270
....*....|....*....|....*....|....*
gi 1729156920 393 EFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEEL 427
Cdd:TIGR02168 992 IEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
334-428 |
7.53e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.00 E-value: 7.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 334 RRQVKLLEEKNTMYMQNTVSLEEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLK----------EKV 403
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARseerreirkdREI 467
|
90 100
....*....|....*....|....*
gi 1729156920 404 DGLQKEKDRLRTERDSLKETIEELR 428
Cdd:COG2433 468 SRLDREIERLERELEEERERIEELK 492
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
263-428 |
7.58e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.16 E-value: 7.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 263 AAKDDYRIRCEELEKEIAELRQQNEELTT-LAEEAQSLKDEMDVLRHSSDKVAKLESQVESYKK--KLEDLGDL----RR 335
Cdd:PHA02562 213 ENIARKQNKYDELVEEAKTIKAEIEELTDeLLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKviKMYEKGGVcptcTQ 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 336 QVKLLEEKNTMYMQNTVSLEEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRT 415
Cdd:PHA02562 293 QISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQA 372
|
170
....*....|...
gi 1729156920 416 ERDSLKETIEELR 428
Cdd:PHA02562 373 EFVDNAEELAKLQ 385
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
154-425 |
9.12e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.89 E-value: 9.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 154 IQELMSKESPVSVGNDAYVDLDRQLKKTTEELNEALATKE-----------EIAQRCHELDMQVAALQEEKSSLLAENQI 222
Cdd:pfam05557 57 IRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKEsqladarevisCLKNELSELRRQIQRAELELQSTNSELEE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 223 LMERLNQSDS----IEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRI---------RCEELEKEIAELRQQNEEL 289
Cdd:pfam05557 137 LQERLDLLKAkaseAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIvknskselaRIPELEKELERLREHNKHL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 290 TT-------LAEEAQSLKDEMDVLRHSSDKVA-------KLESQVESYKKKLEDLG-------DLRRQVKLLEEKNTMYM 348
Cdd:pfam05557 217 NEnienkllLKEEVEDLKRKLEREEKYREEAAtlelekeKLEQELQSWVKLAQDTGlnlrspeDLSRRIEQLQQREIVLK 296
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1729156920 349 QNTVSLEEELRKAHAARSQLETYKRQVVelqnrlseesKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKETIE 425
Cdd:pfam05557 297 EENSSLTSSARQLEKARRELEQELAQYL----------KKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILE 363
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
260-575 |
1.67e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 45.35 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 260 RLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSLKDEMDVLR---HSSDKVAKLESQVESYKKKLEDLGDLR-- 334
Cdd:pfam02463 146 IIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEelkLQELKLKEQAKKALEYYQLKEKLELEEey 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 335 ----RQVKLLEEKNTMYMQNTVSLEEELRKAhAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEK 410
Cdd:pfam02463 226 llylDYLKLNEERIDLLQELLRDEQEEIESS-KQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 411 DRLRTERDSLKETIEELRCVQAQEGQlttsglmplgSQESSDSLAAEIVTPEIKEKLIRLQHENKMLKLNQEGSDNEKIA 490
Cdd:pfam02463 305 LERRKVDDEEKLKESEKEKKKAEKEL----------KKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEE 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 491 LLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDSVLLKKKLEEHLEKLHEANNEIQRKRAIIE 570
Cdd:pfam02463 375 LLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELE 454
|
....*
gi 1729156920 571 DLEPR 575
Cdd:pfam02463 455 KQELK 459
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
183-591 |
2.43e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 183 EELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDPNSPAGRRHlqlqtqleqlqeetfRLE 262
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELE---------------ALE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 263 AAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSLKDEMDVL--RHSSDKVAKLESQVESYKKKLEDLGDLRRQVKLL 340
Cdd:COG4717 139 AELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELleQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 341 EEKNTMYMQNTVSLEEELRKAHAARsQLETYKRQ------VVELQNRLSEESKKADK-------------LEFEYKLLKE 401
Cdd:COG4717 219 QEELEELEEELEQLENELEAAALEE-RLKEARLLlliaaaLLALLGLGGSLLSLILTiagvlflvlgllaLLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 402 KVDGLQKEKDRLRTERDSLKET-IEELRCVQAQEGQLTTSGLMPLGSQ-ESSDSLAAEIVTPEIKEKLIRLQHENKMLkL 479
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEeLEELLAALGLPPDLSPEELLELLDRiEELQELLREAEELEEELQLEELEQEIAAL-L 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 480 NQEGSDNEKIalLQSLLDDANlRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDSvLLKKKLEEHLEKLHEAN 559
Cdd:COG4717 377 AEAGVEDEEE--LRAALEQAE-EYQELKEELEELEEQLEELLGELEELLEALDEEELEEELE-ELEEELEELEEELEELR 452
|
410 420 430
....*....|....*....|....*....|....
