|
Name |
Accession |
Description |
Interval |
E-value |
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
184-710 |
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: 682.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 184 ELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQEETFRLEA 263
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 264 AKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSLKDEMDVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQVKLLEEK 343
Cdd:pfam05622 81 ARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLGDLRRQVKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 344 NTMYMQNTVSLEEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKET 423
Cdd:pfam05622 161 NAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRET 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 424 IEELRCVQAQEGQLtTSAGLMPLGSQESSDSLAAEIVTPEIKEKLIRLQHENKMLKLNQEGSDNEKIALLQSLLDDANLR 503
Cdd:pfam05622 241 NEELRCAQLQQAEL-SQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLGQEGSYRERLTELQQLLEDANRR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 504 KNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDSVLLKKKLEEHLEKLHEANNEIQRKRAIIEDLEPRYN-NSSL 582
Cdd:pfam05622 320 KNELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDsNLAQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 583 KIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGTAPEIQALKNQLQERDRMFHSLEKEYEKTKTQREME 662
Cdd:pfam05622 400 KIDELQEALRKKDEDMKAMEERYKKYVEKAKSVIKTLDPKQNPASPPEIQALKNQLLEKDKKIEHLERDFEKSKLQREQE 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1729156918 663 EKFIVSAWYNMGMTLHKKAAEDRLASTGS-GQSFLARQRQATNTRRSYP 710
Cdd:pfam05622 480 EKLIVTAWYNMGMALHRKAIEERLAGLSSpGQSFLARQRQATNARRGLS 528
|
|
| HkD_Hook3 |
cd22226 |
Hook domain found in protein Hook 3 (Hook3) and similar proteins; Hook3 is an adaptor protein ... |
8-160 |
4.44e-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: 310.36 E-value: 4.44e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 8 ERAELGESLLTWIQTFNVEAPCQTVEDLTNGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYN 87
Cdd:cd22226 1 DRAELCESLLTWIQTFNVDAPCQTVEDLTSGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1729156918 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 |
2.07e-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: 2.07e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 11 ELGESLLTWIQTFNVEAPCQTVEDLTNGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEI 90
Cdd:pfam19047 1 ELCDSLLTWLQTFNVPAPCATVEDLTDGVAMAQVLHQIDPSWFTEAWLSRIKEDVGDNWRLKVSNLKKILQSVVDYYQDV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1729156918 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 |
5.58e-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: 5.58e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 14 ESLLTWIQTFNVEAPCQTVEDLTNGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEILGQ 93
Cdd:cd22222 2 DSLLQWLQTFNLIAPHATAEDLSDGVAIAQVLNQIDPEYFSDSWLSKIKPDVGDNWRLKVSNLKKILKGIVDYYSEVLGQ 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1729156918 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 |
1.36e-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: 1.36e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 12 LGESLLTWIQTFNVEAPCQTVEDLTNGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEIL 91
Cdd:cd22225 1 LCDSLIIWLQTFNTAAPCQTVQDLTSGVAMAQVLHQIDSSWFDESWLSRIKEDVGDNWRIKMSNLKKILQGIVDYYHEFL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 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 |
1.28e-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: 227.84 E-value: 1.28e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 11 ELGESLLTWIQTFNVEAPCQTVEDLTNGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEI 90
Cdd:cd22227 1 ELCDSLLTWLQTFQVPSPCSSYQDLTSGVAIAQVLNRIDPSWFNEAWLGRIKEDTGDNWRLKVSNLKKILQSLLEYYQDV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 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 |
4.77e-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: 4.77e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 13 GESLLTWIQTFNVEAPCQTVEDLTNGVVMAQVLQKIDPAYFDENWLNriKTEVGDNWRLKISNLKKILKGILDYNHEILG 92
Cdd:cd22211 1 EAALLAWINTFPLSSPVESLDDLSDGVVLAEILSQIDPSYFDSEWLE--SRDSSDNWVLKLNNLKKLYRSLSKYYREVLG 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1729156918 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 |
2.67e-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: 2.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 15 SLLTWIQTFNVEAPCQ-TVEDLTNGVVMAQVLQKIDPAYFDEnwlnRIKTEVGDNWRLKISNLKKILKGILDYNHEILGQ 93
Cdd:cd22223 5 PLVTWAKTFADDGSAElSYTDLVDGVFLNNVMLQIDPRPFSE----VSNRNVDDDVNARIQNLDLLLRNIKSFYQEVLQQ 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1729156918 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 |
2.04e-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: 79.97 E-value: 2.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 12 LGESLLTWIQTFNV-----EAPCQTVEDLTNGVVMAQVLQKIDPAYFDEnwlnRIKTEVGDNWRLKISNLKKILKGILDY 86
Cdd:cd22228 2 LQSPLVTWVKTFGPlgfgsEDKLSMYMDLVDGVFLNKIMLQIDPRPTNQ----RVNKHVNNDVNLRIQNLTILVRHIKTY 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1729156918 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 |
5.64e-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: 5.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 16 LLTWIQTFNVEAPCQTVE-----DLTNGVVMAQVLQKIDPAYFDEnwlnRIKTEVGDNWRLKISNLKKILKGILDYNHEI 90
Cdd:cd22229 9 LVTWVKTFGPLATGNGTPldeyvALVDGVFLNEVMLQINPKSSNQ----RVNKKVNNDASLRIQNLSILVKQIKLYYQET 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1729156918 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 ... |
260-592 |
3.40e-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: 70.09 E-value: 3.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 260 RLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSLKDEMDVLRHSSDK-VAKLESQVESYKKKLEDLGdlrrqvK 338
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdLARLEAEVEQLEERIAQLS------K 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 339 LLEEKNTMYMQNTVSLEEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERD 418
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 419 SLKETIEEL--RCVQAQEGQLTTSAGLMPLGSQESSDSLAAEIVTPEIKE-----KLIRLQHENKMLKLNQEGSDN---- 487
Cdd:TIGR02168 835 ATERRLEDLeeQIEELSEDIESLAAEIEELEELIEELESELEALLNERASleealALLRSELEELSEELRELESKRselr 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 488 EKIALLQSLLDDANLRKNELEtenrlvnQRLLEVQSQV-EELQKSLQEQGSKAEDSVLLKKKLEEHLEKLHEANNEIQR- 565
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLE-------VRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPv 987
|
330 340 350
....*....|....*....|....*....|
gi 1729156918 566 -KRAI--IEDLEPRYNNSSLKIEELQEALR 592
Cdd:TIGR02168 988 nLAAIeeYEELKERYDFLTAQKEDLTEAKE 1017
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
130-665 |
3.12e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.01 E-value: 3.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 130 EQKQEYIQTIMMMEESVQHVVMTAIQELMSKESPVSVGNDAYVDLDRQLKKTTEELNEALATKEEIAqrchELDMQVAAL 209
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIE----ELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 210 QEEKSSLLAENQILMERLNQSDS-IEDPNSPAGR---------RHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEI 279
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKeIEELEEKVKElkelkekaeEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 280 AELRQQNEELTTLAEEAQSLKDEMDVLRHSS---DKVAKLESQVESYKKKLEDL--GDLRRQVKLLEEKNTmymqntvSL 354
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEELEERHelyEEAKAKKEELERLKKRLTGLtpEKLEKELEELEKAKE-------EI 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 355 EEELRKAHAARSQLET----YKRQVVELQ-------------------NRLSEESKKADKLEFEYKLLKEKVDGLQKEKD 411
Cdd:PRK03918 404 EEEISKITARIGELKKeikeLKKAIEELKkakgkcpvcgrelteehrkELLEEYTAELKRIEKELKEIEEKERKLRKELR 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 412 RLRTERD------SLKETIEELRCVQAQegqlttsaglmpLGSQESSDSLAAEIVTPEIKEKLIRLQHENKMLK--LNQE 483
Cdd:PRK03918 484 ELEKVLKkeseliKLKELAEQLKELEEK------------LKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKkeLEKL 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 484 GSDNEKIALLQSLLDDANLRKNELETE-NRLVNQRLLEVQSQVEELQK----------SLQEQGSKAEDSVLLKKKLEEH 552
Cdd:PRK03918 552 EELKKKLAELEKKLDELEEELAELLKElEELGFESVEELEERLKELEPfyneylelkdAEKELEREEKELKKLEEELDKA 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 553 LEKLHEANNEIQRKRAIIEDLEPRYNnsslkiEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLdpkqnqgtAPEIQ 632
Cdd:PRK03918 632 FEELAETEKRLEELRKELEELEKKYS------EEEYEELREEYLELSRELAGLRAELEELEKRREEI--------KKTLE 697
|
570 580 590
....*....|....*....|....*....|...
gi 1729156918 633 ALKNQLQERDRMFHSLEKEYEKTKTQREMEEKF 665
Cdd:PRK03918 698 KLKEELEEREKAKKELEKLEKALERVEELREKV 730
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
176-664 |
1.95e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.31 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 176 RQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQ 255
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 256 EETFRLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQS-------LKDEMDVLRHSSDKVAKLESQVESYKKKLE 328
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiklsefYEEYLDELREIEKRLSRLEEEINGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 329 DLGDLRRQVKLLEEKNTMYMQNTVSLEEELRKAHAARSQLETYKRQVVELQNRLSEE-SKKADKLEFEYKLLKEKVDGLQ 407
Cdd:PRK03918 332 ELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKlEKELEELEKAKEEIEEEISKIT 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 408 KEKDRLRTERDSLKETIEELRC------VQAQEGQLTTSAGLMPLGSQESSDSLAAEIVTPEIKEKL-IRLQHENKMLKL 480
Cdd:PRK03918 412 ARIGELKKEIKELKKAIEELKKakgkcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLrKELRELEKVLKK 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 481 NQEGSDNEKIA----LLQSLLDDANLRKNELETEN-RLVNQRLLEVQSQVEELQKSLQEQGSKAEDSVLLKKKLEEHLEK 555
Cdd:PRK03918 492 ESELIKLKELAeqlkELEEKLKKYNLEELEKKAEEyEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEE 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 556 LHEANNEIQRK--------RAIIEDLEPRYN------NSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDP 621
Cdd:PRK03918 572 LAELLKELEELgfesveelEERLKELEPFYNeylelkDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE 651
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1729156918 622 KQNQGTAPEIQALKNQLQERDRMFHSLEKEYEKTKTQREMEEK 664
Cdd:PRK03918 652 LEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKK 694
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
355-660 |
2.59e-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: 64.31 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 355 EEELRKAHAARSQLETYKRQVVEL---QNRLSEESKKADKlefeYKLLKEKVDGLQK-----EKDRLRTERDSLKETIEE 426
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELerqLKSLERQAEKAER----YKELKAELRELELallvlRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 427 LrcvqaqegqlttsaglmplgsQESSDSLAAEIVTPEIKEKLIRLQHenkmlklnqeGSDNEKIALLQSLLDDANLRKNE 506
Cdd:TIGR02168 251 A---------------------EEELEELTAELQELEEKLEELRLEV----------SELEEEIEELQKELYALANEISR 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 507 LETENRLVNQRLLEVQSQVEELQKSLQEQGSK----AEDSVLLKKKLEEHLEKLHEANNEIQRKRAIIEDLEPRYNNSSL 582
Cdd:TIGR02168 300 LEQQKQILRERLANLERQLEELEAQLEELESKldelAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1729156918 583 KIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGTAPEIQALKNQLQERDRMFHSLEKEYEKTKTQRE 660
Cdd:TIGR02168 380 QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE 457
|
|
| HkD_Gipie |
cd22230 |
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar ... |
12-157 |
5.63e-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: 5.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 12 LGESLLTWIQTF-------------NVEAPCQTVED-------LTNGVVMAQVLQKIDPAYFDENWLNRikteVGDNWRL 71
Cdd:cd22230 4 MSGALVTWALGFeglvgeeedslgfPEEEEEEGTLDaekrflrLSNGDLLNRVMGIIDPSPRGGPRMRG----DDGPAAH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 72 KISNLKKILKGILDYNHEILgQQINDFTLPDVNLIGEH----SDVAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQ 147
Cdd:cd22230 80 RVQNLHILWGRLRDFYQEEL-QQLILSPPPDLQVMGRDpfteEAVQELEKLLRLLLGAAVQCERRELFIRHIQGLDLDVQ 158
|
170
....*....|
gi 1729156918 148 HVVMTAIQEL 157
Cdd:cd22230 159 AELAEAIQEV 168
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
283-592 |
1.71e-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: 61.62 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 283 RQQNEELTTLAEEAQSLKDEMDVLRhssDKVAKLESQVESYKKKLED----LGDLRRQVKLLEEKNTMYMQNTVSLEEEL 358
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQ---SELRRIENRLDELSQELSDasrkIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 359 ----RKAHAARSQLETYKRQVVELQNRLSEESKKADKLEfeYKLLKEKVDGLQKEKDRLRTERDSLKETIEELrcvqaqE 434
Cdd:TIGR02169 747 ssleQEIENVKSELKELEARIEELEEDLHKLEEALNDLE--ARLSHSRIPEIQAELSKLEEEVSRIEARLREI------E 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 435 GQLTTSAGLMPLGSQESSdslaaeivtpEIKEKLIRLQHENKMLKLNQEgSDNEKIALLQSLLDDANLRKNELETENRLV 514
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQ----------ELQEQRIDLKEQIKSIEKEIE-NLNGKKEELEEELEELEAALRDLESRLGDL 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 515 NQRLLEVQSQVEELQKSLQEQGSKAEDSVLLKKKLEEHLEKLHEANNEIQR-KRAIIED--LEPRYNNSSLKIEELQEAL 591
Cdd:TIGR02169 888 KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDpKGEDEEIpeEELSLEDVQAELQRVEEEI 967
|
.
