|
Name |
Accession |
Description |
Interval |
E-value |
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
184-711 |
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: 676.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 184 ELNEALSAKEEIAQRCHELDLQVAALQEEKSSLLAENQVLMERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQEETFRLEA 263
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 264 AKDDYRIRCEELEKEISELRQQNDELTTLADDAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKLLEEK 343
Cdd:pfam05622 81 ARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLGDLRRQVKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 344 NTMYMQNTVSLEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRSERDSLKET 423
Cdd:pfam05622 161 NAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRET 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 424 IEELRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKINQEGSDNEKIALLQSLLDDANLRK 503
Cdd:pfam05622 241 NEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLGQEGSYRERLTELQQLLEDANRRK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 504 NELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDaiSVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFN-NSS 582
Cdd:pfam05622 321 NELETQNRLANQRILELQQQVEELQKALQEQGSKAED--SSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDsNLA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 583 LKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQLQERDRQFHSLEKEYEKTKSQREM 662
Cdd:pfam05622 399 QKIDELQEALRKKDEDMKAMEERYKKYVEKAKSVIKTLDPKQNPASPPEIQALKNQLLEKDKKIEHLERDFEKSKLQREQ 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2090181558 663 EEKYIVSAWYNMGMTLHKKAAEDRLASTGS-GQSFLARQRQATSTRRSYP 711
Cdd:pfam05622 479 EEKLIVTAWYNMGMALHRKAIEERLAGLSSpGQSFLARQRQATNARRGLS 528
|
|
| HkD_Hook3 |
cd22226 |
Hook domain found in protein Hook 3 (Hook3) and similar proteins; Hook3 is an adaptor protein ... |
8-160 |
2.39e-102 |
|
Hook domain found in protein Hook 3 (Hook3) and similar proteins; Hook3 is an adaptor protein for microtubule-dependent intracellular vesicle and protein trafficking. It is involved in Golgi and endosome transport. It acts as a scaffold for the opposite-polarity microtubule-based motors cytoplasmic dynein-1 and the kinesin KIF1C. It may participate in the turnover of the endocytosed scavenger receptor. Hook3 is a component of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex.
Pssm-ID: 411797 Cd Length: 153 Bit Score: 309.98 E-value: 2.39e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 8 ERAELCESLLTWIQTFNVDAPCQTVEDLTNGVVMAQVLQKIDPVYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYN 87
Cdd:cd22226 1 DRAELCESLLTWIQTFNVDAPCQTVEDLTSGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2090181558 88 HEILGQQINDFTLPDVNLIAEHSDAAELGRMLQLILGCAVNCEQKQEYIQAIMVMEESVQHVVMTAIQELMSK 160
Cdd:cd22226 81 HEILGQQINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMSK 153
|
|
| HOOK_N |
pfam19047 |
HOOK domain; This domain is found at the N-terminus of HOOK proteins. |
11-161 |
2.63e-95 |
|
HOOK domain; This domain is found at the N-terminus of HOOK proteins.
Pssm-ID: 465958 Cd Length: 151 Bit Score: 291.62 E-value: 2.63e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 11 ELCESLLTWIQTFNVDAPCQTVEDLTNGVVMAQVLQKIDPVYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEI 90
Cdd:pfam19047 1 ELCDSLLTWLQTFNVPAPCATVEDLTDGVAMAQVLHQIDPSWFTEAWLSRIKEDVGDNWRLKVSNLKKILQSVVDYYQDV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2090181558 91 LGQQINDFTLPDVNLIAEHSDAAELGRMLQLILGCAVNCEQKQEYIQAIMVMEESVQHVVMTAIQELMSKE 161
Cdd:pfam19047 81 LGQQISDFLLPDVNLIGEHSDPAELGRLLQLILGCAVNCEKKQEYIQQIMTLEESVQHVVMTAIQELMSKD 151
|
|
| HkD_Hook |
cd22222 |
Hook domain found in Hook family of microtubule-binding proteins; The Hook family includes ... |
13-159 |
2.95e-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: 2.95e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 13 CESLLTWIQTFNVDAPCQTVEDLTNGVVMAQVLQKIDPVYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEILG 92
Cdd:cd22222 1 CDSLLQWLQTFNLIAPHATAEDLSDGVAIAQVLNQIDPEYFSDSWLSKIKPDVGDNWRLKVSNLKKILKGIVDYYSEVLG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2090181558 93 QQINDFTLPDVNLIAEHSDAAELGRMLQLILGCAVNCEQKQEYIQAIMVMEESVQHVVMTAIQELMS 159
Cdd:cd22222 81 QQISGFTMPDVNAIAEKEDPKELGRLLQLVLGCAVNCERKEEYIQAIMGLEESVQHVVMEAIQELMS 147
|
|
| HkD_Hook1 |
cd22225 |
Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a ... |
12-161 |
3.22e-82 |
|
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: 257.47 E-value: 3.22e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 12 LCESLLTWIQTFNVDAPCQTVEDLTNGVVMAQVLQKIDPVYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEIL 91
Cdd:cd22225 1 LCDSLIIWLQTFNTAAPCQTVQDLTSGVAMAQVLHQIDSSWFDESWLSRIKEDVGDNWRIKMSNLKKILQGIVDYYHEFL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 92 GQQINDFTLPDVNLIAEHSDAAELGRMLQLILGCAVNCEQKQEYIQAIMVMEESVQHVVMTAIQELMSKE 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 |
5.44e-71 |
|
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: 5.44e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 11 ELCESLLTWIQTFNVDAPCQTVEDLTNGVVMAQVLQKIDPVYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEI 90
Cdd:cd22227 1 ELCDSLLTWLQTFQVPSPCSSYQDLTSGVAIAQVLNRIDPSWFNEAWLGRIKEDTGDNWRLKVSNLKKILQSLLEYYQDV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 91 LGQQINDFTLPDVNLIAEHSDAAELGRMLQLILGCAVNCEQKQEYIQAIMVMEESVQHVVMTAIQELMSK 160
Cdd:cd22227 81 LGHQVSEDHLPDVNLIGEFSDDTELGKLLQLVLGCAISCEKKQEHIQQIMTLEESVQHVVMEAIQELLTK 150
|
|
| HkD_SF |
cd22211 |
Hook domain-containing proteins superfamily; The Hook domain superfamily includes Hook adaptor ... |
14-159 |
2.34e-55 |
|
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: 185.94 E-value: 2.34e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 14 ESLLTWIQTFNVDAPCQTVEDLTNGVVMAQVLQKIDPVYFDENWLNriKTEVGDNWRLKISNLKKILKGILDYNHEILGQ 93
Cdd:cd22211 2 AALLAWINTFPLSSPVESLDDLSDGVVLAEILSQIDPSYFDSEWLE--SRDSSDNWVLKLNNLKKLYRSLSKYYREVLGQ 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2090181558 94 QINDFTLPDVNLIAEHSDAAELGRMLQLILGCAVNCEQKQEYIQAIMVMEESVQHVVMTAIQELMS 159
Cdd:cd22211 80 QLSDLPLPDLSAIARDGDEEEIVKLLELVLGAAVQCENKEEYIARIQQLDESTQAELMLIIQEVLE 145
|
|
| HkD_HkRP |
cd22223 |
Hook domain found in the Hook-related protein (HkRP) family; The HkRP family includes Daple, ... |
12-157 |
3.00e-24 |
|
Hook domain found in the Hook-related protein (HkRP) family; The HkRP family includes Daple, Girdin and Gipie. Daple, also called Dvl-associating protein with a high frequency of leucine residues, or coiled-coil domain-containing protein 88C (CCDC88C), or Hook-related protein 2 (HkRP2), is a novel non-receptor nucleotide exchange factor (GEF) required for activation of guanine nucleotide-binding proteins (G-proteins) during non-canonical Wnt signaling. Girdin, also called Akt phosphorylation enhancer (APE), or coiled-coil domain-containing protein 88A (CCDC88A), or G alpha-interacting vesicle-associated protein (GIV), or Girders of actin filament, or Hook-related protein 1 (HkRP1), is a bifunctional modulator of guanine nucleotide-binding proteins (G proteins). It acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein G(i) alpha subunits. It also acts as a guanine nucleotide dissociation inhibitor for guanine nucleotide-binding protein G(s) subunit alpha GNAS. In addition, Girdin plays an essential role in cell migration. Gipie, also called GRP78-interacting protein induced by ER stress, or coiled-coil domain-containing protein 88B (CCDC88B), or brain leucine zipper domain-containing protein, or Hook-related protein 3 (HkRP3), is a novel actin cytoskeleton-binding protein and Akt substrate that regulates cell migratory responses in various biological contexts. It acts as a positive regulator of T-cell maturation and inflammatory function. As a microtubule-binding protein, Gipie regulates lytic granule clustering and NK cell killing. All family members contain a conserved globular Hook domain which folds as a variant of the helical calponin homology (CH) domain.