gi 1729156920 560 NEIQRKRAIIEDLEP--RYNNSSLKIEELQEALR 591
Cdd:COG4717 453 EELAELEAELEQLEEdgELAELLQELEELKAELR 486
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
260-531 |
2.77e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.44 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 260 RLEAAKDDYRIRCEELEKEIAELRQQ-NEELTTLAEEAQSLKDEMDVLrhSSDKVAKLESQVESYKKKLEDLGDLRRQVK 338
Cdd:pfam12128 280 ERQETSAELNQLLRTLDDQWKEKRDElNGELSAADAAVAKDRSELEAL--EDQHGAFLDADIETAAADQEQLPSWQSELE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 339 LLEEKNTMYMQNTVSLEEELRKAHAARSQleTYKRQVVELQNRLSEESKKADKLefeyklLKEKVDGLQKEKDRLRTERD 418
Cdd:pfam12128 358 NLEERLKALTGKHQDVTAKYNRRRSKIKE--QNNRDIAGIKDKLAKIREARDRQ------LAVAEDDLQALESELREQLE 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 419 SLKETIEElrcvqAQEGQLTTSGlmplgsqESSDSLAAEIVTPEIKEKLIRLQHENKMLKLNQEGSdNEKIALLQSLLDD 498
Cdd:pfam12128 430 AGKLEFNE-----EEYRLKSRLG-------ELKLRLNQATATPELLLQLENFDERIERAREEQEAA-NAEVERLQSELRQ 496
|
250 260 270
....*....|....*....|....*....|...
gi 1729156920 499 ANLRKNELETENRLVNQRLLEVQSQVEELQKSL 531
Cdd:pfam12128 497 ARKRRDQASEALRQASRRLEERQSALDELELQL 529
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
487-636 |
3.29e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 487 EKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDSvlLKKKLEEHLEKLHEANNEIQRKR 566
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ--LEREIERLERELEERERRRARLE 365
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 567 AIIEDLEPRYNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGTApEIQALKNQ 636
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA-EIASLERR 434
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
364-641 |
3.40e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 364 ARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDsLKETIEELRCVQAQEGQLTtsglm 443
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID-VASAEREIAELEAELERLD----- 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 444 plgsqESSDSLAaeivtpEIKEKLIRLQHEnkmlklnqegsdnekiallqslLDDANLRKNELETENRLVNQRLLEVQSQ 523
Cdd:COG4913 682 -----ASSDDLA------ALEEQLEELEAE----------------------LEELEEELDELKGEIGRLEKELEQAEEE 728
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 524 VEELQKSLQEQGSKAEdsVLLKKKLEEHLEKLHEANNEiqrkRAIIEDLEPRYNNSSLKIEELQEALRKKEeemkqmeer 603
Cdd:COG4913 729 LDELQDRLEAAEDLAR--LELRALLEERFAAALGDAVE----RELRENLEERIDALRARLNRAEEELERAM--------- 793
|
250 260 270
....*....|....*....|....*....|....*...
gi 1729156920 604 yKKYLEKAKSVIRTLDPkqNQGTAPEIQALKNQLQERD 641
Cdd:COG4913 794 -RAFNREWPAETADLDA--DLESLPEYLALLDRLEEDG 828
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
351-591 |
3.47e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 351 TVSLEEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTE----RDSLKETIEE 426
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKvkelKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 427 LRCVQAQEGQLTTSGLMPLGSQESSDSLAAEIvtpeikEKLIRlQHENKMLKLNQEGSDNEKIALLQSLLDDAnLRKNEL 506
Cdd:COG1340 87 LNELREELDELRKELAELNKAGGSIDKLRKEI------ERLEW-RQQTEVLSPEEEKELVEKIKELEKELEKA-KKALEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 507 ETENRLVNQRLLEVQSQVEELQKSLQE---QGSKAEDSVL-LKKKLEEHLEKLHEANNEIQRKRAIIEDLEPRYNNSSLK 582
Cdd:COG1340 159 NEKLKELRAELKELRKEAEEIHKKIKElaeEAQELHEEMIeLYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKE 238
|
....*....