gi 1729156918 592 R 592
Cdd:TIGR02169 968 R 968
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
173-533 |
2.23e-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: 61.24 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 173 DLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLaENQILMERLnqsdsIEDPNSPAGRRHLQLQTQLE 252
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEK-----REYEGYELLKEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 253 QLQEETFRLEAAKDDYRIRCEELEKEIAELRQQNEELTT-----LAEEAQSLKDEMDVLrhsSDKVAKLESQVESYKKKL 327
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKkikdlGEEEQLRVKEKIGEL---EAEIASLERSIAEKEREL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 328 EDLGDLRRQVKLLEEKNTMYMQNtvsLEEELRKAHAARSQLET----YKRQVVELQNRLSEESKKADKLEFEYKLLKEKV 403
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEE---LEREIEEERKRRDKLTEeyaeLKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 404 DGLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTSAGLMPLGSQESSDSLAAEIVTPEIKEKLIRlqheNKMLKLNQE 483
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA----ADLSKYEQE 470
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1729156918 484 GSD-NEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQ 533
Cdd:TIGR02169 471 LYDlKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
173-656 |
5.29e-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: 5.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 173 DLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSiedpnspagrrhlqlqtQLE 252
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER-----------------QLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 253 QLQEETFRLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSLKDEM--------DVLRHSSDKVAKLESQVESYK 324
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELesrleeleEQLETLRSKVAQLELQIASLN 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 325 KKLEdlgDLRRQVKLLEEKNTMYMQNTVSLEEELRKA--HAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEK 402
Cdd:TIGR02168 400 NEIE---RLEARLERLEDRRERLQQEIEELLKKLEEAelKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 403 VDGLQKEKDRLRTERDSLKETIEEL----RCVQAQEGQLTTSAGLMPLGSQ----ESSDSLAAEIVTPEIKEKLI----- 469
Cdd:TIGR02168 477 LDAAERELAQLQARLDSLERLQENLegfsEGVKALLKNQSGLSGILGVLSElisvDEGYEAAIEAALGGRLQAVVvenln 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 470 ----------------------------RLQHENKMLKLNQEG----------SDNEKIALLQSLL---------DDANL 502
Cdd:TIGR02168 557 aakkaiaflkqnelgrvtflpldsikgtEIQGNDREILKNIEGflgvakdlvkFDPKLRKALSYLLggvlvvddlDNALE 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 503 RKNELETENRLV--------------------NQRLLEVQSQVEELQKSLQEQGSKAEDsvlLKKKLEEHLEKLHEANNE 562
Cdd:TIGR02168 637 LAKKLRPGYRIVtldgdlvrpggvitggsaktNSSILERRREIEELEEKIEELEEKIAE---LEKALAELRKELEELEEE 713
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 563 IQRKRAIIEDLEPRYNNSSLKIEEL---QEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGTA------PEIQA 633
Cdd:TIGR02168 714 LEQLRKELEELSRQISALRKDLARLeaeVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAeieeleAQIEQ 793
|
570 580
....*....|....*....|...
gi 1729156918 634 LKNQLQERDRMFHSLEKEYEKTK 656
Cdd:TIGR02168 794 LKEELKALREALDELRAELTLLN 816
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
153-576 |
8.67e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.90 E-value: 8.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 153 AIQELMSKESPVSVGNDAYVDLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDS 232
Cdd:PRK02224 207 RLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 233 IEDpnspagrrhlqlqtqleqlqeetfRLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQslkdemDVLRHSSDK 312
Cdd:PRK02224 287 RLE------------------------ELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELR------DRLEECRVA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 313 VAKLESQVESYKKKLEDlgdlrrqvklLEEKNTMYMQNTVSLEEELRkahAARSQLETYKRQVVELQNRLSEESKKADKL 392
Cdd:PRK02224 337 AQAHNEEAESLREDADD----------LEERAEELREEAAELESELE---EAREAVEDRREEIEELEEEIEELRERFGDA 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 393 EFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEELRCVQAqEGQLTTSAGLMPLGSQESSDSLAAEIVTpEIKEKLIRLQ 472
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDELREREAELEATLRTARERVE-EAEALLEAGKCPECGQPVEGSPHVETIE-EDRERVEELE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 473 HENKMLKLNQEgSDNEKIALLQSLLDDANlRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDsvlLKKKLEEH 552
Cdd:PRK02224 482 AELEDLEEEVE-EVEERLERAEDLVEAED-RIERLEERREDLEELIAERRETIEEKRERAEELRERAAE---LEAEAEEK 556
|
410 420
....*....|....*....|....
gi 1729156918 553 LEKLHEANNEIQRKRAIIEDLEPR 576
Cdd:PRK02224 557 REAAAEAEEEAEEAREEVAELNSK 580
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
213-664 |
9.86e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 9.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 213 KSSLLA-ENQILMERLNQSdsIEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDDYR---IRCEELEKEIAELRQQNEE 288
Cdd:COG4717 36 KSTLLAfIRAMLLERLEKE--ADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAelqEELEELEEELEELEAELEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 289 LTT---LAEEAQSLKDEMDVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEELRkaHAAR 365
Cdd:COG4717 114 LREeleKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLS--LATE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 366 SQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKdrlrtERDSLKETIEELR---------CVQAQEGQ 436
Cdd:COG4717 192 EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL-----EAAALEERLKEARlllliaaalLALLGLGG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 437 LTTSAGLMPLGSQESSDSLAAEIVTPEIKEKLIRLQHENKMLKLN-QEGSDNEKIALLQSLLDDANLRKNELETENRLVN 515
Cdd:COG4717 267 SLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPaLEELEEEELEELLAALGLPPDLSPEELLELLDRI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 516 QRLLEVQSQVEELQKSLQEQGSKAEDSVLLKK---KLEEHLEKLHEANNEIQRKRAIIEDLEPRYNNSSLKIEELQEALr 592
Cdd:COG4717 347 EELQELLREAEELEEELQLEELEQEIAALLAEagvEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL- 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1729156918 593 kkeeemkqMEERYKKYLEKAKSVIRTLDPKQNQGTApEIQALKNQLQ--ERDRMFHSLEKEYEKTKTQREMEEK 664
Cdd:COG4717 426 --------DEEELEEELEELEEELEELEEELEELRE-ELAELEAELEqlEEDGELAELLQELEELKAELRELAE 490
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
260-707 |
1.01e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 260 RLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSLkdemdvLRHSSDKVAKLESQVESYKKKLEDLgdLRRQVKL 339
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAE------EYELLAELARLEQDIARLEERRREL--EERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 340 LEEkntmymqntvsLEEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDS 419
Cdd:COG1196 322 EEE-----------LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 420 LKETIEELRcvQAQEGQLTTSAGLMPLGSQESSDSLAAEIVTPEIKEKLIRLQHENKMLKLNQEGSDNEKIALLQSLLDD 499
Cdd:COG1196 391 ALRAAAELA--AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 500 anLRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDSVLLKKKLEEHLEKLHEANNEIQRKRAIIEDLEprynn 579
Cdd:COG1196 469 --LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE----- 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 580 sslkiEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQN-QGTAPEIQALKNQLQERDRMFHSLEKEYEKTKTQ 658
Cdd:COG1196 542 -----AALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKiRARAALAAALARGAIGAAVDLVASDLREADARYY 616
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1729156918 659 REME---EKFIVSAWYNMGMTLHKKAAEDRLASTGSGQSFLARQRQATNTRR 707
Cdd:COG1196 617 VLGDtllGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR 668
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
282-653 |
2.20e-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: 57.82 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 282 LRQQNEELTTLAEEAQSLKDEMDVLRHSSDKvaKLESQVESYKKKLEDL-GDLRRQVKLLEEKNTMYMQNTVSLEEELRK 360
Cdd:pfam15921 226 LRELDTEISYLKGRIFPVEDQLEALKSESQN--KIELLLQQHQDRIEQLiSEHEVEITGLTEKASSARSQANSIQSQLEI 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 361 AH-AARSQLETYKRQVVELQNRLSEESKKadkLEFEYKLLKEKVDGLQK-------EKDRLRTERDSLketieelrcvqa 432
Cdd:pfam15921 304 IQeQARNQNSMYMRQLSDLESTVSQLRSE---LREAKRMYEDKIEELEKqlvlansELTEARTERDQF------------ 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 433 qegqlttsaglmplgSQES---SDSLAAEIVTPEIKEKLIRLQHENKMLKLNQEGSDNEKIALLQSLLDDANLRKNELET 509
Cdd:pfam15921 369 ---------------SQESgnlDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 510 enrLVNQRLLEVQSQVEELQKSLQEQGSKAEDSVLLKKKLEEHLEKLHEANNEIQRKRAIIEDLEPRYNNSSLKIEELQE 589
Cdd:pfam15921 434 ---LLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKER 510
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1729156918 590 ALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGTapEIQALKNQLQERDRMFHSLEKEYE 653
Cdd:pfam15921 511 AIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQT--ECEALKLQMAEKDKVIEILRQQIE 572
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
174-426 |
3.28e-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: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 174 LDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDPNSpagRRHLQLQTQLEQ 253
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE---ERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 254 LQEETFRLEAAKDDYRIRCEELEKEIAELRQQNEEL---------TTLAEEAQSLKDEMDVLRHSSDKVAKLESQVESYK 324
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAeaelaeaeeALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 325 KKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVD 404
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
250 260
....*....|....*....|..