Pssm-ID: 411794 Cd Length: 149 Bit Score: 99.20 E-value: 3.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 12 LCESLLTWIQTFNVDAPCQ-TVEDLTNGVVMAQVLQKIDPVYFDEnwlnRIKTEVGDNWRLKISNLKKILKGILDYNHEI 90
Cdd:cd22223 2 LSSPLVTWAKTFADDGSAElSYTDLVDGVFLNNVMLQIDPRPFSE----VSNRNVDDDVNARIQNLDLLLRNIKSFYQEV 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2090181558 91 LGQQINdFTLPDVNLIAEHSDA----AELGRMLQLILGCAVNCEQKQEYIQAIMVMEESVQHVVMTAIQEL 157
Cdd:cd22223 78 LQQLIV-MKLPDILTIGREPESeqslEELEKLLLLLLGCAVQCERKEEFIERIKNLDLEVQHALVACIQEV 147
|
|
| HkD_Daple |
cd22228 |
Hook domain found in Daple (Dvl-associating protein with a high frequency of leucine residues) ... |
16-157 |
4.52e-16 |
|
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: 76.12 E-value: 4.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 16 LLTWIQTFnvdAPC--------QTVEDLTNGVVMAQVLQKIDPVYFDEnwlnRIKTEVGDNWRLKISNLKKILKGILDYN 87
Cdd:cd22228 6 LVTWVKTF---GPLgfgsedklSMYMDLVDGVFLNKIMLQIDPRPTNQ----RVNKHVNNDVNLRIQNLTILVRHIKTYY 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2090181558 88 HEILgQQINDFTLPDVNLIAEH----SDAAELGRMLQLILGCAVNCEQKQEYIQAIMVMEESVQHVVMTAIQEL 157
Cdd:cd22228 79 QEVL-QQLIVMNLPNVLMIGKDplsgKSMEEIKKMLLLVLGCAVQCERKEEFIERIKQLDIETQAAIVSHIQEV 151
|
|
| HkD_Girdin |
cd22229 |
Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation ... |
16-157 |
5.95e-12 |
|
Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation enhancer (APE), or coiled-coil domain-containing protein 88A (CCDC88A), or G alpha-interacting vesicle-associated protein (GIV), or Girders of actin filament, or Hook-related protein 1 (HkRP1), is a bifunctional modulator of guanine nucleotide-binding proteins (G proteins). It acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein G(i) alpha subunits. It also acts as a guanine nucleotide dissociation inhibitor for guanine nucleotide-binding protein G(s) subunit alpha GNAS. In addition, Girdin plays an essential role in cell migration.
Pssm-ID: 411800 Cd Length: 156 Bit Score: 64.04 E-value: 5.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 16 LLTWIQTFNVDAPCQTVE-----DLTNGVVMAQVLQKIDPvyfdENWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEI 90
Cdd:cd22229 9 LVTWVKTFGPLATGNGTPldeyvALVDGVFLNEVMLQINP----KSSNQRVNKKVNNDASLRIQNLSILVKQIKLYYQET 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2090181558 91 LgQQINDFTLPDV-----NLIAEHSdAAELGRMLQLILGCAVNCEQKQEYIQAIMVMEESVQHVVMTAIQEL 157
Cdd:cd22229 85 L-QQLIMMSLPNVlvlgrNPLSEQG-TEEMKKLLLLLLGCAVQCERKEEFIERIQTLDFDTKAAVAAHIQEV 154
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
260-593 |
2.49e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.39 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 260 RLEAAKDDYRIRCEELEKEISELRQQNDELTTLADDAQSLKDEIDVLRHSSDK-VSKLEGQVESYKKKLEDL----GDLR 334
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdLARLEAEVEQLEERIAQLskelTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 335 RQVKLLEEKNTMYMQNTVSLEEEL----RKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEK 410
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIeeleAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 411 DRLRSERDSLKETIEELRCVQAQEGQLTTQglmplgSQESSDSLAAEIVTPEIREKLIRLQHENKMLKINQEGSDN---- 486
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEE------LESELEALLNERASLEEALALLRSELEELSEELRELESKRselr 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 487 EKIALLQSLLDDANLRKNELETENRLVNQRLLEVQS----QVEELQKSLQDQGSKAEDAIsvllkKKLEEHLEKLHEANN 562
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSltleEAEALENKIEDDEEEARRRL-----KRLENKIKELGPVNL 989
|
330 340 350
....*....|....*....|....*....|...
gi 2090181558 563 ElqkkrAI--IEDLEPRFNNSSLKIEELQEALR 593
Cdd:TIGR02168 990 A-----AIeeYEELKERYDFLTAQKEDLTEAKE 1017
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
130-665 |
2.78e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.01 E-value: 2.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 130 EQKQEYIQAIMVMEESVQHVVMTAIQELMSKESPVSAGNDAYVDLDRQLKKTSEELNEALSAKEEIAqrchELDLQVAAL 209
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIE----ELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 210 QEEKSSLLAENQVLMERLNQSDS-IEDPNSPAGR---------RHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEI 279
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKeIEELEEKVKElkelkekaeEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 280 SELRQQNDELTTLADDAQSLKDEIDVLRHSS---DKVSKLEGQVESYKKKLEDL--GDLRRQVKLLEEKNTmymqntvSL 354
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEELEERHelyEEAKAKKEELERLKKRLTGLtpEKLEKELEELEKAKE-------EI 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 355 EEELRKANAARSQLETYKRQVVELQNRLSEESKK----ADKLDFEYK-----RLKEKVDSLQKEKDRLRSERDSLKETIE 425
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcGRELTEEHRkelleEYTAELKRIEKELKEIEEKERKLRKELR 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 426 ELRCVQAQEGQLTTQGLM---------PLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKinqegSDNEKIALLQSLL 496
Cdd:PRK03918 484 ELEKVLKKESELIKLKELaeqlkeleeKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLK-----KELEKLEELKKKL 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 497 DDANLRKNELETENRLVNQRLLEVQ-SQVEELQKSLQDQGSKAEDAISVL-LKKKLEEHLEKLHEANNELQKKRAIIEDL 574
Cdd:PRK03918 559 AELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKdAEKELEREEKELKKLEEELDKAFEELAET 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 575 EPRFNNSSLKIEELQealrkKEEEMKQMEERYKKYLEKAKSVirtldpkqnQGAAPEIQALKNQLQERDRQFHSLEKEYE 654
Cdd:PRK03918 639 EKRLEELRKELEELE-----KKYSEEEYEELREEYLELSREL---------AGLRAELEELEKRREEIKKTLEKLKEELE 704
|
570
....*....|.
gi 2090181558 655 KTKSQREMEEK 665
Cdd:PRK03918 705 EREKAKKELEK 715
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
260-635 |
4.80e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 4.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 260 RLEAAKDDY---RIRCEELEKEISELRQQndelttlADDA---QSLKDEIDVLrhssdkvsKLEGQVESYKKKLEDLGDL 333
Cdd:COG1196 180 KLEATEENLerlEDILGELERQLEPLERQ-------AEKAeryRELKEELKEL--------EAELLLLKLRELEAELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 334 RRQVKLLEEKNTMYMQNTVSLEEELRKANAARSQLEtykRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRL 413
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELE---LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 414 RSERDSLKETIEELrcvQAQEGQLTTQGLMplgSQESSDSLAAEIVtpEIREKLIRLQHENKMLKINQEGSDNEKIALLQ 493
Cdd:COG1196 322 EEELAELEEELEEL---EEELEELEEELEE---AEEELEEAEAELA--EAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 494 SLLDDANLRKNELETENRLvNQRLLEVQSQVEELQKSLQDQGSKAEDAisvllKKKLEEHLEKLHEANNELQKKRAIIED 573
Cdd:COG1196 394 AAAELAAQLEELEEAEEAL-LERLERLEEELEELEEALAELEEEEEEE-----EEALEEAAEEEAELEEEEEALLELLAE 467
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2090181558 574 LEPRFNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQAL 635
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL 529
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
153-641 |
1.38e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.68 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 153 AIQELMSKESPVSAGNDAYVDLDRQLKKTSEELNEALSAKEEIAQRCHELDLQVAALQEEKSSLLAENQVLMERLNQSDS 232
Cdd:PRK02224 207 RLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 233 IEDpnspagrrhlqlqtqleqlqeetfRLEAAKDDYRIRCEELEKEISELRQQNDELTtlaDDAQSLKDEIDVLRHSsdk 312
Cdd:PRK02224 287 RLE------------------------ELEEERDDLLAEAGLDDADAEAVEARREELE---DRDEELRDRLEECRVA--- 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 313 VSKLEGQVESYKKKLEDLgdlrrqvkllEEKNTMYMQNTVSLEEELRkanAARSQLETYKRQVVELQNRLSEESKKADKL 392
Cdd:PRK02224 337 AQAHNEEAESLREDADDL----------EERAEELREEAAELESELE---EAREAVEDRREEIEELEEEIEELRERFGDA 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 393 DFEYKRLKEKVDSLQKEKDRLRSERDSLKETIEELRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTpEIREKLIRLQH 472
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIE-EDRERVEELEA 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 473 ENKMLKINQEGSDN--EKIALLQSLLDDANLRKNELETENRLVNQR---LLEVQSQVEELQKSLQDQGSKAEDAISVLLK 547
Cdd:PRK02224 483 ELEDLEEEVEEVEErlERAEDLVEAEDRIERLEERREDLEELIAERretIEEKRERAEELRERAAELEAEAEEKREAAAE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 548 KKL--EEHLEKLHEANNELQKKRAIIEDLEpRFNNSSLKIEELQ---EALRKKEEEMKQMEERYKKYLEKAKSVIRTLDP 622
Cdd:PRK02224 563 AEEeaEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEdeiERLREKREALAELNDERRERLAEKRERKRELEA 641
|
490
....*....|....*....