gi 1729156920 583 IEELQEALR 591
Cdd:COG1340 239 LRELRKELK 247
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
262-663 |
4.49e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 262 EAAKDDYRIRCEELEKEiAELRQQNEELTTLAEEAQSLKDEMDVLRHSSDKVAKL-ESQVESYKKKLEDLGDLRRQVKLL 340
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKK-AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAaKAEAEAAADEAEAAEEKAEAAEKK 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 341 EEKNTMYMQNTVSLEEELRKAHAARSQLETYKRQVVELQNRlSEESKKADKLEFEYKLlKEKVDGLQKEKDRLRtERDSL 420
Cdd:PTZ00121 1373 KEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKA-AAAKKKADEAKKKAEE-KKKADEAKKKAEEAK-KADEA 1449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 421 KETIEELRCVQ-----AQEGQLTTSglMPLGSQESSDSLAAEIVTPEIKEKLIRLQHENKMLKLNQEGSDNEKIALLQSL 495
Cdd:PTZ00121 1450 KKKAEEAKKAEeakkkAEEAKKADE--AKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEA 1527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 496 LDDANLRKNE----LETENRLVNQRLLEVQSQVEELQKSlqEQGSKAEDSVLLKKKLEEHLEKLHEANNEIQRKRAIIED 571
Cdd:PTZ00121 1528 KKAEEAKKADeakkAEEKKKADELKKAEELKKAEEKKKA--EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK 1605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 572 LEP-----RYNNSSLKIEELQEAlrkkeEEMKQMEERYKKYLEKAKSVIRTLDpKQNQGTAPEIQALKNQLQERDRMFHS 646
Cdd:PTZ00121 1606 KMKaeeakKAEEAKIKAEELKKA-----EEEKKKVEQLKKKEAEEKKKAEELK-KAEEENKIKAAEEAKKAEEDKKKAEE 1679
|
410
....*....|....*..
gi 1729156920 647 LEKEYEKTKTQREMEEK 663
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKK 1696
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
182-441 |
5.60e-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: 42.83 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 182 TEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQsdsiedpnspagrrhlqlqtqleqlqeetfrL 261
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA-------------------------------L 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 262 EAAKDDYRIRCEELEKEIAELRQQNEELTT-LAEEAQSLKDEMDVL-RHSSDKVAKLESQVESYKKKLEDLGDLRRQVKL 339
Cdd:COG4942 68 ARRIRALEQELAALEAELAELEKEIAELRAeLEAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 340 LEEKNTMYMQNTVSLEEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKLEfeyKLLKEKVDGLQKEKDRLRTERDS 419
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLL---ARLEKELAELAAELAELQQEAEE 224
|
250 260
....*....|....*....|..
gi 1729156920 420 LKETIEELRCVQAQEGQLTTSG 441
Cdd:COG4942 225 LEALIARLEAEAAAAAERTPAA 246
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
284-590 |
5.98e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 43.35 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 284 QQNEELTTLAEEAQ----SLKDEMDVLRHSSDKVAKLESQ----VESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSLE 355
Cdd:PLN02939 111 IDNEQQTNSKDGEQlsdfQLEDLVGMIQNAEKNILLLNQArlqaLEDLEKILTEKEALQGKINILEMRLSETDARIKLAA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 356 EELRKAHAARSQLETYKRqvvELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEELRCVQAQEG 435
Cdd:PLN02939 191 QEKIHVEILEEQLEKLRN---ELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFKLEKERS 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 436 QLTTSglmpLGSQESSDSLAAEIVTpeikeKLIRLQHENKMlklnqegsdnEKIALLQSLLDDAnlrKNELEtENRLVNQ 515
Cdd:PLN02939 268 LLDAS----LRELESKFIVAQEDVS-----KLSPLQYDCWW----------EKVENLQDLLDRA---TNQVE-KAALVLD 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 516 RLLEVQSQVEELQKSLQEQGSKAEDSVLLK------KKLEEHLEKL-HEANNEIQRKRAIIEDLEPryNNSSLKIEELQE 588
Cdd:PLN02939 325 QNQDLRDKVDKLEASLKEANVSKFSSYKVEllqqklKLLEERLQASdHEIHSYIQLYQESIKEFQD--TLSKLKEESKKR 402
|
..
gi 1729156920 589 AL 590
Cdd:PLN02939 403 SL 404
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
262-411 |
9.37e-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: 42.80 E-value: 9.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 262 EAAKDDYRIRCEELEK--EIAELRQQNEELTTLAEEAQSLKDEMDVLRHSSDKVakLESQVESYKKKLEdlgDLRRQVKL 339
Cdd:pfam17380 443 ERAREMERVRLEEQERqqQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKI--LEKELEERKQAMI---EEERKRKL 517
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1729156920 340 LeEKNTMYMQNTVSLEEELRKAHAA-RSQLETYKRQVVELQNRL-SEESKKADKLEFEYKLLKEKVDGLQKEKD 411
Cdd:pfam17380 518 L-EKEMEERQKAIYEEERRREAEEErRKQQEMEERRRIQEQMRKaTEERSRLEAMEREREMMRQIVESEKARAE 590
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
273-428 |
1.07e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 273 EELEKEIAELRQQNEELTTLAEEAQ--SLKDEMDVLRH-----SSDKVAKLESQVESYKKKLEDLGDLRRQVKLL--EEK 343
Cdd:COG4717 340 LELLDRIEELQELLREAEELEEELQleELEQEIAALLAeagveDEEELRAALEQAEEYQELKEELEELEEQLEELlgELE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 344 NTMYMQNTVSLEEEL----RKAHAARSQLETYKRQVVELQNRLS--EESKKADKLEFEYKLLKEKVDGLQKEKDRLRTER 417
Cdd:COG4717 420 ELLEALDEEELEEELeeleEELEELEEELEELREELAELEAELEqlEEDGELAELLQELEELKAELRELAEEWAALKLAL 499
|
170
....*....|.