gi 1729156918 405 GLQKEKDRLRTERDSLKETIEE 426
Cdd:COG1196 481 ELLEELAEAAARLLLLLEAEAD 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
304-650 |
3.51e-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: 57.37 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 304 DVLRHSSDKVAKLESQVES---YKKKLEDLGDLRRQVKLLEekntmymqntvsLEEELRKAHAARSQLETYKRQVVELQN 380
Cdd:TIGR02168 193 DILNELERQLKSLERQAEKaerYKELKAELRELELALLVLR------------LEELREELEELQEELKEAEEELEELTA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 381 RLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEELRCVQAQegqlttsaglmplgSQESSDSLAAEIV 460
Cdd:TIGR02168 261 ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN--------------LERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 461 tpEIKEKLIRLQHENKMLKlNQEGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQeqgskae 540
Cdd:TIGR02168 327 --ELESKLDELAEELAELE-EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA------- 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 541 dsvLLKKKLEEHLEKLHEANNEIQRKRAIIEDLEPRYnnSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLD 620
Cdd:TIGR02168 397 ---SLNNEIERLEARLERLEDRRERLQQEIEELLKKL--EEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
330 340 350
....*....|....*....|....*....|
gi 1729156918 621 PKQNqgtapEIQALKNQLQERDRMFHSLEK 650
Cdd:TIGR02168 472 EAEQ-----ALDAAERELAQLQARLDSLER 496
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
174-472 |
5.79e-08 |
|
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: 56.61 E-value: 5.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 174 LDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDsiedpnspagRRHLQLQTQLEQ 253
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK----------ERLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 254 LQEETFRLEAAKDDYRIRCEELEKEIAELRQQNEEL--TTLAEEAQSLKDEMDVLRhssDKVAKLESQVESYKKKLEDLg 331
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLeaRLSHSRIPEIQAELSKLE---EEVSRIEARLREIEQKLNRL- 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 332 DLRRQvkLLEEKntmyMQNTVSLEEELRKAHAARSQ-LETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEK 410
Cdd:TIGR02169 825 TLEKE--YLEKE----IQELQEQRIDLKEQIKSIEKeIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL 898
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 411 DRLRTERDSLKETIEELRC--------VQAQEGQLTTSAGLMPLGSQESSDSLAAEIVTPEIKEKLIRLQ 472
Cdd:TIGR02169 899 RELERKIEELEAQIEKKRKrlselkakLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIR 968
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
179-583 |
7.05e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 7.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 179 KKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDsiEDPNSPAGRRHLQLQTQLEQLQEET 258
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE--EKKKAEEAKKAEEDKNMALRKAEEA 1586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 259 FRLEAAKDDYRIRCEELEKEI-AELRQQNEELTTLAEEAQSLKDEMDVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQV 337
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEEKKMkAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 338 KLLEEKNTMYMQNTVSLEEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTER 417
Cdd:PTZ00121 1667 AKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA 1746
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 418 DSLKETIEELRCVQAQEGQLTTSAGLMP----------LGSQESSDSLAAEIVTPEIKEKLIRLQHENKMLKLNQEGSDN 487
Cdd:PTZ00121 1747 EEAKKDEEEKKKIAHLKKEEEKKAEEIRkekeavieeeLDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKE 1826
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 488 EKIALLQSLLDDANLRKNELEtenrlvnqrllEVQSQVEELQKSLQEQGSKAEDSVLLKKKLEEHLEKLHEANneiQRKR 567
Cdd:PTZ00121 1827 MEDSAIKEVADSKNMQLEEAD-----------AFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEAD---EIEK 1892
|
410
....*....|....*.
gi 1729156918 568 AIIEDLEPRYNNSSLK 583
Cdd:PTZ00121 1893 IDKDDIEREIPNNNMA 1908
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
259-520 |
8.88e-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: 55.83 E-value: 8.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 259 FRLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSLKDEMDV-LRHSSDKVAKLESQVESYKKKLEDLG----DL 333
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQqKQILRERLANLERQLEELEAQLEELEskldEL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 334 RRQVKLLEEKNTMYMQNTVSLEEELRKAHA----ARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKE 409
Cdd:TIGR02168 336 AEELAELEEKLEELKEELESLEAELEELEAeleeLESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDR 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 410 KDRLRTERDSLKETIEELRCVQAQEGQLTTSAGLMPLGSQESSDSLAAEIVTPEIKEKLIRLQHENkmlklNQEGSDNEK 489
Cdd:TIGR02168 416 RERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE-----RELAQLQAR 490
|
250 260 270
....*....|....*....|....*....|.
gi 1729156918 490 IALLQSLLddanlrkNELETENRLVNQRLLE 520
Cdd:TIGR02168 491 LDSLERLQ-------ENLEGFSEGVKALLKN 514
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
318-559 |
1.30e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 318 SQVESYKKKLEDLGDLRRQVKLLEEKntmymqntvsLEEELRKAHAARSQLETYKRQVVELQNRLSEeskkadkLEFEYK 397
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKE----------LAALKKEEKALLKQLAALERRIAALARRIRA-------LEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 398 LLKEKVDGLQKEKDRLRTERDSLKETIEELRCVQAQEGQlttSAGLMPLGSQESSDSLAA-----EIVTPEIKEKLIRLQ 472
Cdd:COG4942 80 ALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGR---QPPLALLLSPEDFLDAVRrlqylKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 473 HENKMLKLNQEGSDNEKiALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDSVLLKKKLEEH 552
Cdd:COG4942 157 ADLAELAALRAELEAER-AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
....*..
gi 1729156918 553 LEKLHEA 559
Cdd:COG4942 236 AAAAAER 242
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
173-427 |
1.42e-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: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 173 DLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAE-------------NQILMERLNQSDSIEDPNSP 239
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlshsripeiqaelSKLEEEVSRIEARLREIEQK 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 240 AGRRHLQLQTQLEQLQEetfrLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQ-SLKDEMDVLRHSSDKVAKLES 318
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQE----LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEaALRDLESRLGDLKKERDELEA 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 319 QVESYKKKLEDLG----DLRRQVKLLEEKNTMYMQNTVSLEEELRK---AHAARSQLETYKRQVVELQNRLSEESKKADK 391
Cdd:TIGR02169 897 QLRELERKIEELEaqieKKRKRLSELKAKLEALEEELSEIEDPKGEdeeIPEEELSLEDVQAELQRVEEEIRALEPVNML 976
|
250 260 270
....*....|....*....|....*....|....*.
gi 1729156918 392 LEFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEEL 427
Cdd:TIGR02169 977 AIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
173-644 |
1.45e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.05 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 173 DLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQilMERLNQsDSIEDPNSPAGRRHLQLQTQLE 252
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG--LDDADA-EAVEARREELEDRDEELRDRLE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 253 QLQEETFRLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSlkdemdVLRHSSDKVAKLESQVESYKKKLEDLGD 332
Cdd:PRK02224 332 ECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEARE------AVEDRREEIEELEEEIEELRERFGDAPV 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 333 LRRQVKLLEEkntmymqntvSLEEELRKAHAARSQLETYKRqvvELQNRLSE------------------ESKKADKLEf 394
Cdd:PRK02224 406 DLGNAEDFLE----------ELREERDELREREAELEATLR---TARERVEEaealleagkcpecgqpveGSPHVETIE- 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 395 EYkllKEKVDGLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTSAglmplGSQESSDSLAAEIVTpEIKEKLIRLQHE 474
Cdd:PRK02224 472 ED---RERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLE-----ERREDLEELIAERRE-TIEEKRERAEEL 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 475 NKML-KLNQEGSDNEKIAllqsllDDANLRKNELETENRLVNQRLLEVQSQVEELQKsLQEQGSKAEDSVLLKKKLEEHL 553
Cdd:PRK02224 543 RERAaELEAEAEEKREAA------AEAEEEAEEAREEVAELNSKLAELKERIESLER-IRTLLAAIADAEDEIERLREKR 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 554 EKLHEANNE----IQRKRAIIEDLEPRYNNSslKIEELQEalrkkeeemkqMEERYKKYLEKAKSVIRTLDPKQNQGTAp 629
Cdd:PRK02224 616 EALAELNDErrerLAEKRERKRELEAEFDEA--RIEEARE-----------DKERAEEYLEQVEEKLDELREERDDLQA- 681
|
490
....*....|....*
gi 1729156918 630 EIQALKNQLQERDRM 644
Cdd:PRK02224 682 EIGAVENELEELEEL 696
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
260-666 |
3.92e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 260 RLEAAKDDYRIRCEELEKEIAE-------LRQQNEELTTLAEEAQSLkdeMDVLRHSSDKVAKLESQVESYKKKLEDLGD 332
Cdd:PRK03918 166 NLGEVIKEIKRRIERLEKFIKRtenieelIKEKEKELEEVLREINEI---SSELPELREELEKLEKEVKELEELKEEIEE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 333 LRRQVKLLEEKNTMYMQNTVSLEEELRKAHAARSQLETYKRQVVELQnrlsEESKKADKLEFEYKLLKEKVDGLQKEKDR 412
Cdd:PRK03918 243 LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK----EKAEEYIKLSEFYEEYLDELREIEKRLSR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 413 LRTERDSLKETIEELRCVQAQEGQLTTSaglmplgSQESSDSLAAEIVTPEIKEKLIRLQHENKMLKLNQEGSDNEKIAl 492
Cdd:PRK03918 319 LEEEINGIEERIKELEEKEERLEELKKK-------LKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLE- 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 493 lqSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDSVLLKKKLEEHLEKlheanNEIQRKRAIIED 572
Cdd:PRK03918 391 --KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRK-----ELLEEYTAELKR 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 573 LEPRYNNSSLKIEELQEALRkkeeemkqmeeRYKKYLEKAKSVIRTLDpkqnqgTAPEIQALKNQLQErdrmfHSLEKEY 652
Cdd:PRK03918 464 IEKELKEIEEKERKLRKELR-----------ELEKVLKKESELIKLKE------LAEQLKELEEKLKK-----YNLEELE 521
|
410
....*....|....
gi 1729156918 653 EKTKTQREMEEKFI 666
Cdd:PRK03918 522 KKAEEYEKLKEKLI 535
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
271-666 |
4.88e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 4.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 271 RCEELEKEIAELRQQNEELTTLAEE---AQSLKDEMDVLRHSSD--KVAKLESQVESYKKKLEDLGDLRRQVKLLEEKNT 345
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKAAAAkkkADEAKKKAEEKKKADEakKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 346 MymQNTVSLEEELRKAHAARSQLETYKRQVVELQNRlSEESKKADKLEFEYKllKEKVDGLQKEKDRLRTERDSLKETI- 424
Cdd:PTZ00121 1472 A--DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA-AEAKKKADEAKKAEE--AKKADEAKKAEEAKKADEAKKAEEKk 1546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 425 --EELRcvQAQEGQLTTSAGLMPLGSQESSDSLAAEIVTPEIK-------EKLIRLQHENKMLKLNQEGSDNEKIALLQS 495
Cdd:PTZ00121 1547 kaDELK--KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKkaeeariEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 496 LLDDANLRKNELEtenrlVNQRLLEVQSQVEELQKSLQEQGSKAEDsvlLKKKLEEHLEKLHEANNEIQRKRAIIEDLEp 575
Cdd:PTZ00121 1625 LKKAEEEKKKVEQ-----LKKKEAEEKKKAEELKKAEEENKIKAAE---EAKKAEEDKKKAEEAKKAEEDEKKAAEALK- 1695
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 576 RYNNSSLKIEELqealRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQgTAPEIQALKNQLQERDRMFHSLEKEYEKT 655
Cdd:PTZ00121 1696 KEAEEAKKAEEL----KKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE-DKKKAEEAKKDEEEKKKIAHLKKEEEKKA 1770
|
410
....*....|.
gi 1729156918 656 KTQREMEEKFI 666
Cdd:PTZ00121 1771 EEIRKEKEAVI 1781
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
260-663 |
7.12e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 7.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 260 RLEAAKDDYRIRCEELEKEIAEL----RQQNEELTTLAEEAQSLKDEMDVLRHSSDKVAKLESQVESYKKKLED-LGDLR 334
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREELaeevRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDrLEECR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 335 RQVKLLEEKNTMYMQNTVSLEEELRKAHAARSQLETykrQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLR 414
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDLEERAEELREEAAELES---ELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 415 TERDSLKETIEELRcvqAQEGQLTTSAglmplgsQESSDSLaaeivtpeikEKLIRLQHENKMLKLNQEGSDNEKIallq 494
Cdd:PRK02224 412 DFLEELREERDELR---EREAELEATL-------RTARERV----------EEAEALLEAGKCPECGQPVEGSPHV---- 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 495 SLLDDANLRKNELETEnrlvnqrLLEVQSQVEELQKSLQEqgskAEDSVLLKKKLEEHLEKLHEANNEIQRKRAIIEDLE 574
Cdd:PRK02224 468 ETIEEDRERVEELEAE-------LEDLEEEVEEVEERLER----AEDLVEAEDRIERLEERREDLEELIAERRETIEEKR 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 575 PRYNNSSLKIEELQEALRKKEEEMKQMEERykkyLEKAKSVIRTLDPKQNQGTApEIQALKN---QLQERDRMFHSLEKE 651
Cdd:PRK02224 537 ERAEELRERAAELEAEAEEKREAAAEAEEE----AEEAREEVAELNSKLAELKE-RIESLERirtLLAAIADAEDEIERL 611
|
410
....*....|..