gi 2090181558 623 KQNQGAAPEIQALKNQLQE 641
Cdd:PRK02224 642 EFDEARIEEAREDKERAEE 660
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
371-661 |
1.51e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.69 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 371 YKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDR------LRSERDSLKETIEELRCVQAQEGQLTTQGLMp 444
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKaerykeLKAELRELELALLVLRLEELREELEELQEEL- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 445 LGSQESSDSLAAEIVTPEIREKLIRLQHenkmlkinqeGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQV 524
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEV----------SELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 525 EELQKSLQDQGSKAED--AISVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLKIEELQEALRKKEEEMKQM 602
Cdd:TIGR02168 319 EELEAQLEELESKLDElaEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2090181558 603 EERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQLQERDRQFHSLEKEYEKTKSQRE 661
Cdd:TIGR02168 399 NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE 457
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
153-657 |
2.24e-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: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 153 AIQELMSKESPVSAGNDAYVDLDRQLKKTSEELNEALSAKEEIAQRCHELDLQVAALQEEKSSLLAENQVLMERLNQSds 232
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL-- 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 233 iEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADDAQ----SLKDEIDVLRH 308
Cdd:TIGR02168 315 -ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEeqleTLRSKVAQLEL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 309 ssdKVSKLEGQVESYKKKLEDLGdlRRQVKLLEEkntmymQNTVSLEEELRKANAARSQLETYKRQVVELQNRLSEESKK 388
Cdd:TIGR02168 394 ---QIASLNNEIERLEARLERLE--DRRERLQQE------IEELLKKLEEAELKELQAELEELEEELEELQEELERLEEA 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 389 ADKLDFEYKRLKEKVDSLQKEKDRLRSERDSLKETIEELRCVQAQEGQLTTQ-----GLMPLGSQ----ESSDSLAAEIV 459
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNqsglsGILGVLSElisvDEGYEAAIEAA 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 460 TPEIREKLI---------------------------------RLQHENKMLKINQEG----------SDNEKIALLQSLL 496
Cdd:TIGR02168 543 LGGRLQAVVvenlnaakkaiaflkqnelgrvtflpldsikgtEIQGNDREILKNIEGflgvakdlvkFDPKLRKALSYLL 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 497 ---------DDANLRKNELETENRLV--------------------NQRLLEVQSQVEELQKSLQDQGSKAEDaisvlLK 547
Cdd:TIGR02168 623 ggvlvvddlDNALELAKKLRPGYRIVtldgdlvrpggvitggsaktNSSILERRREIEELEEKIEELEEKIAE-----LE 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 548 KKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLKIEEL---QEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQ 624
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLeaeVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777
|
570 580 590
....*....|....*....|....*....|....*....
gi 2090181558 625 NQGAA------PEIQALKNQLQERDRQFHSLEKEYEKTK 657
Cdd:TIGR02168 778 AEAEAeieeleAQIEQLKEELKALREALDELRAELTLLN 816
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
260-577 |
2.50e-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: 63.92 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 260 RLEAAKDDYrircEELEKEISELRQQNDELTTLADDAQSLKDEIDVLRHS-SDKVSKLEGQVESYKKKLEDL-GDLRRQV 337
Cdd:TIGR02168 233 RLEELREEL----EELQEELKEAEEELEELTAELQELEEKLEELRLEVSElEEEIEELQKELYALANEISRLeQQKQILR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 338 KLLEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRSER 417
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 418 DSLKETIEelrcvqaqegqlttqglmplgsqessdSLAAEIVtpEIREKLIRLQHENKMLKINQEGSDNE----KIALLQ 493
Cdd:TIGR02168 389 AQLELQIA---------------------------SLNNEIE--RLEARLERLEDRRERLQQEIEELLKKleeaELKELQ 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 494 SLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDAISVL-LKKKLEEHLEKLHEANNELQKKRAIIE 572
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLdSLERLQENLEGFSEGVKALLKNQSGLS 519
|
....*
gi 2090181558 573 DLEPR 577
Cdd:TIGR02168 520 GILGV 524
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
328-592 |
2.62e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.93 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 328 EDLGDLRRQVKLLEEKntmymqntvsLEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQ 407
Cdd:TIGR02169 681 ERLEGLKRELSSLQSE----------LRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 408 KEKDRLRSERDSLKETIEELRCVQAQ-EGQLTTQGLMPLGS-----QESSDSLAAEIVtpEIREKLIRLQHENKMLKINQ 481
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELEEDLHKlEEALNDLEARLSHSripeiQAELSKLEEEVS--RIEARLREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 482 EGSDnEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDaisvlLKKKLEEHLEKLHEAN 561
Cdd:TIGR02169 829 EYLE-KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD-----LKKERDELEAQLRELE 902
|
250 260 270
....*....|....*....|....*....|.
gi 2090181558 562 NELQKKRAIIEDLEPRFNNSSLKIEELQEAL 592
Cdd:TIGR02169 903 RKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
173-664 |
2.50e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 173 DLDRQLKKTSEELNEALSAKEEIAQRCHELDLQVAALQEEKSSLLAEnqvLMERLNQSDSIEDPNSPAGRRHLQLQTQLE 252
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE---LARLEQDIARLEERRRELEERLEELEEELA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 253 QLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADDAQSLKDEI--DVLRHSSDKVSKLEGQVESYKKKLEDL 330
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAeeELEELAEELLEALRAAAELAAQLEELE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 331 GDLRRQVKLLEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEK 410
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 411 DRLRSERDSLKETIEE----LRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPE---------IREKLIRLQHENKML 477
Cdd:COG1196 487 AEAAARLLLLLEAEADyegfLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAalaaalqniVVEDDEVAAAAIEYL 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 478 KINQEGsdneKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDAISVLLKKKLEEHLEKL 557
Cdd:COG1196 567 KAAKAG----RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTL 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 558 HEANNELQKKRAIIEDLEPRFNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKN 637
Cdd:COG1196 643 AGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELE 722
|
490 500
....*....|....*....|....*..
gi 2090181558 638 QLQERDRQFHSLEKEYEKTKSQREMEE 664
Cdd:COG1196 723 EEALEEQLEAEREELLEELLEEEELLE 749
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
174-471 |
4.06e-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: 57.00 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 174 LDRQLKKTSEELNEALSAKEEIAQRCHELDLQVAALQEEKSSLLAENQVLMERLNQSDsiedpnspagRRHLQLQTQLEQ 253
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK----------ERLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 254 LQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTtlADDAQSLKDEI-DVLRHSSDKVSKLEGQVESYKKKLEDLgD 332
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE--ARLSHSRIPEIqAELSKLEEEVSRIEARLREIEQKLNRL-T 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 333 LRRQvkLLEEKntmyMQNTVSLEEELR-KANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKD 411
Cdd:TIGR02169 826 LEKE--YLEKE----IQELQEQRIDLKeQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2090181558 412 RLRSERDSLKETIEELRC--------VQAQEGQLTTQG-LMPLGSQESSDSLAAEIVTPEIREKLIRLQ 471
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKrlselkakLEALEEELSEIEdPKGEDEEIPEEELSLEDVQAELQRVEEEIR 968
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
355-670 |
4.91e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 4.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 355 EEELRKANAARSQLETYKRQVVEL---QNRLSEESKKADKldfeYKRLKEKVDSLQK-----EKDRLRSERDSLKETIEE 426
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELerqLKSLERQAEKAER----YKELKAELRELELallvlRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 427 LrcvqaqegqlttqglmplgsQESSDSLAAEIVTPEIREKLIRLQHenkmlkinqeGSDNEKIALLQSLLDDANLRKNEL 506
Cdd:TIGR02168 251 A--------------------EEELEELTAELQELEEKLEELRLEV----------SELEEEIEELQKELYALANEISRL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 507 ETENRLVNQRLLEVQSQVEELQKSLQDqgskaedaisvlLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLKIE 586
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEE------------LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 587 ELQEALRKKEEEMKQMEERYKKYLEkaksvirtldpkqnqgaapEIQALKNQLQERDRQFHSLEKEYEKTKSQREMEEKY 666
Cdd:TIGR02168 369 ELESRLEELEEQLETLRSKVAQLEL-------------------QIASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429
|
....