gi 1729156920 418 DSLKETIEELR 428
Cdd:COG4717 500 ELLEEAREEYR 510
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
156-570 |
1.13e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 156 ELMSKESPVSVGNDAYVDLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALqEEKSSLLAENQILMERLNQSDSIED 235
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEL-EERHELYEEAKAKKEELERLKKRLT 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 236 PNSPagrrhlqlqtqlEQLQEETFRLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSLK-------------DE 302
Cdd:PRK03918 383 GLTP------------EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgrelteeHR 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 303 MDVLRHSSDKVAKLESQVESYKKKLEDL-GDLRRQVKLLEEKNTMYMQNTV-----SLEEELR-----KAHAARSQLETY 371
Cdd:PRK03918 451 KELLEEYTAELKRIEKELKEIEEKERKLrKELRELEKVLKKESELIKLKELaeqlkELEEKLKkynleELEKKAEEYEKL 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 372 KRQVVEL---QNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTE--------RDSLKETIEELRCVQAQEGQLTTS 440
Cdd:PRK03918 531 KEKLIKLkgeIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEleelgfesVEELEERLKELEPFYNEYLELKDA 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 441 GLMPLGSQESSDSLAAEIVtpEIKEKLIRLQHENKMLKlnqegsdnEKIALLQSLLDD---ANLRKNELETENRL--VNQ 515
Cdd:PRK03918 611 EKELEREEKELKKLEEELD--KAFEELAETEKRLEELR--------KELEELEKKYSEeeyEELREEYLELSRELagLRA 680
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1729156920 516 RLLEVQSQVEELQKS---LQEQGSKAEDSVLLKKKLEEHLEKLHEANNEIQRKRAIIE 570
Cdd:PRK03918 681 ELEELEKRREEIKKTlekLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLK 738
|
|
| DUF2046 |
pfam09755 |
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ... |
261-404 |
1.20e-03 |
|
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues of a family of proteins of unknown function possibly containing a coiled-coil domain.
Pssm-ID: 401633 [Multi-domain] Cd Length: 304 Bit Score: 41.74 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 261 LEAAKDDYRIRCEELEKEIAELRQ----------QNEEL--TTLAEEAQSLKDEMDVLRHSSDKvaKLESQVESYKKKLE 328
Cdd:pfam09755 40 LKMELETYKLRCKALQEENRALRQasvniqakaeQEEEFisNTLLKKIQALKKEKETLAMNYEQ--EEEFLTNDLSRKLT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 329 DLGDLRRQVKLLEEKNTMYMQNTVSLEEELRKA--HAARSQLETYKRQVVELQNRLSEES--------KKADKLEFEYKL 398
Cdd:pfam09755 118 QLRQEKVELEQTLEQEQEYQVNKLMRKIEKLEAetLNKQTNLEQLRREKVELENTLEQEQealvnrlwKRMDKLEAEKRL 197
|
....*.
gi 1729156920 399 LKEKVD 404
Cdd:pfam09755 198 LQEKLD 203
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
265-427 |
1.33e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 265 KDDYRIRCEELEKEIAELRQQ----NEELTTLAEEAQSLKDEMDVLRhssDKVAKLESQVESYKKKLEDLGDLRRQVKLL 340
Cdd:COG1340 45 RDELNAQVKELREEAQELREKrdelNEKVKELKEERDELNEKLNELR---EELDELRKELAELNKAGGSIDKLRKEIERL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 341 EEKntmyMQNTV-SLEEE---------LRKAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEK 410
Cdd:COG1340 122 EWR----QQTEVlSPEEEkelvekikeLEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEM 197
|
170
....*....|....*..