gi 1729156918 652 YEKTKTQREMEE 663
Cdd:PRK02224 612 REKREALAELND 623
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
173-640 |
1.23e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 173 DLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDpnsPAGRRHLQLQTQLE 252
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA---EAEEELEELAEELL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 253 QLQEETFRLEAAKDDYRIRCEELEKEIAELRQQNEEL-TTLAEEAQSLKDEMDVLRHSSDKVAKLESQVESYKKKLEDLG 331
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELeEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 332 DLRRQVKLLEEKNTMYMQNTVSLEEELRKAHAARSQLE--TYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKE 409
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLegVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 410 KDRLRTERDsLKETIEELRcvQAQEGQLTTSAGLMPLGSQESSDSLAAEIVTPEIKEKLIRLQHENkmLKLNQEGSDNEK 489
Cdd:COG1196 550 NIVVEDDEV-AAAAIEYLK--AAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREAD--ARYYVLGDTLLG 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 490 IALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGS----KAEDSVLLKKKLEEHLEKLHEANNEIQR 565
Cdd:COG1196 625 RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAalleAEAELEELAERLAEEELELEEALLAEEE 704
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1729156918 566 KRAIIEDLEPRYNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGTApEIQALKNQLQE 640
Cdd:COG1196 705 EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER-ELERLEREIEA 778
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
273-592 |
1.46e-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: 51.90 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 273 EELEKEIAELRQQNEELTTLAEEAQSLKDEMDV----LRHSSDKVAKLESQVESYKKKLEDLGDLRRQVKLLEEKNTMYM 348
Cdd:pfam02463 202 LKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLneerIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEK 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 349 QNTVSLEEELRKAHA-ARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEEL 427
Cdd:pfam02463 282 KLQEEELKLLAKEEEeLKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEEL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 428 RCVQAQEgqlttsaglmplgSQESSDSLAAEIVTPEIKEKLIRLQHENKMLKLNQEGSDNEKIALLQSLLDDANLRKNEL 507
Cdd:pfam02463 362 EKLQEKL-------------EQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 508 ETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDSVLLKKKLEEHLEKLHEANNEIQRKRAIIEDLEPRYNNSSLKIEEL 587
Cdd:pfam02463 429 LEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSG 508
|
....*
gi 1729156918 588 QEALR 592
Cdd:pfam02463 509 LKVLL 513
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
304-592 |
2.36e-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: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 304 DVLRHSSDKVAKLESQVESYKkkleDLGDLRRQVK--LLEEKNTM--------YMQNTVSLEEELRKAHAARSQLEtykr 373
Cdd:COG4913 184 RRLGIGSEKALRLLHKTQSFK----PIGDLDDFVReyMLEEPDTFeaadalveHFDDLERAHEALEDAREQIELLE---- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 374 QVVELQNRLSEESKKADKLEF------------EYKLLKEKVDGLQKEKDRLRTERDSLKETIEELRcvqaqegqlttsa 441
Cdd:COG4913 256 PIRELAERYAAARERLAELEYlraalrlwfaqrRLELLEAELEELRAELARLEAELERLEARLDALR------------- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 442 glmplgsqessdslaaeivtpeikEKLIRLQHEnkmlklnQEGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEV 521
Cdd:COG4913 323 ------------------------EELDELEAQ-------IRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAL 371
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1729156918 522 QSQVEELQKSLQEQGSKAEDSV--------LLKKKLEEHLEKLHEANNEIQRKRAIIEDLEPRYNNSSLKIEELQEALR 592
Cdd:COG4913 372 GLPLPASAEEFAALRAEAAALLealeeeleALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
260-428 |
2.69e-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: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 260 RLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAE-------------EAQSLKDEMDVLRHSSDKVAKLESQVESYKKK 326
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeidvasaerEIAELEAELERLDASSDDLAALEEQLEELEAE 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 327 LEDL----GDLRRQVKLLEEKNTmymqntvSLEEELRKAHAARSQLETYKRQVV--ELQNRLSEESKKAdklefeykLLK 400
Cdd:COG4913 701 LEELeeelDELKGEIGRLEKELE-------QAEEELDELQDRLEAAEDLARLELraLLEERFAAALGDA--------VER 765
|
170 180
....*....|....*....|....*...
gi 1729156918 401 EKVDGLQKEKDRLRTERDSLKETIEELR 428
Cdd:COG4913 766 ELRENLEERIDALRARLNRAEEELERAM 793
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
273-583 |
2.90e-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: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 273 EELEKEIAELRqqnEELTTLAEEAQSLKDEMDVLRHSSDKVAKLESQVESykkkLEDLGDLRRQVklleekntmymqntV 352
Cdd:COG4913 613 AALEAELAELE---EELAEAEERLEALEAELDALQERREALQRLAEYSWD----EIDVASAEREI--------------A 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 353 SLEEELRKAHAARSQLETYKRQVVELQNRLseeskkaDKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEELrcvqA 432
Cdd:COG4913 672 ELEAELERLDASSDDLAALEEQLEELEAEL-------EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA----E 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 433 QEGQLTTSAGLMPLGSQESSDSLAAEIVTpeikekliRLQHENKMLKLNQEGSDNEKIALLQSLLDDANLRKNELETE-- 510
Cdd:COG4913 741 DLARLELRALLEERFAAALGDAVERELRE--------NLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADle 812
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 511 ---------NRLVNQRLLEVQSQVEELQKSLQEQgskaedsvllkkKLEEHLEKLHEANNEIQRKraiIEDLeprynNSS 581
Cdd:COG4913 813 slpeylallDRLEEDGLPEYEERFKELLNENSIE------------FVADLLSKLRRAIREIKER---IDPL-----NDS 872
|
..
gi 1729156918 582 LK 583
Cdd:COG4913 873 LK 874
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
260-426 |
3.27e-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: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 260 RLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSLKDEMDV-LRHSSDKVAKLESQVESYKKKLEDLGDLRRQVK 338
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKeIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 339 LLEEKNTMYMQNTVsLEEELRKAHAarsQLETYKRQVVELQNRLSEESKKADKLEFEyklLKEKVDGLQKEKDRLRTERD 418
Cdd:COG1579 94 LQKEIESLKRRISD-LEDEILELME---RIEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAERE 166
|
....*...
gi 1729156918 419 SLKETIEE 426
Cdd:COG1579 167 ELAAKIPP 174
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
266-659 |
3.66e-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: 50.84 E-value: 3.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 266 DDYRIRCEELEKEIAELRQQNEELTTLAEEaqsLKDEMDVLRHSSDKVaklesqvESYKKKLEDLGDLRRQVKLLEEKNT 345
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDE---KRQQLERLRREREKA-------ERYQALLKEKREYEGYELLKEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 346 MYMQNTV-----SLEEELRKAHAARSQLEtykRQVVELQNRLSEESKKADKL-EFEYKLLKEKVDGLQKEKDRLRterDS 419
Cdd:TIGR02169 236 ERQKEAIerqlaSLEEELEKLTEEISELE---KRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLE---RS 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 420 LKETIEELRCVQAQEGQLttsaglmplgsQESSDSLAAEIvtPEIKEKLIRLQHENKMLKlnqegsdnEKIALLQSLLDD 499
Cdd:TIGR02169 310 IAEKERELEDAEERLAKL-----------EAEIDKLLAEI--EELEREIEEERKRRDKLT--------EEYAELKEELED 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 500 ANLRKNELETENRLVNQRLLEVQSQVEELQKSLQEqgSKAEDSVLLKKKLEEHlEKLHEANNEIQRKRAIIEDLEPRYNN 579
Cdd:TIGR02169 369 LRAELEEVDKEFAETRDELKDYREKLEKLKREINE--LKRELDRLQEELQRLS-EELADLNAAIAGIEAKINELEEEKED 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 580 SSLKIEELQEALrkkeeemkqmeERYKKYLEKAKSvirtldpkqnqgtapEIQALKNQLQERDRMFHSLEKEYEKTKTQR 659
Cdd:TIGR02169 446 KALEIKKQEWKL-----------EQLAADLSKYEQ---------------ELYDLKEEYDRVEKELSKLQRELAEAEAQA 499
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
327-664 |
3.76e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 327 LEDL-GDLRRQVKlleekntmymqntvSLEEELRKAHAARsqleTYKRQVVELQNRLSeeSKKADKLEFEYKLLKEKVDG 405
Cdd:COG1196 191 LEDIlGELERQLE--------------PLERQAEKAERYR----ELKEELKELEAELL--LLKLRELEAELEELEAELEE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 406 LQKEKDRLRTERDSLKETIEELRCVQAQEgqlttsaglmplgSQESSDSLAAEIvtpEIKEKLIRLQHENKMLKlnqegs 485
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEEL-------------ELELEEAQAEEY---ELLAELARLEQDIARLE------ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 486 dnEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDsvlLKKKLEEHLEKLHEANNEIQR 565
Cdd:COG1196 309 --ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE---AEEALLEAEAELAEAEEELEE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 566 KRAIIEDLEPRYNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQgtapEIQALKNQLQERDRMF 645
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA----LEEAAEEEAELEEEEE 459
|
330
....*....|....*....
gi 1729156918 646 HSLEKEYEKTKTQREMEEK 664
Cdd:COG1196 460 ALLELLAELLEEAALLEAA 478
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
384-660 |
4.13e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 4.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 384 EESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTSAglmplgsQESSDSLAAEIVTPE 463
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL-------RKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 464 ikEKLIRLQHENKMLKlNQEGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDSV 543
Cdd:TIGR02168 747 --ERIAQLSKELTELE-AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 544 LLKKKLEEHLE----KLHEANNEIQRKRAIIEDLEPRYNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTL 619
Cdd:TIGR02168 824 ERLESLERRIAaterRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1729156918 620 DPKQNqgtapEIQALKNQLQERDRMFHSLEKEYEKTKTQRE 660
Cdd:TIGR02168 904 RELES-----KRSELRRELEELREKLAQLELRLEGLEVRID 939
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
260-664 |
4.28e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 260 RLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSLKDEMDVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQVKL 339
Cdd:PTZ00121 1225 KAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKA 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 340 LEEKNTmymqntvslEEELRKAHAARSQLETYKRQVVELQNRlSEESKKAD--------KLEFEYKLLKEKVDGLQKEKD 411
Cdd:PTZ00121 1305 DEAKKK---------AEEAKKADEAKKKAEEAKKKADAAKKK-AEEAKKAAeaakaeaeAAADEAEAAEEKAEAAEKKKE 1374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 412 RLRTERDSLKETIEELRcvQAQEgqLTTSAGLMPLGSQESSDSLAAEIVTPEIKEKLIRLQHENKMLKLNQEGSDNEKIA 491
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEKK--KADE--AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAK 1450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 492 LLQSLLDDA-NLRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDSvllkKKLEEHLEKLHEANNEIQRKRAIi 570
Cdd:PTZ00121 1451 KKAEEAKKAeEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEA----KKAAEAKKKADEAKKAEEAKKAD- 1525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 571 edlEPRYNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGTAPEIQALKNQLQERDRMFHSLEK 650
Cdd:PTZ00121 1526 ---EAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYE 1602
|
410
....*....|....*..
gi 1729156918 651 EYEKTKTQ---REMEEK 664
Cdd:PTZ00121 1603 EEKKMKAEeakKAEEAK 1619
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
191-442 |
6.44e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 6.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 191 TKEEIAQRCHELDMQVAALQEEKSSL---LAENQILMERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDD 267
Cdd:PRK02224 469 TIEEDRERVEELEAELEDLEEEVEEVeerLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAE 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 268 YRIRCEELEKEIAELRQQNEE----LTTLAEEAQSLKDEMDVL---RHSSDKVAKLESQVESYKKKLEDLGDLRRQVK-L 339
Cdd:PRK02224 549 LEAEAEEKREAAAEAEEEAEEareeVAELNSKLAELKERIESLeriRTLLAAIADAEDEIERLREKREALAELNDERReR 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 340 LEEKNTMYMQNTVSLEEE-LRKAHAARSQLETYKRQVVElqnRLSEESKKADKLEFEYKLLKEKVDGLqkekDRLRTERD 418
Cdd:PRK02224 629 LAEKRERKRELEAEFDEArIEEAREDKERAEEYLEQVEE---KLDELREERDDLQAEIGAVENELEEL----EELRERRE 701
|
250 260
....*....|....*....|....