gi 2090181558 667 IVSA 670
Cdd:TIGR02168 430 LEEA 433
|
|
| HkD_Gipie |
cd22230 |
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar ... |
35-157 |
7.26e-08 |
|
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: 52.53 E-value: 7.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 35 LTNGVVMAQVLQKIDPVYFDENWLNRikteVGDNWRLKISNLKKILKGILDYNHEILgQQINDFTLPDVNLIAEH----S 110
Cdd:cd22230 47 LSNGDLLNRVMGIIDPSPRGGPRMRG----DDGPAAHRVQNLHILWGRLRDFYQEEL-QQLILSPPPDLQVMGRDpfteE 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2090181558 111 DAAELGRMLQLILGCAVNCEQKQEYIQAIMVMEESVQHVVMTAIQEL 157
Cdd:cd22230 122 AVQELEKLLRLLLGAAVQCERRELFIRHIQGLDLDVQAELAEAIQEV 168
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
184-470 |
1.66e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 184 ELNEALSAKEEIAQRCHELDLQVAALQEEKSSLlaeNQVLMERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQEETFRLEA 263
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEEL---EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 264 AKDDYRIRCEELEKEISELRQQ----NDELTTLADDAQSLKDEIDVLRHSSDKVSKLEGQV-ESYKKKLEDLGDLRRQVK 338
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEElaeaEAEIEELEAQIEQLKEELKALREALDELRAELTLLnEEAANLRERLESLERRIA 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 339 LLEEKNTMYMQNTVSLEEELRKANAARSQLETY----KRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLR 414
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAAEIEELEELieelESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 415 SERDSLKETIEELRCVQAQ--------------EGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRL 470
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGlevridnlqerlseEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
173-532 |
1.68e-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: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 173 DLDRQLKKTSEELNEALSAKEEIAQRCHELDLQVAALQEEKSSLLaENQVLMERLnqsdsIEDPNSPAGRRHLQLQTQLE 252
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEK-----REYEGYELLKEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 253 QLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADDAQS-----LKDEIDVLrhsSDKVSKLEGQVESYKKKL 327
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEeeqlrVKEKIGEL---EAEIASLERSIAEKEREL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 328 EDLGDLRRQVKLLEEKNTMYMQNtvsLEEELRKANAARSQLET----YKRQVVELQNRLSEESKKADKLDFEYKRLKEKV 403
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEE---LEREIEEERKRRDKLTEeyaeLKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 404 DSLQKEKDRLRSERDSLKETIEELRCVQAQ-EGQLTTQGLMPLGSQESSDSLAAEIvtPEIREKLIRLQheNKMLKINQE 482
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADlNAAIAGIEAKINELEEEKEDKALEI--KKQEWKLEQLA--ADLSKYEQE 470
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2090181558 483 GSD-NEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQ 532
Cdd:TIGR02169 471 LYDlKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
260-708 |
2.47e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 260 RLEAAKDDYRIRCEELEKEISELRQQNDELTTLADDAQSLkdeidvLRHSSDKVSKLEGQVESYKKKLEDLgdLRRQVKL 339
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAE------EYELLAELARLEQDIARLEERRREL--EERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 340 LEEkntmymqntvsLEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRSERDS 419
Cdd:COG1196 322 EEE-----------LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 420 LKETIEELRcVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKINQEGSDNEKIALLQSLLDDa 499
Cdd:COG1196 391 ALRAAAELA-AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL- 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 500 nLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQgskAEDAISVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPrfn 579
Cdd:COG1196 469 -LEEAALLEAALAELLEELAEAAARLLLLLEAEAD---YEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE--- 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 580 nsslkiEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQN-QGAAPEIQALKNQLQERDRQFHSLEKEYEKTKS 658
Cdd:COG1196 542 ------AALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKiRARAALAAALARGAIGAAVDLVASDLREADARY 615
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2090181558 659 QREME---EKYIVSAWYNMGMTLHKKAAEDRLASTGSGQSFLARQRQATSTRR 708
Cdd:COG1196 616 YVLGDtllGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR 668
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
238-668 |
3.00e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 238 SPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADDAQSLKDEIDVLRHSSD------ 311
Cdd:COG4717 60 KPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQElealea 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 312 KVSKLEGQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEELRkaNAARSQLETYKRQVVELQNRLSEESKKADK 391
Cdd:COG4717 140 ELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLS--LATEEELQDLAEELEELQQRLAELEEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 392 LDFEYKRLKEKVDSLQKEKdrlrsERDSLKETIEELR----------CVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTP 461
Cdd:COG4717 218 AQEELEELEEELEQLENEL-----EAAALEERLKEARlllliaaallALLGLGGSLLSLILTIAGVLFLVLGLLALLFLL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 462 EIREKLIRLQHENKMLKIN-QEGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGskAED 540
Cdd:COG4717 293 LAREKASLGKEAEELQALPaLEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE--LEQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 541 AISVLLKK---KLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLKIEELQEALrkkeeemkqMEERYKKYLEKAKSVI 617
Cdd:COG4717 371 EIAALLAEagvEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL---------DEEELEEELEELEEEL 441
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2090181558 618 RTLDPKQNQgAAPEIQALKNQLQ--ERDRQFHSLEKEYEKTKSQ-REMEEKYIV 668
Cdd:COG4717 442 EELEEELEE-LREELAELEAELEqlEEDGELAELLQELEELKAElRELAEEWAA 494
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
269-667 |
3.87e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 269 RIRCEELEKEISELRQQNDELTTLADDAQSLKDEIDVLRHS----SDKVSKLEGQVESYKKKLEDLGDLRRQVKLLEEKN 344
Cdd:PRK03918 213 SSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSkrklEEKIRELEERIEELKKEIEELEEKVKELKELKEKA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 345 TMYMQNTVSLEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLdfeyKRLKEKVDSLQKEKDRLRS---ERDSLK 421
Cdd:PRK03918 293 EEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL----EELKKKLKELEKRLEELEErheLYEEAK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 422 ETIEELRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKIN---------------QEGSDN 486
Cdd:PRK03918 369 AKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAieelkkakgkcpvcgRELTEE 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 487 EKIALLQS-LLDDANLRKNELETENRL--VNQRLLEVQSQVEEL-----QKSLQDQGSKAEDAISVLLKKKLE---EHLE 555
Cdd:PRK03918 449 HRKELLEEyTAELKRIEKELKEIEEKErkLRKELRELEKVLKKEselikLKELAEQLKELEEKLKKYNLEELEkkaEEYE 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 556 KLHEANNELQKKRAIIED----LEPRFNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQ----- 626
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKelekLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEylelk 608
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2090181558 627 GAAPEIQALKNQLQERDRQFHSLEKEYEKTKSQREMEEKYI 667
Cdd:PRK03918 609 DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL 649
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
130-654 |
5.86e-07 |
|
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: 53.20 E-value: 5.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 130 EQKQEYIQAIMVMEESVQHVVMT--AIQELMSKEspvsagNDAYVDLDRQLKKTSEELNEALSAKEEIaqrcheLDLQVA 207
Cdd:pfam15921 103 KQKFYLRQSVIDLQTKLQEMQMErdAMADIRRRE------SQSQEDLRNQLQNTVHELEAAKCLKEDM------LEDSNT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 208 ALQEEKSSLLAENQVLMERLNQSDSIEDPNSPAGRRHlqlqtqlEQLQEETFRLEAAKDDYRIRceELEKEISELRQQ-- 285
Cdd:pfam15921 171 QIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEH-------DSMSTMHFRSLGSAISKILR--ELDTEISYLKGRif 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 286 --NDELTTLADDAQSlKDEIdVLRHSSDKVSKLEGQVEsykkkLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEelrkana 363
Cdd:pfam15921 242 pvEDQLEALKSESQN-KIEL-LLQQHQDRIEQLISEHE-----VEITGLTEKASSARSQANSIQSQLEIIQEQ------- 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 364 ARSQLETYKRQVVELQNRLSEESKKADkldfEYKRLKE-KVDSLQKEKDRLRSErdsLKETIEELRCVQAQEGQLttqgl 442
Cdd:pfam15921 308 ARNQNSMYMRQLSDLESTVSQLRSELR----EAKRMYEdKIEELEKQLVLANSE---LTEARTERDQFSQESGNL----- 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 443 mplgsqesSDSLAAEIVTPEIREKLIRLQHENKMLKINQEGSDNEKIALLQSLLDDANLRKNELETenrLVNQRLLEVQS 522
Cdd:pfam15921 376 --------DDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEA---LLKAMKSECQG 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 523 QVEELQKSLQDQGSKAEDAISvlLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLKIEELQEALRKKEEEMKQM 602
Cdd:pfam15921 445 QMERQMAAIQGKNESLEKVSS--LTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKL 522
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2090181558 603 EERYKKYLEKAKSVIRTLDPKQNqgAAPEIQALKNQLQERDRQFHSLEKEYE 654
Cdd:pfam15921 523 RSRVDLKLQELQHLKNEGDHLRN--VQTECEALKLQMAEKDKVIEILRQQIE 572
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
304-593 |
7.79e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 7.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 304 DVLRHSSDKVSKLEGQVESYKkkleDLGDLRRQVK--LLEEKNTM--------YMQNTVSLEEELRKANAARSQLEtykr 373
Cdd:COG4913 184 RRLGIGSEKALRLLHKTQSFK----PIGDLDDFVReyMLEEPDTFeaadalveHFDDLERAHEALEDAREQIELLE---- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 374 QVVELQNRLSEESKKADKLD-----FEYKRLKEKVDSLQKEKDRLRSERDSLKETIEELrcvQAQEGQLttqglmplgsq 448
Cdd:COG4913 256 PIRELAERYAAARERLAELEylraaLRLWFAQRRLELLEAELEELRAELARLEAELERL---EARLDAL----------- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 449 essdslaaeivtpeiREKLIRLQHEnkmlkinQEGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQ 528
Cdd:COG4913 322 ---------------REELDELEAQ-------IRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASA 379
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2090181558 529 KSLQDQGSKAEDAISVL------LKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLKIEELQEALR 593
Cdd:COG4913 380 EEFAALRAEAAALLEALeeeleaLEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
260-577 |
9.34e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 9.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 260 RLEAAKDDY---RIRCEELEKEISELRQQNDELTTLADDA------QSLKDEIDVLRHSSDK-------------VSKLE 317
Cdd:TIGR02169 171 KKEKALEELeevEENIERLDLIIDEKRQQLERLRREREKAeryqalLKEKREYEGYELLKEKealerqkeaierqLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 318 GQVESYKKKLEDLGD-LRRQVKLLEEKNTMYMQNT----VSLEEELRKANA----ARSQLETYKRQVVELQNRLSEESKK 388
Cdd:TIGR02169 251 EELEKLTEEISELEKrLEEIEQLLEELNKKIKDLGeeeqLRVKEKIGELEAeiasLERSIAEKERELEDAEERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 389 ADKLDFEYKRLKEKVDSLQKEKDRLRSERDSLKETIEELRcVQAQEgqlttqglmplgsqESSDSLAAEIVTPEIREKLI 468
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLR-AELEE--------------VDKEFAETRDELKDYREKLE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 469 RLQHENKMLKINQEGSDNEKIALLQSLLDdanlRKNELETenrlVNQRLLEVQSQVEELQKSLQDQGSKAEDAISVL--L 546
Cdd:TIGR02169 396 KLKREINELKRELDRLQEELQRLSEELAD----LNAAIAG----IEAKINELEEEKEDKALEIKKQEWKLEQLAADLskY 467
|
330 340 350
....*....|....*....|....*....|.