gi 1729156920 411 DRLRTERDSLKETIEEL 427
Cdd:COG1340 198 IELYKEADELRKEADEL 214
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
169-668 |
1.52e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 169 DAYVDLDRQLKKTTEELnEALATKEEIAQRCHELDMQVAALQEEKSSLLAENqilmerlnqsdsiedpnspAGRRHLQLQ 248
Cdd:COG4913 235 DDLERAHEALEDAREQI-ELLEPIRELAERYAAARERLAELEYLRAALRLWF-------------------AQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 249 TQLEQLQEETFRLEAAKDDYRIRCEELEKEIAELRQQ-----NEELTTLAEEAQSLKDEMDVLRHSSDKVAKLESQVE-S 322
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQirgngGDRLEQLEREIERLERELEERERRRARLEALLAALGlP 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 323 YKKKLEDLGDLRRQVK-LLEEKNTMYMQntvsLEEELRKAHAARSQLE------------------TYKRQVVELQNRLS 383
Cdd:COG4913 375 LPASAEEFAALRAEAAaLLEALEEELEA----LEEALAEAEAALRDLRrelreleaeiaslerrksNIPARLLALRDALA 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 384 EE-SKKADKLEF------------------E----------------YKLLKEKVDGLQKEKdRLRTERdsLKETIEELR 428
Cdd:COG4913 451 EAlGLDEAELPFvgelievrpeeerwrgaiErvlggfaltllvppehYAAALRWVNRLHLRG-RLVYER--VRTGLPDPE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 429 CVQAQEGQLttSGLMPLGSQESSDSLAAEI---------------------VTPE--IKEKLIRLQH--ENKMLKLNQEG 483
Cdd:COG4913 528 RPRLDPDSL--AGKLDFKPHPFRAWLEAELgrrfdyvcvdspeelrrhpraITRAgqVKGNGTRHEKddRRRIRSRYVLG 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 484 SDN-EKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKsLQEQGSKAEDSVLLKKK---LEEHLEKLHEAN 559
Cdd:COG4913 606 FDNrAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQR-LAEYSWDEIDVASAEREiaeLEAELERLDASS 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 560 NEIQRKRAIIEDLEprynnssLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGTAPEIQALKNQLQE 639
Cdd:COG4913 685 DDLAALEEQLEELE-------AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAA 757
|
570 580 590
....*....|....*....|....*....|....*
gi 1729156920 640 ------RDRMFHSLEKEYEKTKTQREMEEKFIVSA 668
Cdd:COG4913 758 algdavERELRENLEERIDALRARLNRAEEELERA 792
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
275-427 |
1.78e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.77 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 275 LEKEIAELRQQNEELTTLAEEAQS--LKDEMDVLRHSSDKVAKLESQVEsykkkledlgDLRRQVKLLEEKNTMymqntv 352
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEEreLTEEEEEIRRLEEQVERLEAEVE----------ELEAELEEKDERIER------ 445
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1729156920 353 sLEEELRKahaARSQletykrqvvelQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEEL 427
Cdd:COG2433 446 -LERELSE---ARSE-----------ERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLE 505
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
273-615 |
1.93e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.88 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 273 EELEKEIAELRQQNEELTTLAEEAQSLKDEMDVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTV 352
Cdd:pfam02463 657 GLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINE 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 353 SLEEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEELRCVQA 432
Cdd:pfam02463 737 ELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAEL 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 433 QEGQLTTSGLMPLGSQESSDSLAAEIVTPEIKEKLIRLQHENKMLKLNQEGSDNEKIALLQSLLDDANLRKNEL--ETEN 510
Cdd:pfam02463 817 LEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESkeEKEK 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 511 RLVNQRLLEVQSQVEELQKSLQEQGSKAEDSVLLKKKLEEHLEKLHEANNEIQRKRAIIEDLEPRYNNSSLKIEELQEAL 590
Cdd:pfam02463 897 EEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVN 976
|
330 340
....*....|....*....|....*
gi 1729156920 591 RKKEEEMKQMEERYKKYLEKAKSVI 615
Cdd:pfam02463 977 LMAIEEFEEKEERYNKDELEKERLE 1001
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
174-409 |
1.99e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.81 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 174 LDRQLKKTTEELNEALATKEEIAqrcHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDpnspagrrhlqlqtqleq 253
Cdd:PLN02939 199 LEEQLEKLRNELLIRGATEGLCV---HSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEE------------------ 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 254 lqeETFRLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAqsLKDEMDVLRHSSDKVAKlesQVESYKKKLEDLGDL 333
Cdd:PLN02939 258 ---RVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLQYDC--WWEKVENLQDLLDRATN---QVEKAALVLDQNQDL 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 334 RRQVKLLEE--------KNTMY----MQNTV-SLEEELRKAHAA-RSQLETYKRQVVELQ---NRLSEESKKadklefey 396
Cdd:PLN02939 330 RDKVDKLEAslkeanvsKFSSYkvelLQQKLkLLEERLQASDHEiHSYIQLYQESIKEFQdtlSKLKEESKK-------- 401
|
250
....*....|...