gi 1729156918 419 SLKETIEELRCVQAQEGQLTTSAG 442
Cdd:PRK02224 702 ALENRVEALEALYDEAEELESMYG 725
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
173-427 |
7.81e-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: 7.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 173 DLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAE----NQILMERLNQSDSIEDPNSPAGRRHLQLQ 248
Cdd:TIGR02168 723 ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERleeaEEELAEAEAEIEELEAQIEQLKEELKALR 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 249 TQLEQLQEETFRLEAAKDDYRIRCEELEKEIAELRQQNEElttLAEEAQSLKDEMDVLRHSsdkVAKLESQVESYKKKLE 328
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLED---LEEQIEELSEDIESLAAE---IEELEELIEELESELE 876
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 329 DLGDLRRQVK-LLEEKNTMYMQNTVSLEEELRKAHAARSQLETYKRQVVELQNRLSE--------ESKKADKLEFEYKLL 399
Cdd:TIGR02168 877 ALLNERASLEeALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGlevridnlQERLSEEYSLTLEEA 956
|
250 260
....*....|....*....|....*...
gi 1729156918 400 KEKVDGLQKEKDRLRTERDSLKETIEEL 427
Cdd:TIGR02168 957 EALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
360-568 |
8.73e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 8.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 360 KAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEEL------RCVQAQ 433
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERreelgeRARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 434 EGQLTTSAGLMPLGSQESSDSLaaeivtpeikeklirlqheNKMLKLNQ-EGSDNEKIALLQSLLDDANLRKNELETENR 512
Cdd:COG3883 97 RSGGSVSYLDVLLGSESFSDFL-------------------DRLSALSKiADADADLLEELKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1729156918 513 LVNQRLLEVQSQVEELQKSLQEQGSKAEDSVLLKKKLEEHLEKLHEANNEIQRKRA 568
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
259-669 |
2.70e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 259 FRLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSLKDEM--DVLRHSSDKVAKLESQVEsykkkledlgDLRRQ 336
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELeaQIRGNGGDRLEQLEREIE----------RLERE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 337 VKLLEEKNTMYMQNTVSLEEELRkahAARSQLETYKRQVVELQNRLSEESKKADKLEFEyklLKEKVDGLQKEKDRLRTE 416
Cdd:COG4913 354 LEERERRRARLEALLAALGLPLP---ASAEEFAALRAEAAALLEALEEELEALEEALAE---AEAALRDLRRELRELEAE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 417 RDSLK-------ETIEELRCVQAQEGQLTTS-----AGLM---------------------------------------- 444
Cdd:COG4913 428 IASLErrksnipARLLALRDALAEALGLDEAelpfvGELIevrpeeerwrgaiervlggfaltllvppehyaaalrwvnr 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 445 ------------------PLGSQESSDSLAAEIVT------PEIKEKLIR------------LQHENK------MLKLNQ 482
Cdd:COG4913 508 lhlrgrlvyervrtglpdPERPRLDPDSLAGKLDFkphpfrAWLEAELGRrfdyvcvdspeeLRRHPRaitragQVKGNG 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 483 E----------------GSDN-EKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKsLQEQGSKAEDSVLL 545
Cdd:COG4913 588 TrhekddrrrirsryvlGFDNrAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQR-LAEYSWDEIDVASA 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 546 KKK---LEEHLEKLHEANNEIQRKRAIIEDLEprynnssLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPK 622
Cdd:COG4913 667 EREiaeLEAELERLDASSDDLAALEEQLEELE-------AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1729156918 623 QNQGTAPEIQALKNQLQE------RDRMFHSLEKEYEKTKTQREMEEKFIVSA 669
Cdd:COG4913 740 EDLARLELRALLEERFAAalgdavERELRENLEERIDALRARLNRAEEELERA 792
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
298-568 |
3.19e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 47.23 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 298 SLKDEMD-VLR--HSSDKVaklesQVESYKKKLEDLgdlrrQVKLLEEKNTMYMQNTVSLEEELRKAHAARSQLETYKrq 374
Cdd:PRK05771 13 TLKSYKDeVLEalHELGVV-----HIEDLKEELSNE-----RLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVS-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 375 VVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLK--ETIE-ELRCVQAQEGqLTTSAGLMPLGSQES 451
Cdd:PRK05771 81 VKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwGNFDlDLSLLLGFKY-VSVFVGTVPEDKLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 452 SDSLAAEIVTPEIKEKlirlqHENKMLKLNQEGSDNEKIAllqSLLDDANLRKNELETEnRLVNQRLLEVQSQVEELQKS 531
Cdd:PRK05771 160 LKLESDVENVEYISTD-----KGYVYVVVVVLKELSDEVE---EELKKLGFERLELEEE-GTPSELIREIKEELEEIEKE 230
|
250 260 270
....*....|....*....|....*....|....*..
gi 1729156918 532 LQEQGSKAEDsvlLKKKLEEHLEKLHEAnNEIQRKRA 568
Cdd:PRK05771 231 RESLLEELKE---LAKKYLEELLALYEY-LEIELERA 263
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
360-592 |
3.51e-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: 46.68 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 360 KAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEELrcvQAQEGQLTT 439
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL---EKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 440 SaglmplgSQESSDSLAAEIVTpeikekLIRL-QHENKMLKLNQEGSD--NEKIALLQSLLDDANLRKNELETENRLVNQ 516
Cdd:COG4942 98 E-------LEAQKEELAELLRA------LYRLgRQPPLALLLSPEDFLdaVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1729156918 517 RLLEVQSQVEELQKSLQEQGSKAEDsvlLKKKLEEHLEKLHEANNEIQRKRAIIEDLEPRYNNSSLKIEELQEALR 592
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAA---LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
261-428 |
4.31e-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: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 261 LEAAKDDYRIRCEELEKEIAELRQQNEeLTTLAEEAQSLKDEMDVLRhssDKVAKLESQVESYKKKLEDLgdlRRQVKLL 340
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNG-LVDLSEEAKLLLQQLSELE---SQLAEARAELAEAEARLAAL---RAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 341 EEKNTMYMQNTV--SLEEELRKAHAARSQLET-----------YKRQVVELQNRLSEESKKA-DKLEFEYKLLKEKVDGL 406
Cdd:COG3206 253 PDALPELLQSPViqQLRAQLAELEAELAELSArytpnhpdviaLRAQIAALRAQLQQEAQRIlASLEAELEALQAREASL 332
|
170 180
....*....|....*....|..
gi 1729156918 407 QKEKDRLRTERDSLKETIEELR 428
Cdd:COG3206 333 QAQLAQLEARLAELPELEAELR 354
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
144-667 |
5.72e-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: 5.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 144 ESVQHVVMTAIQELMSKESPVSVGNDAYVDLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQIL 223
Cdd:TIGR02168 284 EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 224 -MERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAkddyRIRCEELEKEIAELRQQNEELTTLAEEAQSLKDE 302
Cdd:TIGR02168 364 eAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL----EARLERLEDRRERLQQEIEELLKKLEEAELKELQ 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 303 M----------DVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQVKLLEEKNTMymqnTVSLEEELRKAHAARSQLETYK 372
Cdd:TIGR02168 440 AeleeleeeleELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS----LERLQENLEGFSEGVKALLKNQ 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 373 RQVVELQNRLSeeskkaDKLEFEYKLLKEKVDGLQKEKDRLRTER-DSLKETIEELRcvQAQEGQLT------------T 439
Cdd:TIGR02168 516 SGLSGILGVLS------ELISVDEGYEAAIEAALGGRLQAVVVENlNAAKKAIAFLK--QNELGRVTflpldsikgteiQ 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 440 SAGLMPLGSQESSDSLAAEIVTPEIK----------------------EKLIRLQHENKMLKLNQE---------GSDNE 488
Cdd:TIGR02168 588 GNDREILKNIEGFLGVAKDLVKFDPKlrkalsyllggvlvvddldnalELAKKLRPGYRIVTLDGDlvrpggvitGGSAK 667
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 489 KIALLQSllddanlRKNELETenrlVNQRLLEVQSQVEELQKSLQ----EQGSKAEDSVLLKKKLEEHLEKLHEANNEIQ 564
Cdd:TIGR02168 668 TNSSILE-------RRREIEE----LEEKIEELEEKIAELEKALAelrkELEELEEELEQLRKELEELSRQISALRKDLA 736
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 565 RKRAIIEDLEPRYNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGTAPE--IQALKNQLQERD 642
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALReaLDELRAELTLLN 816
|
570 580
....*....|....*....|....*
gi 1729156918 643 RMFHSLEKEYEKTKTQREMEEKFIV 667
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLE 841
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
173-427 |
6.22e-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: 6.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 173 DLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQ-----------SDSIEDPNSPAG 241
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaanlrerLESLERRIAATE 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 242 RRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEIAELrqqNEELTTLAEEAQSLKDEMDVLrhsSDKVAKLESQVE 321
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL---LNERASLEEALALLRSELEEL---SEELRELESKRS 911
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 322 SYKKKLEDLGDLRRQVKLLEEKNTMYMQNT---------VSLEEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKL 392
Cdd:TIGR02168 912 ELRRELEELREKLAQLELRLEGLEVRIDNLqerlseeysLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAA 991
|
250 260 270
....*....|....*....|....*....|....*
gi 1729156918 393 EFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEEL 427
Cdd:TIGR02168 992 IEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
173-595 |
6.75e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 6.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 173 DLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDPnspAGRRHLQLQTQLE 252
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE---EEEALEEAAEEEA 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 253 QLQEETFRLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSLKDEMDVLRHSSDKVAKLESQVESYKKKLEDLGD 332
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 333 LRRQVKLLEEKNTMYMQNTV--------SLEEELRKAHAAR------------SQLETYKRQVVELQNRLSEESKKADKL 392
Cdd:COG1196 533 EAAYEAALEAALAAALQNIVveddevaaAAIEYLKAAKAGRatflpldkirarAALAAALARGAIGAAVDLVASDLREAD 612
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 393 EFEYKLLKEKVdGLQKEKDRLRTERDSLKETIEELRCVQAQEGQLttSAGLMPLGSQESSDSLAAEIVTPEIKEKLIRLQ 472
Cdd:COG1196 613 ARYYVLGDTLL-GRTLVAARLEAALRRAVTLAGRLREVTLEGEGG--SAGGSLTGGSRRELLAALLEAEAELEELAERLA 689
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 473 HENKMLKLNQEgsdnEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDSVLLKKKLEEH 552
Cdd:COG1196 690 EEELELEEALL----AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEEL 765
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1729156918 553 LEKLHEANNEIQRK-----RAIIE--DLEPRYNNSSLKIEELQEALRKKE 595
Cdd:COG1196 766 ERELERLEREIEALgpvnlLAIEEyeELEERYDFLSEQREDLEEARETLE 815
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
260-532 |
6.75e-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: 46.37 E-value: 6.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 260 RLEAAKDDYRIRCEELEKEIAELRQQ-NEELTTLAEEAQSLKDEMDVLrhSSDKVAKLESQVESYKKKLEDLGDLRRQVK 338
Cdd:pfam12128 280 ERQETSAELNQLLRTLDDQWKEKRDElNGELSAADAAVAKDRSELEAL--EDQHGAFLDADIETAAADQEQLPSWQSELE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 339 LLEEKntmymqntvsleeelrkaHAArsqLETYKRQVVELQNRLseESKKADKLEFEYKLLKEKVDGLQKEKDRLRT-ER 417
Cdd:pfam12128 358 NLEER------------------LKA---LTGKHQDVTAKYNRR--RSKIKEQNNRDIAGIKDKLAKIREARDRQLAvAE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 418 DSLKETIEELRC-VQAQEGQLTTSAGLMPLGSQESSDSLAAEIVTPEIKEKLIRLQHENKMLKLNQEGSdNEKIALLQSL 496
Cdd:pfam12128 415 DDLQALESELREqLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAA-NAEVERLQSE 493
|
250 260 270
....*....|....*....|....*....|....*.