gi 2090181558 547 KKKLEEHLEKLHEANNELQKKRAIIEDLEPR 577
Cdd:TIGR02169 468 EQELYDLKEEYDRVEKELSKLQRELAEAEAQ 498
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
336-540 |
1.36e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 336 QVKLLEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRS 415
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 416 ERDSLKETIEELrcVQAQEGQLTTQGLMPLGSQESSDSLAA-----EIVTPEIREKLIRLQHENKMLKINQEGSDNEKiA 490
Cdd:COG4942 98 ELEAQKEELAEL--LRALYRLGRQPPLALLLSPEDFLDAVRrlqylKYLAPARREQAEELRADLAELAALRAELEAER-A 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2090181558 491 LLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAED 540
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
359-665 |
1.70e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 359 RKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEyKRLKEKVDSLQKEKD------RLRSERDSLKETIEELRCVQA 432
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE-REKAERYQALLKEKReyegyeLLKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 433 QEGQLttQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQhENKMLKINQE-GSDNEKIALLQSLLDDANLRKNELETENR 511
Cdd:TIGR02169 249 LEEEL--EKLTEEISELEKRLEEIEQLLEELNKKIKDLG-EEEQLRVKEKiGELEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 512 LVNQRLLEVQSQVEELQKSLQDQGSKAEDAISVL---------LKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSS 582
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYaelkeeledLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 583 LKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPE--IQALKNQLQERDRQFHSLEKEYEK----- 655
Cdd:TIGR02169 406 RELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEwkLEQLAADLSKYEQELYDLKEEYDRvekel 485
|
330
....*....|
gi 2090181558 656 TKSQREMEEK 665
Cdd:TIGR02169 486 SKLQRELAEA 495
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
273-655 |
2.27e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 51.27 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 273 EELEKEISELRQQNDELTTLADDAQSLKDE-------IDVLRHSSD----KVSKLEGQVESYKKKLEdlGDLRRQVKLLE 341
Cdd:pfam15921 377 DQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDdrnmEVQRLEALLKAMKSECQ--GQMERQMAAIQ 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 342 EKN------TMYMQNTVSLEEELRKA----NAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKD 411
Cdd:pfam15921 455 GKNeslekvSSLTAQLESTKEMLRKVveelTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQ 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 412 RLRSERDSLKETieelrcvqaqegqlttqglmplgsQESSDSLAAEIVTPEIREKLIRLQHENKMLKINQEGSDNEKI-- 489
Cdd:pfam15921 535 HLKNEGDHLRNV------------------------QTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMqv 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 490 --ALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQ---KSLQDQGSKAEDAISVlLKKKLEEHLEKLHEANNEL 564
Cdd:pfam15921 591 ekAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLElekVKLVNAGSERLRAVKD-IKQERDQLLNEVKTSRNEL 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 565 QKKRAIIEDLEPRFNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEK-----------AKSVIRTLDPKQNQGAA--PE 631
Cdd:pfam15921 670 NSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSmegsdghamkvAMGMQKQITAKRGQIDAlqSK 749
|
410 420
....*....|....*....|....
gi 2090181558 632 IQALKNQLQERDRQFHSLEKEYEK 655
Cdd:pfam15921 750 IQFLEEAMTNANKEKHFLKEEKNK 773
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
154-425 |
5.55e-06 |
|
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: 49.74 E-value: 5.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 154 IQELMSKESPVSAGNDAYVDLDRQLKKTSEELNEALSAKE-----------EIAQRCHELDLQVAALQEEKSSLLAENQV 222
Cdd:pfam05557 57 IRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKEsqladarevisCLKNELSELRRQIQRAELELQSTNSELEE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 223 LMERLNQSDS----IEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRI---------RCEELEKEISELRQQNDEL 289
Cdd:pfam05557 137 LQERLDLLKAkaseAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIvknskselaRIPELEKELERLREHNKHL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 290 TTLADDAQSLKDEIDVLRHSSDKV--------------SKLEGQVESYKKKLEDLG-------DLRRQVKLLEEKNTMYM 348
Cdd:pfam05557 217 NENIENKLLLKEEVEDLKRKLEREekyreeaatlelekEKLEQELQSWVKLAQDTGlnlrspeDLSRRIEQLQQREIVLK 296
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2090181558 349 QNTVSLEEELRKANAARSQLETYKRQVVelqnrlseesKKADKLDFEYKRLKEKVDSLQKEKDRLRSERDSLKETIE 425
Cdd:pfam05557 297 EENSSLTSSARQLEKARRELEQELAQYL----------KKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILE 363
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
174-413 |
5.60e-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: 50.06 E-value: 5.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 174 LDRQLKKTSEELNEALSAKEEIAQRCHELDLQVAALQEEKSSLLAENQVLMERLNQSDSIEDPnspAGRRHLQLQTQLEQ 253
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE---LRAELTLLNEEAAN 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 254 LQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADDAQSLKDEI-DVLRHSSDKVSKLEGQVESYKKKLEdlgD 332
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELeSELEALLNERASLEEALALLRSELE---E 898
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 333 LRRQVKLLEEKNTMYMQNTVSLEEELrkaNAARSQLETYKRQVVELQNRLSEE--------SKKADKLDFEYKRLKEKVD 404
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKL---AQLELRLEGLEVRIDNLQERLSEEysltleeaEALENKIEDDEEEARRRLK 975
|
....*....
gi 2090181558 405 SLQKEKDRL 413
Cdd:TIGR02168 976 RLENKIKEL 984
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
364-643 |
7.45e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 7.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 364 ARSQLETYKRQVVELQNRLSEeskkadkldfeykrLKEKVDSLQKEKDRLRSERDSLkETIEELRcvqaqegqlttqglm 443
Cdd:COG4913 608 NRAKLAALEAELAELEEELAE--------------AEERLEALEAELDALQERREAL-QRLAEYS--------------- 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 444 plgsqessdslAAEIVTPEIREKLIRLQHENKMLKinqegSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQ 523
Cdd:COG4913 658 -----------WDEIDVASAEREIAELEAELERLD-----ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE 721
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 524 V---EELQKSLQDQGSKAEDAISVLLKKKLEEHLEKLHEANNELQKKRAI---IEDLEPRFNNSSLKIEELQEAlrkkee 597
Cdd:COG4913 722 LeqaEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLeerIDALRARLNRAEEELERAMRA------ 795
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2090181558 598 emkqmeerykkYLEKAKSVIRTLDPkqNQGAAPEIQALKNQLQERD 643
Cdd:COG4913 796 -----------FNREWPAETADLDA--DLESLPEYLALLDRLEEDG 828
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
273-658 |
8.14e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.51 E-value: 8.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 273 EELEKEISELRQQNDELTTLADDAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDlgdlrrqvkllEEKNTMYMQNTV 352
Cdd:PRK01156 325 HAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEE-----------YSKNIERMSAFI 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 353 SLEEELRKANAArsqletykrqvvELQNRLSEESKKADKLDfeykrlkEKVDSLQKEKDRLRSERDSLKETIEelrcvqa 432
Cdd:PRK01156 394 SEILKIQEIDPD------------AIKKELNEINVKLQDIS-------SKVSSLNQRIRALRENLDELSRNME------- 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 433 qegQLTTQGLMPLGSQESSDSLAAEIVTpEIREKLIRLqhENKMLKINQEGSD-NEKIALLQSLLDDANLRK-NELETEN 510
Cdd:PRK01156 448 ---MLNGQSVCPVCGTTLGEEKSNHIIN-HYNEKKSRL--EEKIREIEIEVKDiDEKIVDLKKRKEYLESEEiNKSINEY 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 511 RLVNQRLLEVQSQVEELQKsLQDQGSKAEDAISVLLKKKLEEHLEKLHEANNELQKKRAI-IEDLEPRFNNSSLKIEELQ 589
Cdd:PRK01156 522 NKIESARADLEDIKIKINE-LKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVISLIdIETNRSRSNEIKKQLNDLE 600
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2090181558 590 EALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNqgaapEIQALKNQLQERDRQFHSLEKEYEKTKS 658
Cdd:PRK01156 601 SRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYN-----EIQENKILIEKLRGKIDNYKKQIAEIDS 664
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
299-587 |
1.23e-05 |
|
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: 48.81 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 299 LKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEEL-RKANAARSQLETYKRQVVE 377
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLaKEEEELKSELLKLERRKVD 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 378 LQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRSERDSLKETIEELRCVQAQEgqlttqglmplgSQESSDSLAAE 457
Cdd:pfam02463 312 DEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKL------------EQLEEELLAKK 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 458 IVTPEIREKLIRLQHENKMLKINQEGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSK 537
Cdd:pfam02463 380 KLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELK 459
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2090181558 538 AEDAISVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLKIEE 587
Cdd:pfam02463 460 LLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGL 509
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
260-661 |
1.28e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 260 RLEAAKDdyriRCEELEKEISELRQQNDELTTLADD---AQSLKDEIDVLRHSSDKVSKLEG---QVESYKKKLEDLGDL 333
Cdd:PTZ00121 1358 EAEAAEE----KAEAAEKKKEEAKKKADAAKKKAEEkkkADEAKKKAEEDKKKADELKKAAAakkKADEAKKKAEEKKKA 1433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 334 RRQVKLLEEKNTMymQNTVSLEEELRKANAARSQLETyKRQVVELQNRlSEESKKADKLDFEYKRLKEKVDSLQKeKDRL 413
Cdd:PTZ00121 1434 DEAKKKAEEAKKA--DEAKKKAEEAKKAEEAKKKAEE-AKKADEAKKK-AEEAKKADEAKKKAEEAKKKADEAKK-AAEA 1508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 414 RSERDSLKETIEELRCVQAQEGQlttqglmplgSQESSDSL--AAEIVTPEIREKLIRLQHENKMLKINQEGSDNEkial 491
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAE----------EAKKADEAkkAEEKKKADELKKAEELKKAEEKKKAEEAKKAEE---- 1574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 492 lqslldDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDA-ISVLLKKKLEEHLEKLHEANNELQKKRAI 570
Cdd:PTZ00121 1575 ------DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAkIKAEELKKAEEEKKKVEQLKKKEAEEKKK 1648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 571 IEDLEPRFNNSSLKIEELQ----------EALRKKEEEMKQMEERYKKYLEKAKSVIRTldPKQNQGAAPEIQALKNQLQ 640
Cdd:PTZ00121 1649 AEELKKAEEENKIKAAEEAkkaeedkkkaEEAKKAEEDEKKAAEALKKEAEEAKKAEEL--KKKEAEEKKKAEELKKAEE 1726
|
410 420
....*....|....*....|.