gi 1729156920 397 KLLKEKVDGLQKE 409
Cdd:PLN02939 402 RSLEHPADDMPSE 414
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
139-665 |
1.99e-03 |
|
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: 41.59 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 139 IMMMEESVQHVVMTAIQELMSK----ESPVSVGNDAYVDLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKS 214
Cdd:TIGR02169 281 IKDLGEEEQLRVKEKIGELEAEiaslERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYA 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 215 SLLAENQILMERLNQSDSiedpnsPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAE 294
Cdd:TIGR02169 361 ELKEELEDLRAELEEVDK------EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEA 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 295 EAQSLKDEMDVLRhssDKVAKLESQVESYKkklEDLGDLRRQVKLLEEKNTMYMQNTVSLEEELRKAHAARSQLETYKRQ 374
Cdd:TIGR02169 435 KINELEEEKEDKA---LEIKKQEWKLEQLA---ADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 375 vvelqNRLSEESKKAD------------KLEFEYKLLKEKVDGLQKEKDRLRTERDSlKETIEELRCVQAqeGQLTTSGL 442
Cdd:TIGR02169 509 -----GRAVEEVLKASiqgvhgtvaqlgSVGERYATAIEVAAGNRLNNVVVEDDAVA-KEAIELLKRRKA--GRATFLPL 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 443 MPLGSQESSDSLAAEIVTPEIKEKLI---------------------------RLQHENKMLKLNQE----------GSD 485
Cdd:TIGR02169 581 NKMRDERRDLSILSEDGVIGFAVDLVefdpkyepafkyvfgdtlvvedieaarRLMGKYRMVTLEGElfeksgamtgGSR 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 486 NEKIALLQSLLDDANL-----RKNELETENRLVNQRLLEVQSQVEELQKSLQEqgskaedsvlLKKKLEEHLEKLHEANN 560
Cdd:TIGR02169 661 APRGGILFSRSEPAELqrlreRLEGLKRELSSLQSELRRIENRLDELSQELSD----------ASRKIGEIEKEIEQLEQ 730
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 561 EIQRKRAIIEDLEPRYNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGTAPEIQALKNQLQER 640
Cdd:TIGR02169 731 EEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRI 810
|
570 580
....*....|....*....|....*
gi 1729156920 641 DRMFHSLEKEYEKTKTQREMEEKFI 665
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEI 835
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
261-575 |
2.11e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.35 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 261 LEAAKDDYRIRCEE----LEKEIAELRQQNEELTTLAEEAQSLKDEMDVlrhSSDKVAKLESQVESYKKKLED----LGD 332
Cdd:pfam10174 343 LQTEVDALRLRLEEkesfLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDV---KERKINVLQKKIENLQEQLRDkdkqLAG 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 333 LRRQVKLLEEKNTMYMQNTVSLEEEL----RKAHAARSQLETYKRQVVELqnrlSEESKKadklefEYKLLKEKVDGLQK 408
Cdd:pfam10174 420 LKERVKSLQTDSSNTDTALTTLEEALsekeRIIERLKEQREREDRERLEE----LESLKK------ENKDLKEKVSALQP 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 409 EKdrlrTERDSLKETIEELRCVQAQEGQLTTSGLMPLgsqessdslaaEIVTPEIKEKLIRLQHEnkmLKLNQEGSDNEK 488
Cdd:pfam10174 490 EL----TEKESSLIDLKEHASSLASSGLKKDSKLKSL-----------EIAVEQKKEECSKLENQ---LKKAHNAEEAVR 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 489 IAllqsllDDANLRKNELETEnrlvnqrlleVQSQVEELQKSLQEqgskaedsvllkkkLEEHLEKLHEANNEIQRKRAI 568
Cdd:pfam10174 552 TN------PEINDRIRLLEQE----------VARYKEESGKAQAE--------------VERLLGILREVENEKNDKDKK 601
|
....*..