gi 1729156918 497 LDDANLRKNELETENRLVNQRLLEVQSQVEELQKSL 532
Cdd:pfam12128 494 LRQARKRRDQASEALRQASRRLEERQSALDELELQL 529
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
262-664 |
7.15e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 7.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 262 EAAKDDYRIRCEELEKEiAELRQQNEELTTLAEEAQSLKDEMDVLRHSSDKVAKL-ESQVESYKKKLEDLGDLRRQVKLL 340
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKK-AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAaKAEAEAAADEAEAAEEKAEAAEKK 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 341 EEKNTMYMQNTVSLEEELRKAHAARSQLETYKRQVVELQNRlSEESKKADKLEFEYKLlKEKVDGLQKEKDRLRtERDSL 420
Cdd:PTZ00121 1373 KEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKA-AAAKKKADEAKKKAEE-KKKADEAKKKAEEAK-KADEA 1449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 421 KETIEELRCVQ--AQEGQLTTSAGLMPLGSQESSDSLAAEIVTPEIKEKLIRLQHENKMLKLNQEGSDNEKIALLQSLLD 498
Cdd:PTZ00121 1450 KKKAEEAKKAEeaKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK 1529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 499 DANLRKNE----LETENRLVNQRLLEVQSQVEELQKSlqEQGSKAEDSVLLKKKLEEHLEKLHEANNEIQRKRAIIEDLE 574
Cdd:PTZ00121 1530 AEEAKKADeakkAEEKKKADELKKAEELKKAEEKKKA--EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM 1607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 575 P-----RYNNSSLKIEELQEAlrkkeEEMKQMEERYKKYLEKAKSVIRTLDpKQNQGTAPEIQALKNQLQERDRMFHSLE 649
Cdd:PTZ00121 1608 KaeeakKAEEAKIKAEELKKA-----EEEKKKVEQLKKKEAEEKKKAEELK-KAEEENKIKAAEEAKKAEEDKKKAEEAK 1681
|
410
....*....|....*
gi 1729156918 650 KEYEKTKTQREMEEK 664
Cdd:PTZ00121 1682 KAEEDEKKAAEALKK 1696
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
263-428 |
7.47e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.16 E-value: 7.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 263 AAKDDYRIRCEELEKEIAELRQQNEELTT-LAEEAQSLKDEMDVLRHSSDKVAKLESQVESYKK--KLEDLGDL----RR 335
Cdd:PHA02562 213 ENIARKQNKYDELVEEAKTIKAEIEELTDeLLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKviKMYEKGGVcptcTQ 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 336 QVKLLEEKNTMYMQNTVSLEEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRT 415
Cdd:PHA02562 293 QISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQA 372
|
170
....*....|...
gi 1729156918 416 ERDSLKETIEELR 428
Cdd:PHA02562 373 EFVDNAEELAKLQ 385
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
334-428 |
7.48e-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: 7.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 334 RRQVKLLEEKNTMYMQNTVSLEEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLK----------EKV 403
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARseerreirkdREI 467
|
90 100
....*....|....*....|....*
gi 1729156918 404 DGLQKEKDRLRTERDSLKETIEELR 428
Cdd:COG2433 468 SRLDREIERLERELEEERERIEELK 492
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
154-425 |
8.98e-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: 8.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 154 IQELMSKESPVSVGNDAYVDLDRQLKKTTEELNEALATKE-----------EIAQRCHELDMQVAALQEEKSSLLAENQI 222
Cdd:pfam05557 57 IRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKEsqladarevisCLKNELSELRRQIQRAELELQSTNSELEE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 223 LMERLNQSDS----IEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRI---------RCEELEKEIAELRQQNEEL 289
Cdd:pfam05557 137 LQERLDLLKAkaseAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIvknskselaRIPELEKELERLREHNKHL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 290 TT-------LAEEAQSLKDEMDVLRHSSDKVA-------KLESQVESYKKKLEDLG-------DLRRQVKLLEEKNTMYM 348
Cdd:pfam05557 217 NEnienkllLKEEVEDLKRKLEREEKYREEAAtlelekeKLEQELQSWVKLAQDTGlnlrspeDLSRRIEQLQQREIVLK 296
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1729156918 349 QNTVSLEEELRKAHAARSQLETYKRQVVelqnrlseesKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKETIE 425
Cdd:pfam05557 297 EENSSLTSSARQLEKARRELEQELAQYL----------KKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILE 363
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
273-614 |
1.15e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.88 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 273 EELEKEIAELRQQNEELTTLAEEAQSLKDE-------MDVLRHSSD----KVAKLESQVESYKKKLEdlGDLRRQVKLLE 341
Cdd:pfam15921 377 DQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDdrnmEVQRLEALLKAMKSECQ--GQMERQMAAIQ 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 342 EKN------TMYMQNTVSLEEELRKA----HAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKD 411
Cdd:pfam15921 455 GKNeslekvSSLTAQLESTKEMLRKVveelTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQ 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 412 RLRTERDSLKETieelrcvqaqegqlttsaglmplgsQESSDSLAAEIVTPEIKEKLIRLQHENKMLKLNQEGSDNEKI- 490
Cdd:pfam15921 535 HLKNEGDHLRNV-------------------------QTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMq 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 491 ---ALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDSVLLKKKLEEHLEKLHeanNEIQRKR 567
Cdd:pfam15921 590 vekAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLL---NEVKTSR 666
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1729156918 568 AIIEDLEPRYnnsslkiEELQEALRKKEEEMKQMEERYKKYLEKAKS 614
Cdd:pfam15921 667 NELNSLSEDY-------EVLKRNFRNKSEEMETTTNKLKMQLKSAQS 706
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
183-592 |
1.54e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 183 EELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDPNSPAGRRHlqlqtqleqlqeetfRLE 262
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELE---------------ALE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 263 AAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSLKDEMDVL--RHSSDKVAKLESQVESYKKKLEDLGDLRRQVKLL 340
Cdd:COG4717 139 AELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELleQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 341 EEKNTMYMQNTVSLEEELRKAHAARsQLETYKRQ------VVELQNRLSEESKKADK-------------LEFEYKLLKE 401
Cdd:COG4717 219 QEELEELEEELEQLENELEAAALEE-RLKEARLLlliaaaLLALLGLGGSLLSLILTiagvlflvlgllaLLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 402 KVDGLQKEKDRLRTERDSLKET-IEELRCVQAQEGQLTTSAGLMPLGSQESSDSLAAEIVTPEIKEKLIRLQHENKMLkL 480
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEeLEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL-L 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 481 NQEGSDNEKIalLQSLLDDANlRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDSvLLKKKLEEHLEKLHEAN 560
Cdd:COG4717 377 AEAGVEDEEE--LRAALEQAE-EYQELKEELEELEEQLEELLGELEELLEALDEEELEEELE-ELEEELEELEEELEELR 452
|
410 420 430
....*....|....*....|....*....|....
gi 1729156918 561 NEIQRKRAIIEDLEP--RYNNSSLKIEELQEALR 592
Cdd:COG4717 453 EELAELEAELEQLEEdgELAELLQELEELKAELR 486
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
260-576 |
2.07e-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: 44.96 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 260 RLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSLKDEMDVLR---HSSDKVAKLESQVESYKKKLEDLGDLR-- 334
Cdd:pfam02463 146 IIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEelkLQELKLKEQAKKALEYYQLKEKLELEEey 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 335 ----RQVKLLEEKNTMYMQNTVSLEEELRKAhAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEK 410
Cdd:pfam02463 226 llylDYLKLNEERIDLLQELLRDEQEEIESS-KQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 411 DRLRTERDSLKETIEELRCVQAQEGQlttsaglmplgSQESSDSLAAEIVTPEIKEKLIRLQHENKMLKLNQEGSDNEKI 490
Cdd:pfam02463 305 LERRKVDDEEKLKESEKEKKKAEKEL-----------KKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 491 ALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDSVLLKKKLEEHLEKLHEANNEIQRKRAII 570
Cdd:pfam02463 374 ELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEEL 453
|
....*.
gi 1729156918 571 EDLEPR 576
Cdd:pfam02463 454 EKQELK 459
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
182-443 |
3.13e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 182 TEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQsdsiedpnspagrrhlqlqtqleqlqeetfrL 261
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA-------------------------------L 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 262 EAAKDDYRIRCEELEKEIAELRQQNEELTT-LAEEAQSLKDEMDVL-RHSSDKVAKLESQVESYKKKLEDLGDLRRQVKL 339
Cdd:COG4942 68 ARRIRALEQELAALEAELAELEKEIAELRAeLEAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 340 LEEKNTMYMQNTVSLEEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKLEfeyKLLKEKVDGLQKEKDRLRTERDS 419
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLL---ARLEKELAELAAELAELQQEAEE 224
|
250 260
....*....|....*....|....
gi 1729156918 420 LKETIEELRCVQAQEGQLTTSAGL 443
Cdd:COG4942 225 LEALIARLEAEAAAAAERTPAAGF 248
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
364-642 |
4.63e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 364 ARSQLETYKRQVVELQNRLSEeskkadklefeyklLKEKVDGLQKEKDRLRTERDSLkETIEELRcvqaqegqlttsagl 443
Cdd:COG4913 608 NRAKLAALEAELAELEEELAE--------------AEERLEALEAELDALQERREAL-QRLAEYS--------------- 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 444 mplgsqessdslAAEIVTPEIKEKLIRLQHENKMLKlnqegSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQS 523
Cdd:COG4913 658 ------------WDEIDVASAEREIAELEAELERLD-----ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEK 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 524 QVEELQKSLQEQGSKAEDSVLLKKK-LEEHLEKLHEANNEIQRKRAIIEDLEPRYNNSSLKIEELQEALRKKEeemkqme 602
Cdd:COG4913 721 ELEQAEEELDELQDRLEAAEDLARLeLRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAM------- 793
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1729156918 603 eryKKYLEKAKSVIRTLDPkqNQGTAPEIQALKNQLQERD 642
Cdd:COG4913 794 ---RAFNREWPAETADLDA--DLESLPEYLALLDRLEEDG 828
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
275-666 |
5.65e-04 |
|
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: 43.47 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 275 LEKEIAELRQQNEELTTLAEEAQSLKDEMDVLRHSSDKVAKLESQVESYKKKLEDL--------GDLRRQVKLLEEKNTM 346
Cdd:TIGR04523 98 INKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKEleklnnkyNDLKKQKEELENELNL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 347 YMQNTVSLEEELRKAHAARSQLETykrqvveLQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEE 426
Cdd:TIGR04523 178 LEKEKLNIQKNIDKIKNKLLKLEL-------LLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISN 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 427 lrcvqAQEGQLTTSAGLMPLGSQESSDSLAAEIVTPEIKEKLIRLQH-ENKMLKLNQEgSDNEKIALLQSLLDDANLRKN 505
Cdd:TIGR04523 251 -----TQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQlKSEISDLNNQ-KEQDWNKELKSELKNQEKKLE 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 506 ELETENRLVNQRLLEVQSQVEELQKSLQEQGSkaeDSVLLKKKLEEHLEKLHEANNEIQRKRAIIEDLEPRYNNSSLKIE 585
Cdd:TIGR04523 325 EIQNQISQNNKIISQLNEQISQLKKELTNSES---ENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 586 ELQEALRKKEEEMKQMEERYKKyLEKAKSVIRTLDPKQNQgtapEIQALKNQLqerdrmfHSLEKEYEKTKTQREMEEKF 665
Cdd:TIGR04523 402 NQEKLNQQKDEQIKKLQQEKEL-LEKEIERLKETIIKNNS----EIKDLTNQD-------SVKELIIKNLDNTRESLETQ 469
|
.