gi 2090181558 641 ERDRQFHSLEKEYEKTKSQRE 661
Cdd:PTZ00121 1727 ENKIKAEEAKKEAEEDKKKAE 1747
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
334-428 |
1.48e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 48.32 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 334 RRQVKLLEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLK----------EKV 403
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARseerreirkdREI 467
|
90 100
....*....|....*....|....*
gi 2090181558 404 DSLQKEKDRLRSERDSLKETIEELR 428
Cdd:COG2433 468 SRLDREIERLERELEEERERIEELK 492
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
260-499 |
1.66e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 260 RLEAAKDDYRIRCEELEKEISELRQQNDELTTLADDA-------------QSLKDEIDVLRHSSDKVSKLEGQVESYKKK 326
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvasaereiAELEAELERLDASSDDLAALEEQLEELEAE 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 327 LEDL----GDLRRQVKLLEEKNTmymqntvSLEEELRKANAARSQLETYKRQVV--ELQNRLSEESKKAdkldfeykRLK 400
Cdd:COG4913 701 LEELeeelDELKGEIGRLEKELE-------QAEEELDELQDRLEAAEDLARLELraLLEERFAAALGDA--------VER 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 401 EKVDSLQKEKDRLRSERDSLKETIEELRCVQAQEGQLTTQGLMP-LGSQESSDSLAAEIVT---PEIREKLIRLQHENKm 476
Cdd:COG4913 766 ELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDAdLESLPEYLALLDRLEEdglPEYEERFKELLNENS- 844
|
250 260
....*....|....*....|...
gi 2090181558 477 lkinqegsdNEKIALLQSLLDDA 499
Cdd:COG4913 845 ---------IEFVADLLSKLRRA 858
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
271-667 |
1.69e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 271 RCEELEKEISELRQQNDELTTladdAQSLKDEIDVLRHSSDKVSKlegqVESYKKKLEDLGDLRRQVKLLEEKNTMymQN 350
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKK----AAAAKKKADEAKKKAEEKKK----ADEAKKKAEEAKKADEAKKKAEEAKKA--EE 1461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 351 TVSLEEELRKANAARSQLETyKRQVVELQNRLSEESKKADKLDfEYKRLKEKVDSLQKEKDRLRSE---RDSLKETIEEL 427
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEE-AKKADEAKKKAEEAKKKADEAK-KAAEAKKKADEAKKAEEAKKADeakKAEEAKKADEA 1539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 428 RcvQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKINQE-GSDNEKIALLQSLLDDANLRKNEL 506
Cdd:PTZ00121 1540 K--KAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEArIEEVMKLYEEEKKMKAEEAKKAEE 1617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 507 ETENRLVNQRLLEVQSQVEELQKSLQDQGSKAED---------AISVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEpR 577
Cdd:PTZ00121 1618 AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElkkaeeenkIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALK-K 1696
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 578 FNNSSLKIEELqealRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAApEIQALKNQLQERDRQFHSLEKEYEKTK 657
Cdd:PTZ00121 1697 EAEEAKKAEEL----KKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK-KAEEAKKDEEEKKKIAHLKKEEEKKAE 1771
|
410
....*....|
gi 2090181558 658 SQREMEEKYI 667
Cdd:PTZ00121 1772 EIRKEKEAVI 1781
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
273-427 |
2.14e-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: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 273 EELEKEISELRQqndELTTLADDAQSLKDEIDVLRHSSDKVSKLEGQVESykkkLEDLGDLRRQVklleekntmymqntV 352
Cdd:COG4913 613 AALEAELAELEE---ELAEAEERLEALEAELDALQERREALQRLAEYSWD----EIDVASAEREI--------------A 671
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2090181558 353 SLEEELRKANAARSQLETYKRQVVELQNRLseeskkaDKLDFEYKRLKEKVDSLQKEKDRLRSERDSLKETIEEL 427
Cdd:COG4913 672 ELEAELERLDASSDDLAALEEQLEELEAEL-------EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
179-431 |
2.26e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 179 KKTSEELNEALSAKEEIAQRCHELDLQVAALQEEKSSLLAENQVLMERLNQSDSIedpnspagRRHLQLQTQLEQLQEET 258
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEK--------KKAEEAKKAEEDKNMAL 1580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 259 FRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADDAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDL----- 333
Cdd:PTZ00121 1581 RKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAeeenk 1660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 334 --RRQVKLLEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKD 411
Cdd:PTZ00121 1661 ikAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE 1740
|
250 260
....*....|....*....|
gi 2090181558 412 RLRSERDSLKETIEELRCVQ 431
Cdd:PTZ00121 1741 EDKKKAEEAKKDEEEKKKIA 1760
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
360-543 |
2.37e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 360 KANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRSERDSLKETIEELRCV-------QA 432
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElgeraraLY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 433 QEGQLTTQGLMPLGSQESSD----SLAAEIVTPEIREKLIRLQHENKMLKiNQEGSDNEKIALLQSLLDDANLRKNELET 508
Cdd:COG3883 97 RSGGSVSYLDVLLGSESFSDfldrLSALSKIADADADLLEELKADKAELE-AKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 2090181558 509 ---ENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDAIS 543
Cdd:COG3883 176 qqaEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
259-670 |
2.52e-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: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 259 FRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADDAQSLKDEI--DVLRHSSDKVSKLEGQVEsykkkledlgDLRRQ 336
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELeaQIRGNGGDRLEQLEREIE----------RLERE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 337 VKLLEEKNTMYMQNTVSLEEElrkANAARSQLETYKRQVVELQNRLSEESKKA----DKLDFEYKRLKEKVDSLQKEKDR 412
Cdd:COG4913 354 LEERERRRARLEALLAALGLP---LPASAEEFAALRAEAAALLEALEEELEALeealAEAEAALRDLRRELRELEAEIAS 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 413 LRSERDSLKETIEELRCVQAQE---------------------------------------------------------- 434
Cdd:COG4913 431 LERRKSNIPARLLALRDALAEAlgldeaelpfvgelievrpeeerwrgaiervlggfaltllvppehyaaalrwvnrlhl 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 435 -GQLTTQGLMPLGSQE-----SSDSLAAEIVT------PEIREKLIR------------LQHENK------MLKINQE-- 482
Cdd:COG4913 511 rGRLVYERVRTGLPDPerprlDPDSLAGKLDFkphpfrAWLEAELGRrfdyvcvdspeeLRRHPRaitragQVKGNGTrh 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 483 --------------GSDN-EKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKsLQDQGSKAEDAISVLLK 547
Cdd:COG4913 591 ekddrrrirsryvlGFDNrAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQR-LAEYSWDEIDVASAERE 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 548 -KKLEEHLEKLHEANNELQKKRAIIEDLEprfnnssLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQ 626
Cdd:COG4913 670 iAELEAELERLDASSDDLAALEEQLEELE-------AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2090181558 627 GAAPEIQALKNQLQE------RDRQFHSLEKEYEKTKSQREMEEKYIVSA 670
Cdd:COG4913 743 ARLELRALLEERFAAalgdavERELRENLEERIDALRARLNRAEEELERA 792
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
260-426 |
3.70e-05 |
|
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: 45.69 E-value: 3.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 260 RLEAAKDDYRIRCEELEKEISELRQQNDELTTLADDAQSLKDEIDV-LRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVK 338
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKeIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 339 LLEEKNTMYMQNTVsLEEELRKANAarsQLETYKRQVVELQNRLSEeskKADKLDFEYKRLKEKVDSLQKEKDRLRSERD 418
Cdd:COG1579 94 LQKEIESLKRRISD-LEDEILELME---RIEELEEELAELEAELAE---LEAELEEKKAELDEELAELEAELEELEAERE 166
|
....*...
gi 2090181558 419 SLKETIEE 426
Cdd:COG1579 167 ELAAKIPP 174
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
261-428 |
3.70e-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: 3.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 261 LEAAKDDYRIRCEELEKEISELRQQNDeLTTLADDAQSLKDEIDVLRhssDKVSKLEGQVESYKKKLEDLgdlRRQVKLL 340
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNG-LVDLSEEAKLLLQQLSELE---SQLAEARAELAEAEARLAAL---RAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 341 EEKNTMYMQNTV--SLEEELRKANAARSQLET-----------YKRQVVELQNRLSEESKKA-DKLDFEYKRLKEKVDSL 406
Cdd:COG3206 253 PDALPELLQSPViqQLRAQLAELEAELAELSArytpnhpdviaLRAQIAALRAQLQQEAQRIlASLEAELEALQAREASL 332
|
170 180
....*....|....*....|..
gi 2090181558 407 QKEKDRLRSERDSLKETIEELR 428
Cdd:COG3206 333 QAQLAQLEARLAELPELEAELR 354
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
263-428 |
3.96e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.93 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 263 AAKDDYRIRCEELEKEISELRQQNDELTT-LADDAQSLKDEIDVLRHSSDKVSKLEGQVESYKK--KLEDLGDL----RR 335
Cdd:PHA02562 213 ENIARKQNKYDELVEEAKTIKAEIEELTDeLLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKviKMYEKGGVcptcTQ 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 336 QVKLLEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRS 415
Cdd:PHA02562 293 QISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQA 372
|
170
....*....|...
gi 2090181558 416 ERDSLKETIEELR 428
Cdd:PHA02562 373 EFVDNAEELAKLQ 385
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
173-427 |
5.87e-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: 5.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 173 DLDRQLKKTSEELNEALSAKEEIAQRCHELDLQVAALQEEKSSLLAENQVLMERLNQ-----------SDSIEDPNSPAG 241
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaanlrerLESLERRIAATE 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 242 RRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADDAQSLKDE-IDVLRHSSDKVSKLEGQV 320
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEElSEELRELESKRSELRREL 917
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 321 ESYKKKLEDLgDLRRQ---VKLLEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQVVELQNRLSE---------Eskk 388
Cdd:TIGR02168 918 EELREKLAQL-ELRLEgleVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaaiE--- 993
|
250 260 270
....*....|....*....|....*....|....*....