gi 1729156920 569 IEDLEPR 575
Cdd:pfam10174 602 IAELESL 608
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
275-665 |
2.18e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.54 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 275 LEKEIAELRQQNEELTTLAEEAQSLKDEMDVLRHSSDKVAKLESQVESYKKKLEDL--------GDLRRQVKLLEEKNTM 346
Cdd:TIGR04523 98 INKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKEleklnnkyNDLKKQKEELENELNL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 347 YMQNTVSLEEELRKAHAARSQLETykrqvveLQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDrlrTERDSLKETIEE 426
Cdd:TIGR04523 178 LEKEKLNIQKNIDKIKNKLLKLEL-------LLSNLKKKIQKNKSLESQISELKKQNNQLKDNIE---KKQQEINEKTTE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 427 LRCVQAQEGQLTTSgLMPLGSQESSDSLAAEIVTPEIKEKLIRLQH-ENKMLKLNQEgSDNEKIALLQSLLDDANLRKNE 505
Cdd:TIGR04523 248 ISNTQTQLNQLKDE-QNKIKKQLSEKQKELEQNNKKIKELEKQLNQlKSEISDLNNQ-KEQDWNKELKSELKNQEKKLEE 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 506 LETENRLVNQRLLEVQSQVEELQKSLQEQGSkaeDSVLLKKKLEEHLEKLHEANNEIQRKRAIIEDLEPRYNNSSLKIEE 585
Cdd:TIGR04523 326 IQNQISQNNKIISQLNEQISQLKKELTNSES---ENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQN 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 586 LQEALRKKEEEMKQMEERYKKyLEKAKSVIRTLDPKQNQgtapEIQALKNQLqerdrmfHSLEKEYEKTKTQREMEEKFI 665
Cdd:TIGR04523 403 QEKLNQQKDEQIKKLQQEKEL-LEKEIERLKETIIKNNS----EIKDLTNQD-------SVKELIIKNLDNTRESLETQL 470
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
273-557 |
2.60e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 273 EELEKEIAELRQQNEELttlAEEAQSLKDEMDVLRhssDKVAKLESQVESYKKKLEDLGDLRRQVKLLEEKNTmymqntv 352
Cdd:TIGR04523 422 ELLEKEIERLKETIIKN---NSEIKDLTNQDSVKE---LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQ------- 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 353 sleeelrkahaarSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEELrcvqa 432
Cdd:TIGR04523 489 -------------KELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKD----- 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 433 qEGQLTTSGLmplgsqessdslaaEIVTPEIKEKLIRLQHENKMLKLNQEGsdnekialLQSLLDdanlrknELETENRL 512
Cdd:TIGR04523 551 -DFELKKENL--------------EKEIDEKNKEIEELKQTQKSLKKKQEE--------KQELID-------QKEKEKKD 600
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1729156920 513 VNQRLLEVQSQVEELQKSLQEQGSKAEDSVLLKKKLEEHLEKLHE 557
Cdd:TIGR04523 601 LIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQ 645
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
266-376 |
2.61e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 266 DDYRIRCEELEKEIAELRQQNEELTtlAEEAQSLKDEMDVLRhssDKVAKLESQVESYKKKLEDLGDLRRQvklLEEKNt 345
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEQDEAS--FERLAELRDELAELE---EELEALKARWEAEKELIEEIQELKEE---LEQRY- 484
|
90 100 110
....*....|....*....|....*....|.
gi 1729156920 346 mymQNTVSLEEELRKAHAARSQLETYKRQVV 376
Cdd:COG0542 485 ---GKIPELEKELAELEEELAELAPLLREEV 512
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
175-411 |
3.23e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 175 DRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSiedpnspagrrhlqlqtqleql 254
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA---------------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 255 qeetfRLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAE--EAQSLKDEMDvlrhssdKVAKLESQVESYKKKLEDLGD 332
Cdd:COG3883 73 -----EIAEAEAEIEERREELGERARALYRSGGSVSYLDVllGSESFSDFLD-------RLSALSKIADADADLLEELKA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1729156920 333 LRRQVKLLEEKntmymqntvsLEEELRKAHAARSQLETYKRqvvELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKD 411
Cdd:COG3883 141 DKAELEAKKAE----------LEAKLAELEALKAELEAAKA---ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
360-659 |
5.56e-03 |
|
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: 40.10 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 360 KAHAARSqLETYKRQVVELQNRLSEESKKADKLEFEYKL----LKEKVDGLQKEKDRL----RTE-------RDSLKETI 424
Cdd:pfam15921 73 KEHIERV-LEEYSHQVKDLQRRLNESNELHEKQKFYLRQsvidLQTKLQEMQMERDAMadirRREsqsqedlRNQLQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 425 EELRCVQA-QEGQLTTSGLMPlgSQESSDSLAAEIVTPEIKEKLIRLQhENKMLKLNQEgsDNEKIALLQSLLDDANLRK 503
Cdd:pfam15921 152 HELEAAKClKEDMLEDSNTQI--EQLRKMMLSHEGVLQEIRSILVDFE-EASGKKIYEH--DSMSTMHFRSLGSAISKIL 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 504 NELETENRLVNQRLLEVQSQVEELQkslQEQGSKAEdsvLLKKKLEEHLEKL---HEAN---------------NEIQRK 565
Cdd:pfam15921 227 RELDTEISYLKGRIFPVEDQLEALK---SESQNKIE---LLLQQHQDRIEQLiseHEVEitgltekassarsqaNSIQSQ 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 566 RAIIEDLEPRYNNSSLK--------IEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQgTAPEIQALKNQL 637
Cdd:pfam15921 301 LEIIQEQARNQNSMYMRqlsdlestVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQ-FSQESGNLDDQL 379
|
330 340
....*....|....*....|..