gi 1729156918 666 I 666
Cdd:TIGR04523 470 L 470
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
261-555 |
7.24e-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: 43.29 E-value: 7.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 261 LEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEA-QSLKDEMDVLR-----HSSDKVAKLESQVESYKKKLEDLGDLR 334
Cdd:pfam12128 609 AEEALQSAREKQAAAEEQLVQANGELEKASREETFArTALKNARLDLRrlfdeKQSEKDKKNKALAERKDSANERLNSLE 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 335 RQVKLLEEKNTMYMQNTvslEEELRKAHAARSQletyKRQVVELQNRLSEESKKADKLEfEYKLLKEKVDGLQKEKDR-- 412
Cdd:pfam12128 689 AQLKQLDKKHQAWLEEQ---KEQKREARTEKQA----YWQVVEGALDAQLALLKAAIAA-RRSGAKAELKALETWYKRdl 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 413 ------------LRTERDSLKETIEELrcvqAQEGQLTTSAGLMpLGSQESSDSLAAEIVTPEIKEKLIRLQHENKMLKL 480
Cdd:pfam12128 761 aslgvdpdviakLKREIRTLERKIERI----AVRRQEVLRYFDW-YQETWLQRRPRLATQLSNIERAISELQQQLARLIA 835
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1729156918 481 NQEgSDNEKIALLQSLLDDANLRKNELETENRLVNQRL--LEVQSQVEELQKSLQEQGSKAEDSVLLKKKLEEHLEK 555
Cdd:pfam12128 836 DTK-LRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLatLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKK 911
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
284-591 |
7.67e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.97 E-value: 7.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 284 QQNEELTTLAEEAQ----SLKDEMDVLRHSSDKVAKLESQ----VESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSLE 355
Cdd:PLN02939 111 IDNEQQTNSKDGEQlsdfQLEDLVGMIQNAEKNILLLNQArlqaLEDLEKILTEKEALQGKINILEMRLSETDARIKLAA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 356 EELRKAHAARSQLETYKRqvvELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEELRCVQAQEG 435
Cdd:PLN02939 191 QEKIHVEILEEQLEKLRN---ELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFKLEKERS 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 436 QLTTSaglmpLGSQESSDSLAAEIVTpeikeKLIRLQHENKMlklnqegsdnEKIALLQSLLDDAnlrKNELEtENRLVN 515
Cdd:PLN02939 268 LLDAS-----LRELESKFIVAQEDVS-----KLSPLQYDCWW----------EKVENLQDLLDRA---TNQVE-KAALVL 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 516 QRLLEVQSQVEELQKSLQEQGSKAEDSVLLK------KKLEEHLEKL-HEANNEIQRKRAIIEDLEPryNNSSLKIEELQ 588
Cdd:PLN02939 324 DQNQDLRDKVDKLEASLKEANVSKFSSYKVEllqqklKLLEERLQASdHEIHSYIQLYQESIKEFQD--TLSKLKEESKK 401
|
...
gi 1729156918 589 EAL 591
Cdd:PLN02939 402 RSL 404
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
262-411 |
9.38e-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: 9.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 262 EAAKDDYRIRCEELEK--EIAELRQQNEELTTLAEEAQSLKDEMDVLRHSSDKVakLESQVESYKKKLEdlgDLRRQVKL 339
Cdd:pfam17380 443 ERAREMERVRLEEQERqqQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKI--LEKELEERKQAMI---EEERKRKL 517
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1729156918 340 LeEKNTMYMQNTVSLEEELRKAHAA-RSQLETYKRQVVELQNRL-SEESKKADKLEFEYKLLKEKVDGLQKEKD 411
Cdd:pfam17380 518 L-EKEMEERQKAIYEEERRREAEEErRKQQEMEERRRIQEQMRKaTEERSRLEAMEREREMMRQIVESEKARAE 590
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
273-428 |
1.12e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 273 EELEKEIAELRQQNEELTTLAEEAQ--SLKDEMDVLRH-----SSDKVAKLESQVESYKKKLEDLGDLRRQVKLL--EEK 343
Cdd:COG4717 340 LELLDRIEELQELLREAEELEEELQleELEQEIAALLAeagveDEEELRAALEQAEEYQELKEELEELEEQLEELlgELE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 344 NTMYMQNTVSLEEEL----RKAHAARSQLETYKRQVVELQNRLS--EESKKADKLEFEYKLLKEKVDGLQKEKDRLRTER 417
Cdd:COG4717 420 ELLEALDEEELEEELeeleEELEELEEELEELREELAELEAELEqlEEDGELAELLQELEELKAELRELAEEWAALKLAL 499
|
170
....*....|.
gi 1729156918 418 DSLKETIEELR 428
Cdd:COG4717 500 ELLEEAREEYR 510
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
351-592 |
1.14e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 351 TVSLEEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTE----RDSLKETIEE 426
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKvkelKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 427 LRCVQAQEGQLTTSAGLMPLGSqESSDSLAAEIvtpeikEKLIRlQHENKMLKLNQEGSDNEKIALLQSLLDDAnLRKNE 506
Cdd:COG1340 87 LNELREELDELRKELAELNKAG-GSIDKLRKEI------ERLEW-RQQTEVLSPEEEKELVEKIKELEKELEKA-KKALE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 507 LETENRLVNQRLLEVQSQVEELQKSLQE---QGSKAEDSVL-LKKKLEEHLEKLHEANNEIQRKRAIIEDLEPRYNNSSL 582
Cdd:COG1340 158 KNEKLKELRAELKELRKEAEEIHKKIKElaeEAQELHEEMIeLYKEADELRKEADELHKEIVEAQEKADELHEEIIELQK 237
|
250
....*....|
gi 1729156918 583 KIEELQEALR 592
Cdd:COG1340 238 ELRELRKELK 247
|
|
| DUF2046 |
pfam09755 |
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ... |
261-404 |
1.16e-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: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 261 LEAAKDDYRIRCEELEKEIAELRQ----------QNEEL--TTLAEEAQSLKDEMDVLRHSSDKvaKLESQVESYKKKLE 328
Cdd:pfam09755 40 LKMELETYKLRCKALQEENRALRQasvniqakaeQEEEFisNTLLKKIQALKKEKETLAMNYEQ--EEEFLTNDLSRKLT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 329 DLGDLRRQVKLLEEKNTMYMQNTVSLEEELRKA--HAARSQLETYKRQVVELQNRLSEES--------KKADKLEFEYKL 398
Cdd:pfam09755 118 QLRQEKVELEQTLEQEQEYQVNKLMRKIEKLEAetLNKQTNLEQLRREKVELENTLEQEQealvnrlwKRMDKLEAEKRL 197
|
....*.
gi 1729156918 399 LKEKVD 404
Cdd:pfam09755 198 LQEKLD 203
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
156-571 |
1.49e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 156 ELMSKESPVSVGNDAYVDLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALqEEKSSLLAENQILMERLNQSDSIED 235
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEL-EERHELYEEAKAKKEELERLKKRLT 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 236 PNSPagrrhlqlqtqlEQLQEETFRLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSLKDEMDVLRHSSDKVAK 315
Cdd:PRK03918 383 GLTP------------EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHR 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 316 LEsQVESYKKKLEDLgdlRRQVKLLEEKNTMYMQNTVSLEEELRKAHAARSQLETYKrQVVELQNRLSE-ESKKADKLEF 394
Cdd:PRK03918 451 KE-LLEEYTAELKRI---EKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAE-QLKELEEKLKKyNLEELEKKAE 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 395 EYKLLKEKVDGLQKEKDRLRTERDSLKE-------TIEELRCVQAQEGQLTTSAGLMPLGSQESSDSLAAEIVTP----- 462
Cdd:PRK03918 526 EYEKLKEKLIKLKGEIKSLKKELEKLEElkkklaeLEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFyneyl 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 463 ----------EIKEKLIRLQHENKMLKLNQEGSDNE------KIALLQSLLDD---ANLRKNELETENRL--VNQRLLEV 521
Cdd:PRK03918 606 elkdaekeleREEKELKKLEEELDKAFEELAETEKRleelrkELEELEKKYSEeeyEELREEYLELSRELagLRAELEEL 685
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1729156918 522 QSQVEELQKS---LQEQGSKAEDSVLLKKKLEEHLEKLHEANNEIQRKRAIIE 571
Cdd:PRK03918 686 EKRREEIKKTlekLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLK 738
|
|
| 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 1729156918 275 LEKEIAELRQQNEELTTLAEEAQS--LKDEMDVLRHSSDKVAKLESQVEsykkkledlgDLRRQVKLLEEKNTMymqntv 352
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEEreLTEEEEEIRRLEEQVERLEAEVE----------ELEAELEEKDERIER------ 445
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1729156918 353 sLEEELRKahaARSQletykrqvvelQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEEL 427
Cdd:COG2433 446 -LERELSE---ARSE-----------ERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLE 505
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
174-409 |
1.96e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.81 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 174 LDRQLKKTTEELNEALATKEEIAqrcHELDMQVAALQEEKSSLLAENQILMERLnqsDSIEDPNSPAGRRHLQLQTQLEQ 253
Cdd:PLN02939 199 LEEQLEKLRNELLIRGATEGLCV---HSLSKELDVLKEENMLLKDDIQFLKAEL---IEVAETEERVFKLEKERSLLDAS 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 254 LQEETFRLEAAKDDYR----IRCEELEKEIAELRQQNEELTTLAEEAQSLKDEMDVLRhssDKVAKLESQVES---YKKK 326
Cdd:PLN02939 273 LRELESKFIVAQEDVSklspLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLR---DKVDKLEASLKEanvSKFS 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 327 LEDLGDLRRQVKLLEEKNTmymqntvsleeelRKAHAARSQLETYKRQVVELQ---NRLSEESKKadklefeyKLLKEKV 403
Cdd:PLN02939 350 SYKVELLQQKLKLLEERLQ-------------ASDHEIHSYIQLYQESIKEFQdtlSKLKEESKK--------RSLEHPA 408
|
....*.
gi 1729156918 404 DGLQKE 409
Cdd:PLN02939 409 DDMPSE 414
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
260-573 |
2.32e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 260 RLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSLKDEMDVLRHSSDK-VAKLESQV--------ESYKKKLEDL 330
Cdd:pfam01576 409 KLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKdVSSLESQLqdtqellqEETRQKLNLS 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 331 GDLRrqvKLLEEKNTMYMQntvsLEEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDG----- 405
Cdd:pfam01576 489 TRLR---QLEDERNSLQEQ----LEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEAltqql 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 406 ----------------LQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTSAGLMPLGSQESSDSLAAEIVTPEIK---- 465
Cdd:pfam01576 562 eekaaaydklektknrLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRalsl 641
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 466 --------EKLIRLQHENKMLKLNQEGsdnekialLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQEqgs 537
Cdd:pfam01576 642 araleealEAKEELERTNKQLRAEMED--------LVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQA--- 710
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1729156918 538 kAEDSVL--------LKKKLEEHLEKLHEANNEiqRKRAIIEDL 573
Cdd:pfam01576 711 -TEDAKLrlevnmqaLKAQFERDLQARDEQGEE--KRRQLVKQV 751
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
260-616 |
2.43e-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: 41.50 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 260 RLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSLKDEMDVLRHSSDKvaKLESQVESYKKKLEDLGDLRRQVKL 339
Cdd:pfam02463 656 EGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQRE--KEELKKLKLEAEELLADRVQEAQDK 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 340 LEEKNTMYMQNTVSLEEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDS 419
Cdd:pfam02463 734 INEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEE 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 420 LKETIEElrcvqaQEGQLTTSAGLMPLGSQESSDSLAAEIVTPEIKEKLIRLQHENKMLKLNQEGSDNEKIALLQSLLDD 499
Cdd:pfam02463 814 AELLEEE------QLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDE 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 500 anlRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDSVLLKKKLEEHLEKLHEANNEIQRKRAIIEDLEPRYNN 579
Cdd:pfam02463 888 ---LESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKR 964
|
330 340 350
....*....|....*....|....*....|....*..
gi 1729156918 580 SSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVI 616
Cdd:pfam02463 965 LLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLE 1001
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
266-376 |
2.64e-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: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 266 DDYRIRCEELEKEIAELRQQNEELTtlAEEAQSLKDEMDVLRhssDKVAKLESQVESYKKKLEDLGDLRRQvklLEEKNt 345
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEQDEAS--FERLAELRDELAELE---EELEALKARWEAEKELIEEIQELKEE---LEQRY- 484
|
90 100 110
....*....|....*....|....*....|.