gi 2090181558 389 adkldfEYKRLKEKVDSLQKEKDRLRSERDSLKETIEEL 427
Cdd:TIGR02168 994 ------EYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
351-593 |
6.77e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.29 E-value: 6.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 351 TVSLEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRSE----RDSLKETIEE 426
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKvkelKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 427 LRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIvtpeirEKLIRlQHENKMLKINQEGSDNEKIALLQSLLDDAnLRKNEL 506
Cdd:COG1340 87 LNELREELDELRKELAELNKAGGSIDKLRKEI------ERLEW-RQQTEVLSPEEEKELVEKIKELEKELEKA-KKALEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 507 ETENRLVNQRLLEVQSQVEELQKSLQDQGSKAE--DAISVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLK 584
Cdd:COG1340 159 NEKLKELRAELKELRKEAEEIHKKIKELAEEAQelHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKE 238
|
....*....
gi 2090181558 585 IEELQEALR 593
Cdd:COG1340 239 LRELRKELK 247
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
183-439 |
8.12e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 8.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 183 EELNEALSAKEEIAQRCHELDLQVAALQEEksslLAENQVLMERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQEETFRLE 262
Cdd:PRK02224 468 ETIEEDRERVEELEAELEDLEEEVEEVEER----LERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELR 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 263 AAKDDYRIRCEELEKEISELRQQNDE----LTTLADDAQSLKDEIDVL---RHSSDKVSKLEGQVESYKKKLEDLGDLRR 335
Cdd:PRK02224 544 ERAAELEAEAEEKREAAAEAEEEAEEareeVAELNSKLAELKERIESLeriRTLLAAIADAEDEIERLREKREALAELND 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 336 QVK-LLEEKNTMYMQNTVSLEEE-LRKANAARSQLETYKRQVvelqnrlseeskkADKLDfeykRLKEKVDSLQ------ 407
Cdd:PRK02224 624 ERReRLAEKRERKRELEAEFDEArIEEAREDKERAEEYLEQV-------------EEKLD----ELREERDDLQaeigav 686
|
250 260 270
....*....|....*....|....*....|....*.
gi 2090181558 408 ----KEKDRLRSERDSLKETIEELRCVQAQEGQLTT 439
Cdd:PRK02224 687 enelEELEELRERREALENRVEALEALYDEAEELES 722
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
260-688 |
8.62e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 8.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 260 RLEAAKDDYRIRCEELEKEISELRQQNDELTTLADDAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDlgdlRRQVKL 339
Cdd:PTZ00121 1244 KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEE----AKKADE 1319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 340 LEEKntmymqntvsLEEELRKANAARSQLETYKRQVvelQNRLSEESKKADKLdfeyKRLKEKVDSLQKEKDRLRSERDS 419
Cdd:PTZ00121 1320 AKKK----------AEEAKKKADAAKKKAEEAKKAA---EAAKAEAEAAADEA----EAAEEKAEAAEKKKEEAKKKADA 1382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 420 LKETIEELRcvQAQEGQLTTQGLMPlGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKINQEGSDNEKIALLQSLLDDA 499
Cdd:PTZ00121 1383 AKKKAEEKK--KADEAKKKAEEDKK-KADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKA 1459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 500 -NLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDAISVLLKKKLEEHLEKLHEAN--NELQKKRAIIEDLEP 576
Cdd:PTZ00121 1460 eEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKkaDEAKKAEEAKKADEA 1539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 577 RFNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQLQERDRQFHSLEK-EYEK 655
Cdd:PTZ00121 1540 KKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKaEEAK 1619
|
410 420 430
....*....|....*....|....*....|....*.
gi 2090181558 656 TKSQ---REMEEKYIVSAWYNMGMTLHKKAAEDRLA 688
Cdd:PTZ00121 1620 IKAEelkKAEEEKKKVEQLKKKEAEEKKKAEELKKA 1655
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
298-577 |
1.15e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.30 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 298 SLKDEID-VLR--HSSDKVsklegQVESYKKKLEDLgdlrrQVKLLEEKNTMYMQNTVSLEEELRKANAARSQLETYKrq 374
Cdd:PRK05771 13 TLKSYKDeVLEalHELGVV-----HIEDLKEELSNE-----RLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVS-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 375 VVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRSERDSLK--ETIE-ELRCVQAQEGQLTTQGLMPLGSQESS 451
Cdd:PRK05771 81 VKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwGNFDlDLSLLLGFKYVSVFVGTVPEDKLEEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 452 DSLAAEIVTPEIREKlirlqHENKMLKINQEGSDNEKIAllqSLLDDANLRKNELETENRL------VNQRLLEVQSQVE 525
Cdd:PRK05771 161 KLESDVENVEYISTD-----KGYVYVVVVVLKELSDEVE---EELKKLGFERLELEEEGTPselireIKEELEEIEKERE 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2090181558 526 ELQKSLQDQGSKAEDAISVL------LKKKLE--------------------EHLEKLHEANNELQKKRAIIEDLEPR 577
Cdd:PRK05771 233 SLLEELKELAKKYLEELLALyeyleiELERAEalskflktdktfaiegwvpeDRVKKLKELIDKATGGSAYVEFVEPD 310
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
368-661 |
1.55e-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: 45.11 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 368 LETYKRQVVELQNRLSEESKKADKLDFEYKR----LKEKVDSLQKEKDRL----RSE-------RDSLKETIEELRCVQA 432
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNELHEKQKFYLRQsvidLQTKLQEMQMERDAMadirRREsqsqedlRNQLQNTVHELEAAKC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 433 QEGQLTTQGLMPLgSQESSDSLAAEIVTPEIREKLIRLQhENKMLKINQEgsDNEKIALLQSLLDDANLRKNELETENRL 512
Cdd:pfam15921 160 LKEDMLEDSNTQI-EQLRKMMLSHEGVLQEIRSILVDFE-EASGKKIYEH--DSMSTMHFRSLGSAISKILRELDTEISY 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 513 VNQRLLEVQSQVEELQKSLQDQG----SKAEDAISVLLKKK------LEEHLEKLHEANNELQKKRAIIEDLEPRFNNSS 582
Cdd:pfam15921 236 LKGRIFPVEDQLEALKSESQNKIelllQQHQDRIEQLISEHeveitgLTEKASSARSQANSIQSQLEIIQEQARNQNSMY 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 583 LK--------IEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQgAAPEIQALKNQLQERDRQFHSLEKEYE 654
Cdd:pfam15921 316 MRqlsdlestVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQ-FSQESGNLDDQLQKLLADLHKREKELS 394
|
....*..
gi 2090181558 655 KTKSQRE 661
Cdd:pfam15921 395 LEKEQNK 401
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
262-665 |
1.56e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 262 EAAKDDYRIRCEELEKEISELRQQnDELTTLADDAQSLKDEIDvlRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKLLE 341
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKKA-DEAKKKAEEAKKKADAAK--KKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 342 EKNtmymqntvslEEELRKANAARSQLETyKRQVVELQNRLSEESKKADKLDfEYKRLKEKVDSLQKEKDRLRsERDSLK 421
Cdd:PTZ00121 1371 KKK----------EEAKKKADAAKKKAEE-KKKADEAKKKAEEDKKKADELK-KAAAAKKKADEAKKKAEEKK-KADEAK 1437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 422 ETIEELRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKINQEGSDNEKIALLQSLLDDA-- 499
Cdd:PTZ00121 1438 KKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAkk 1517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 500 --NLRKNE----LETENRLVNQRLLEVQSQVEELQKSlqDQGSKAEDAISVLLKKKLEEHLEKLHEANNELQK--KRAII 571
Cdd:PTZ00121 1518 aeEAKKADeakkAEEAKKADEAKKAEEKKKADELKKA--EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaeEARIE 1595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 572 EDLEPRFNNSSLKIEELQ---------EALRKKEEEMKQMEERYKKYLEKAKSVIRTldPKQNQGAAPEIQALKNQLQER 642
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKkaeeakikaEELKKAEEEKKKVEQLKKKEAEEKKKAEEL--KKAEEENKIKAAEEAKKAEED 1673
|
410 420
....*....|....*....|...