gi 1729156920 638 QERDRMFHSLEKEYEKTKTQRE 659
Cdd:pfam15921 380 QKLLADLHKREKELSLEKEQNK 401
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
273-457 |
5.93e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 273 EELEKEIAELRQQNEELTTLAEEAQSLKDEMDVLRhssDKVAKLESQVESYKKKLEdlgdlRRQVKLLEEKNTMYMQNTV 352
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQAELEALQ---AEIDKLQAEIAEAEAEIE-----ERREELGERARALYRSGGS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 353 -----------SLEEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLK 421
Cdd:COG3883 102 vsyldvllgseSFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQE 181
|
170 180 190
....*....|....*....|....*....|....*.
gi 1729156920 422 ETIEELRCVQAQEGQLTTSGLMPLGSQESSDSLAAE 457
Cdd:COG3883 182 ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
273-422 |
6.15e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 6.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 273 EELEKEIAELRQQNEELTTLA-------EEAQSLKDEMDVLRHSSDKVAKLESQVESYKKKLEDLgdlrrQVKLLEEKNT 345
Cdd:PRK03918 588 EELEERLKELEPFYNEYLELKdaekeleREEKELKKLEEELDKAFEELAETEKRLEELRKELEEL-----EKKYSEEEYE 662
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1729156920 346 MYMQNTVSLEEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKE 422
Cdd:PRK03918 663 ELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKE 739
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
492-590 |
6.27e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.28 E-value: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 492 LQSLLDDANLRKnELETENRLVNQRLLEVQSQVEELQKSLQeqgskaeDSVLLKKKLEEHLEKLHEANNEIQR-KRAIIE 570
Cdd:PRK11281 41 VQAQLDALNKQK-LLEAEDKLVQQDLEQTLALLDKIDRQKE-------ETEQLKQQLAQAPAKLRQAQAELEAlKDDNDE 112
|
90 100
....*....|....*....|
gi 1729156920 571 DLEPRYNNSSLKieELQEAL 590
Cdd:PRK11281 113 ETRETLSTLSLR--QLESRL 130
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
263-553 |
6.83e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.89 E-value: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 263 AAKDDYRIRCEELEKEIA----ELRQQNEELTTLAEEAQSLKDEmdvlRHSSDKVAKLESQVEsykKKLEDLGDLrrqvk 338
Cdd:PRK11281 73 DKIDRQKEETEQLKQQLAqapaKLRQAQAELEALKDDNDEETRE----TLSTLSLRQLESRLA---QTLDQLQNA----- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 339 lleekntmymQNTVSleeelrkahAARSQLETYKRQVVELQNRLSEESKKadklefeykllkekvdgLQKEKDRLRTERD 418
Cdd:PRK11281 141 ----------QNDLA---------EYNSQLVSLQTQPERAQAALYANSQR-----------------LQQIRNLLKGGKV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 419 SLKETIEELRcvqaqegqlttsglmplgsqessDSLAAEIVtpeikekLIRLQheNKMLKLNQEGSdNEKIALLQSLLDD 498
Cdd:PRK11281 185 GGKALRPSQR-----------------------VLLQAEQA-------LLNAQ--NDLQRKSLEGN-TQLQDLLQKQRDY 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 499 ANLRKNELETENRL----VNQ-RLLEVQSQVEELQKslQEQGSKAEDSVLLKKKLEEHLE 553
Cdd:PRK11281 232 LTARIQRLEHQLQLlqeaINSkRLTLSEKTVQEAQS--QDEAARIQANPLVAQELEINLQ 289
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
457-588 |
7.13e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.91 E-value: 7.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156920 457 EIVTP-EIKEKLIRLQHENKMLKLN--QEGSDNEKIALLQSLLDDANLRKNELET---ENRLVNQRLLEVQSQ-VEELQK 529
Cdd:PRK05771 10 LIVTLkSYKDEVLEALHELGVVHIEdlKEELSNERLRKLRSLLTKLSEALDKLRSylpKLNPLREEKKKVSVKsLEELIK 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1729156920 530 SLQEQGSKAEDSVllkkklEEHLEKLHEANNEIQRKRAIIEDLEPrYNNSSLKIEELQE 588
Cdd:PRK05771 90 DVEEELEKIEKEI------KELEEEISELENEIKELEQEIERLEP-WGNFDLDLSLLLG 141
|
|
| |