gi 1729156918 346 mymQNTVSLEEELRKAHAARSQLETYKRQVV 376
Cdd:COG0542 485 ---GKIPELEKELAELEEELAELAPLLREEV 512
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
260-482 |
3.58e-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: 40.87 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 260 RLEAAKDdyrIRcEELEKEIAELRQQNEELTTLAEEAQSLKDEmdvLRHSSDKVA----KLESQVESYKKKLEDLgdlRR 335
Cdd:pfam15921 644 RLRAVKD---IK-QERDQLLNEVKTSRNELNSLSEDYEVLKRN---FRNKSEEMEtttnKLKMQLKSAQSELEQT---RN 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 336 QVKLLEEKNTMYMQNTVSLEEELRkahAARSQLETYKRQVVELQNRLSEESKkadklefEYKLLKEKVDGLQKEKDRLRT 415
Cdd:pfam15921 714 TLKSMEGSDGHAMKVAMGMQKQIT---AKRGQIDALQSKIQFLEEAMTNANK-------EKHFLKEEKNKLSQELSTVAT 783
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1729156918 416 ERDSLKETIEELRcvqAQEGQLTTSAGLMPLGSQESSDSLAaeivtpEIKEKLIRLQHENKMLKLNQ 482
Cdd:pfam15921 784 EKNKMAGELEVLR---SQERRLKEKVANMEVALDKASLQFA------ECQDIIQRQEQESVRLKLQH 841
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
175-411 |
3.62e-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: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 175 DRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSiedpnspagrrhlqlqtqleql 254
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA---------------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 255 qeetfRLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAE--EAQSLKDEMDvlrhssdKVAKLESQVESYKKKLEDLGD 332
Cdd:COG3883 73 -----EIAEAEAEIEERREELGERARALYRSGGSVSYLDVllGSESFSDFLD-------RLSALSKIADADADLLEELKA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1729156918 333 LRRQVKLLEEKntmymqntvsLEEELRKAHAARSQLETYKRqvvELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKD 411
Cdd:COG3883 141 DKAELEAKKAE----------LEAKLAELEALKAELEAAKA---ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
260-555 |
3.71e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.86 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 260 RLEAAKDDYRIRCEELEKEIAELRQQN----------EELTTLAEEAQSLKDEMDVLRHSSDKVAKLESQVESYKKKLE- 328
Cdd:pfam05483 371 RLEKNEDQLKIITMELQKKSSELEEMTkfknnkevelEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREk 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 329 DLGDLRRQVKLLEEKNTMYMQNTVSLEEELRKAHAARSQLETYKRQVVELQNRLSEEskkADKLEFEYKLLKEKVDGLQK 408
Cdd:pfam05483 451 EIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQE---ASDMTLELKKHQEDIINCKK 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 409 EKDRLRTERDSLKET----IEELRCVQAQEGQLTTSAGLMPLGSQESSDSLAAEIVTPEIKEKLIRLQHENKMLKLNQEG 484
Cdd:pfam05483 528 QEERMLKQIENLEEKemnlRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKN 607
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1729156918 485 SDNEKIALLQSLLDDANLRKN-ELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDSVLLKKKLEEHLEK 555
Cdd:pfam05483 608 KNIEELHQENKALKKKGSAENkQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEK 679
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
139-666 |
3.97e-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: 40.82 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 139 IMMMEESVQHVVMTAIQELMSK----ESPVSVGNDAYVDLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKS 214
Cdd:TIGR02169 281 IKDLGEEEQLRVKEKIGELEAEiaslERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYA 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 215 SLLAENQILMERLNQSDSiedpnsPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAE 294
Cdd:TIGR02169 361 ELKEELEDLRAELEEVDK------EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEA 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 295 EAQSLKDEMDVLRhssDKVAKLESQVESYKkklEDLGDLRRQVKLLEEKNTMYMQNTVSLEEELRKAHAARSQLETYKRQ 374
Cdd:TIGR02169 435 KINELEEEKEDKA---LEIKKQEWKLEQLA---ADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 375 vvelqNRLSEESKKAD------------KLEFEYKLLKEKVDGLQKEKDRLRTERDSlKETIEELRCVQAqeGQLTtsag 442
Cdd:TIGR02169 509 -----GRAVEEVLKASiqgvhgtvaqlgSVGERYATAIEVAAGNRLNNVVVEDDAVA-KEAIELLKRRKA--GRAT---- 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 443 LMPLGSQESSDSLAAEIVTPEIKEKLI------------------------------RLQHENKMLKLNQE--------- 483
Cdd:TIGR02169 577 FLPLNKMRDERRDLSILSEDGVIGFAVdlvefdpkyepafkyvfgdtlvvedieaarRLMGKYRMVTLEGElfeksgamt 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 484 -GSDNEKIALLQSLLDDANL-----RKNELETENRLVNQRLLEVQSQVEELQKSLQEqgskaedsvlLKKKLEEHLEKLH 557
Cdd:TIGR02169 657 gGSRAPRGGILFSRSEPAELqrlreRLEGLKRELSSLQSELRRIENRLDELSQELSD----------ASRKIGEIEKEIE 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 558 EANNEIQRKRAIIEDLEPRYNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGTAPEIQALKNQ 637
Cdd:TIGR02169 727 QLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEE 806
|
570 580
....*....|....*....|....*....
gi 1729156918 638 LQERDRMFHSLEKEYEKTKTQREMEEKFI 666
Cdd:TIGR02169 807 VSRIEARLREIEQKLNRLTLEKEYLEKEI 835
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
273-458 |
4.50e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 273 EELEKEIAELRQQNEELTTLAEEAQSLKDEMDVLRHSSDKV-AKLESQVESYKKKLEDLGDLRRQVK-----------LL 340
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLqAEIAEAEAEIEERREELGERARALYrsggsvsyldvLL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 341 EEKNT------MYMQNTVSL--EEELRKAHAARSQLETYKRQVVELQNRLSEeskKADKLEFEYKLLKEKVDGLQKEKDR 412
Cdd:COG3883 110 GSESFsdfldrLSALSKIADadADLLEELKADKAELEAKKAELEAKLAELEA---LKAELEAAKAELEAQQAEQEALLAQ 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1729156918 413 LRTERDSLKETIEELRCVQAQEGQLTTSAGLMPLGSQESSDSLAAE 458
Cdd:COG3883 187 LSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
360-660 |
4.69e-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: 40.49 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 360 KAHAARSqLETYKRQVVELQNRLSEESKKADKLEFEYKL----LKEKVDGLQKEKDRL----RTE-------RDSLKETI 424
Cdd:pfam15921 73 KEHIERV-LEEYSHQVKDLQRRLNESNELHEKQKFYLRQsvidLQTKLQEMQMERDAMadirRREsqsqedlRNQLQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 425 EELRCVQA-QEGQLTTSAGLMplgSQESSDSLAAEIVTPEIKEKLIRLQhENKMLKLNQEgsDNEKIALLQSLLDDANLR 503
Cdd:pfam15921 152 HELEAAKClKEDMLEDSNTQI---EQLRKMMLSHEGVLQEIRSILVDFE-EASGKKIYEH--DSMSTMHFRSLGSAISKI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 504 KNELETENRLVNQRLLEVQSQVEELQkslQEQGSKAEdsvLLKKKLEEHLEKL---HEAN---------------NEIQR 565
Cdd:pfam15921 226 LRELDTEISYLKGRIFPVEDQLEALK---SESQNKIE---LLLQQHQDRIEQLiseHEVEitgltekassarsqaNSIQS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 566 KRAIIEDLEPRYNNSSLK--------IEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQgTAPEIQALKNQ 637
Cdd:pfam15921 300 QLEIIQEQARNQNSMYMRqlsdlestVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQ-FSQESGNLDDQ 378
|
330 340
....*....|....*....|...
gi 1729156918 638 LQERDRMFHSLEKEYEKTKTQRE 660
Cdd:pfam15921 379 LQKLLADLHKREKELSLEKEQNK 401
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
273-422 |
6.01e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 273 EELEKEIAELRQQNEELTTLA-------EEAQSLKDEMDVLRHSSDKVAKLESQVESYKKKLEDLgdlrrQVKLLEEKNT 345
Cdd:PRK03918 588 EELEERLKELEPFYNEYLELKdaekeleREEKELKKLEEELDKAFEELAETEKRLEELRKELEEL-----EKKYSEEEYE 662
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1729156918 346 MYMQNTVSLEEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKE 422
Cdd:PRK03918 663 ELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKE 739
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
493-591 |
6.28e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.28 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 493 LQSLLDDANLRKnELETENRLVNQRLLEVQSQVEELQKSLQeqgskaeDSVLLKKKLEEHLEKLHEANNEIQR-KRAIIE 571
Cdd:PRK11281 41 VQAQLDALNKQK-LLEAEDKLVQQDLEQTLALLDKIDRQKE-------ETEQLKQQLAQAPAKLRQAQAELEAlKDDNDE 112
|
90 100
....*....|....*....|
gi 1729156918 572 DLEPRYNNSSLKieELQEAL 591
Cdd:PRK11281 113 ETRETLSTLSLR--QLESRL 130
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
176-393 |
6.92e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 6.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 176 RQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNqsdsiedpnspagrrhlqlqtqleqlq 255
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID--------------------------- 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 256 eetfrLEAAKDdyriRCEELEKEIAELRQQNEELTTLAEEAQSLKDEMDVLRhssDKVAKLESQVESYKKKLEDLGDLRR 335
Cdd:COG4913 663 -----VASAER----EIAELEAELERLDASSDDLAALEEQLEELEAELEELE---EELDELKGEIGRLEKELEQAEEELD 730
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1729156918 336 QVKLLEEKNTMYMQNTVSLEEELRKAHAARSQLETYKRQvvELQNRLSEESKKADKLE 393
Cdd:COG4913 731 ELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRE--NLEERIDALRARLNRAE 786
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
458-589 |
6.96e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.91 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 458 EIVTP-EIKEKLIRLQHENKMLKLN--QEGSDNEKIALLQSLLDDANLRKNELET---ENRLVNQRLLEVQSQ-VEELQK 530
Cdd:PRK05771 10 LIVTLkSYKDEVLEALHELGVVHIEdlKEELSNERLRKLRSLLTKLSEALDKLRSylpKLNPLREEKKKVSVKsLEELIK 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1729156918 531 SLQEQGSKAEDSVllkkklEEHLEKLHEANNEIQRKRAIIEDLEPrYNNSSLKIEELQE 589
Cdd:PRK05771 90 DVEEELEKIEKEI------KELEEEISELENEIKELEQEIERLEP-WGNFDLDLSLLLG 141
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
263-554 |
8.98e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.51 E-value: 8.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 263 AAKDDYRIRCEELEKEIA----ELRQQNEELTTLAEEAQSLKDEmdvlRHSSDKVAKLESQVEsykKKLEDLGDLrrqvk 338
Cdd:PRK11281 73 DKIDRQKEETEQLKQQLAqapaKLRQAQAELEALKDDNDEETRE----TLSTLSLRQLESRLA---QTLDQLQNA----- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 339 lleekntmymQNTVSleeelrkahAARSQLETYKRQVVELQNRLSEESKKadklefeykllkekvdgLQKEKDRLRTERD 418
Cdd:PRK11281 141 ----------QNDLA---------EYNSQLVSLQTQPERAQAALYANSQR-----------------LQQIRNLLKGGKV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156918 419 SLKETIEELRcvqaqegqlttsaglmplgsqessDSLAAEIVtpeikekLIRLQheNKMLKLNQEGSdNEKIALLQSLLD 498
Cdd:PRK11281 185 GGKALRPSQR------------------------VLLQAEQA-------LLNAQ--NDLQRKSLEGN-TQLQDLLQKQRD 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1729156918 499 DANLRKNELETENRL----VNQ-RLLEVQSQVEELQKslQEQGSKAEDSVLLKKKLEEHLE 554
Cdd:PRK11281 231 YLTARIQRLEHQLQLlqeaINSkRLTLSEKTVQEAQS--QDEAARIQANPLVAQELEINLQ 289
|
|
| |