gi 2090181558 643 DRQFHSLEKEYEKTKSQREMEEK 665
Cdd:PTZ00121 1674 KKKAEEAKKAEEDEKKAAEALKK 1696
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
169-428 |
1.88e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 169 DAYVDLDRQLKKTSEELnEALSAKEEIAQRCHELDLQVAALQEEKSSLLAENqvlmerlnqsdsiedpnspAGRRHLQLQ 248
Cdd:COG4913 235 DDLERAHEALEDAREQI-ELLEPIRELAERYAAARERLAELEYLRAALRLWF-------------------AQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 249 TQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTlaDDAQSLKDEIDVLRhssDKVSKLEGQVESYKKKLE 328
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGG--DRLEQLEREIERLE---RELEERERRRARLEALLA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 329 DLGdlrrqvklleekntmyMQNTVSLEEELRKANAARSQLETYKRQVVELQNRLseeskkaDKLDFEYKRLKEKVDSLQK 408
Cdd:COG4913 370 ALG----------------LPLPASAEEFAALRAEAAALLEALEEELEALEEAL-------AEAEAALRDLRRELRELEA 426
|
250 260
....*....|....*....|
gi 2090181558 409 EKDRLRSERDSLKETIEELR 428
Cdd:COG4913 427 EIASLERRKSNIPARLLALR 446
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
384-661 |
2.16e-04 |
|
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: 44.66 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 384 EESKKADKLDFEYKRLKEKVDSLQKEKDRLRSERDSLKETIEELRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTpei 463
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA--- 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 464 rekliRLQHENKMLkinqegsdNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLqdqgSKAEDAIS 543
Cdd:TIGR02168 751 -----QLSKELTEL--------EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL----DELRAELT 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 544 vLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDP- 622
Cdd:TIGR02168 814 -LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALl 892
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2090181558 623 --------KQNQGAAPEIQALKNQLQERDRQFHSLEKEYEKTKSQRE 661
Cdd:TIGR02168 893 rseleelsEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
301-668 |
2.32e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 301 DEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEELRKANAarsQLETYKRQVVELQN 380
Cdd:PRK03918 138 DAILESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEK---ELEEVLREINEISS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 381 RLSEESKKADKLDFEYKRL---KEKVDSLQKEKDRLRSERDSLKETIEELRCVQAQegqlTTQGLMPLGSQESSDSLAAE 457
Cdd:PRK03918 215 ELPELREELEKLEKEVKELeelKEEIEELEKELESLEGSKRKLEEKIRELEERIEE----LKKEIEELEEKVKELKELKE 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 458 IVTPEIREKLIRLQHENKMLKINQEGSD-NEKIALLQSLLDDANLRKNEL-ETENRL--VNQRLLEVQSQVEELQ--KSL 531
Cdd:PRK03918 291 KAEEYIKLSEFYEEYLDELREIEKRLSRlEEEINGIEERIKELEEKEERLeELKKKLkeLEKRLEELEERHELYEeaKAK 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 532 QDQGSKAEDAISVLLKKKLEEHLEKLHEANNELQKKraiIEDLEPRFNNSSLKIEELQEALRKkeeemkqmeerykkyLE 611
Cdd:PRK03918 371 KEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEE---ISKITARIGELKKEIKELKKAIEE---------------LK 432
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2090181558 612 KAKSVI----RTLDPKQNQGA----APEIQALKNQLQERDRQFHSLEKEYEKTKSQREMEEKYIV 668
Cdd:PRK03918 433 KAKGKCpvcgRELTEEHRKELleeyTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIK 497
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
290-427 |
2.80e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.08 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 290 TTLADDAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKlEDLGDLRRQVKLLEEKNtmymqntVSLEEELRKANAARSQLE 369
Cdd:COG2433 376 LSIEEALEELIEKELPEEEPEAEREKEHEERELTEEE-EEIRRLEEQVERLEAEV-------EELEAELEEKDERIERLE 447
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2090181558 370 TYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRSERDSLKETIEEL 427
Cdd:COG2433 448 RELSEARSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLE 505
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
273-574 |
2.93e-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: 44.24 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 273 EELEKEISELRQQNDELTTLADDAQSLKDEIDVLRH--SSDKVSKLEGQVESYKKKLEDL-----------GDLRRQVKL 339
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNqkEQDWNKELKSELKNQEKKLEEIqnqisqnnkiiSQLNEQISQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 340 LEEKNTMYMQNTVSLEEELRKANAA-----------RSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQK 408
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEieklkkenqsyKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 409 EKDRLRSERDSLKETIEELRcVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHE-----NKMLKINQEG 483
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLT-NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKElkskeKELKKLNEEK 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 484 SD-NEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEdaisvllKKKLEEHLEKLHEANN 562
Cdd:TIGR04523 506 KElEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKE-------IDEKNKEIEELKQTQK 578
|
330
....*....|..
gi 2090181558 563 ELQKKRAIIEDL 574
Cdd:TIGR04523 579 SLKKKQEEKQEL 590
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
371-665 |
4.45e-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: 43.81 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 371 YKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQK-EKDRLRSERDSLKETIEELRCVQAQEGQLTTQGLMPLGSQE 449
Cdd:pfam02463 167 LKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEqAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 450 SS--DSLAAEIVTPEIREKLIRLQHENKMLKINQEGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEEL 527
Cdd:pfam02463 247 RDeqEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 528 QKSL--------QDQGSKAEDAISVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLKIEELQEALRKKEEEM 599
Cdd:pfam02463 327 EKELkkekeeieELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKE 406
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2090181558 600 KQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQLQERDRQFHSLEKEYEKTKSQREMEEK 665
Cdd:pfam02463 407 AQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSED 472
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
168-425 |
5.38e-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: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 168 NDAYVDLDRQLKKTSEELNEALSAKEEIAQrchELDLQVAALQEEKSSLLAENQVLM-ERLNQSDSIEDPNSPAGRRHLQ 246
Cdd:TIGR04523 379 NQSYKQEIKNLESQINDLESKIQNQEKLNQ---QKDEQIKKLQQEKELLEKEIERLKeTIIKNNSEIKDLTNQDSVKELI 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 247 LQTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADDAQSLKDEIDVLRHSSDKVSKLEGQVESYKKK 326
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 327 LED-LGDLRRQVK---------LLEEKNTMYMQNTVSLEEELRKANAARSQLET----YKRQVVELQNRLSEESKKADKL 392
Cdd:TIGR04523 536 KESkISDLEDELNkddfelkkeNLEKEIDEKNKEIEELKQTQKSLKKKQEEKQElidqKEKEKKDLIKEIEEKEKKISSL 615
|
250 260 270
....*....|....*....|....*....|...
gi 2090181558 393 DFEYKRLKEKVDSLQKEKDRLRSERDSLKETIE 425
Cdd:TIGR04523 616 EKELEKAKKENEKLSSIIKNIKSKKNKLKQEVK 648
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
265-531 |
5.86e-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: 5.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 265 KDDYRIRCEELEKEISELRQQNDELTTLADDAQSLKDEidvlrhssdkvskLEGQVESYKkklEDLGDLRRQVKLLEEKN 344
Cdd:pfam12128 268 KSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDE-------------LNGELSAAD---AAVAKDRSELEALEDQH 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 345 TMYmqntvsLEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDS-LQKEKDRLRSERDSLKET 423
Cdd:pfam12128 332 GAF------LDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEqNNRDIAGIKDKLAKIREA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 424 IEELRCV-----QAQEGQLTTQ---GLMPLGSQESSDSLAAE-----IVTPEIREKLIrLQHENKMLKIN----QEGSDN 486
Cdd:pfam12128 406 RDRQLAVaeddlQALESELREQleaGKLEFNEEEYRLKSRLGelklrLNQATATPELL-LQLENFDERIErareEQEAAN 484
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2090181558 487 EKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSL 531
Cdd:pfam12128 485 AEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQL 529
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
190-440 |
6.25e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.99 E-value: 6.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 190 SAKEEIAQRCHELDL-QVAALQEEKSS-----LLAENQVLMERLNQSDSIEDPNSpagrrhlqlQTQLEQLQEETFRLEA 263
Cdd:PRK05771 16 SYKDEVLEALHELGVvHIEDLKEELSNerlrkLRSLLTKLSEALDKLRSYLPKLN---------PLREEKKKVSVKSLEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 264 AKDDYRIRCEELEKEISELrqqNDELTTLADDAQSLKDEIDVLR------------HSSDKVSKLEGQVESYKKKLEDLG 331
Cdd:PRK05771 87 LIKDVEEELEKIEKEIKEL---EEEISELENEIKELEQEIERLEpwgnfdldlsllLGFKYVSVFVGTVPEDKLEELKLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 332 DLRRQVKLLEE-KNTMYM------QNTVSLEEELRKANAARSQLetykrqvvelqnrlsEESKKADKLdfeYKRLKEKVD 404
Cdd:PRK05771 164 SDVENVEYISTdKGYVYVvvvvlkELSDEVEEELKKLGFERLEL---------------EEEGTPSEL---IREIKEELE 225
|
250 260 270
....*....|....*....|....*....|....*.
gi 2090181558 405 SLQKEKDRLRSERDSLKETIEELrcVQAQEGQLTTQ 440
Cdd:PRK05771 226 EIEKERESLLEELKELAKKYLEE--LLALYEYLEIE 259
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
274-617 |
6.53e-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: 43.42 E-value: 6.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 274 ELEKEISELRQQNDELTTLADDAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKLLEEKNtmymqNTVS 353
Cdd:pfam02463 663 EVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDK-----INEE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 354 LEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRSERDSLKETIEELRCVQAQ 433
Cdd:pfam02463 738 LKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELL 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 434 EGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKINQEGSDNEKIALLQSLLDDANLRKNELETENRLV 513
Cdd:pfam02463 818 EEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 514 NQRLLEVQSQVEELQKSLQDQGSKAEDAISVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLKIEELQEALR 593
Cdd:pfam02463 898 EKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNL 977
|
330 340
....*....|....*....|....
gi 2090181558 594 KKEEEMKQMEERYKKYLEKAKSVI 617
Cdd:pfam02463 978 MAIEEFEEKEERYNKDELEKERLE 1001
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
173-593 |
1.34e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 173 DLDRQLKKTSEELNEALSAKEEIAQRCHELDLQVAALQEEKSSLLAENQVLMERLNQSDSIEDPN----SPAGRRHLQLQ 248
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAeeelEELAEELLEAL 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 249 TQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADDAQSLKDEID------------VLRHSSDKVSKL 316
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAeeeaeleeeeeaLLELLAELLEEA 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 317 EGQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEELRKANAAR--------SQLETYKRQVVE------LQNRL 382
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlagavavlIGVEAAYEAALEaalaaaLQNIV 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 383 SEESKKADKLDFEYKRLKEKVDS---LQKEKDRLRSERDSLKETIEELRCVQAQEGQLTTQGLMPLGSQESSDSLAAE-- 457
Cdd:COG1196 553 VEDDEVAAAAIEYLKAAKAGRATflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAArl 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 458 ------IVTPEIREKLIRLQHEnkMLKINQEGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSL 531
Cdd:COG1196 633 eaalrrAVTLAGRLREVTLEGE--GGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA 710
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2090181558 532 QDQGSKAEDAISVLLKKKLEEHLEklHEANNELQKKRAIIEDLEPRFNNSSLKIEELQEALR 593
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAER--EELLEELLEEEELLEEEALEELPEPPDLEELERELE 770
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
488-665 |
1.37e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 488 KIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDaisvlLKKKLEEHLEKLHEANNELQKK 567
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE-----LELELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 568 RAIIEDLEPRFNNSSLKIEELQEALRKKEEEMKQMEERykkyLEKAKSVIRTLDPKQNQGAApEIQALKNQLQERDRQFH 647
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEE----LEELEEELEEAEEELEEAEA-ELAEAEEALLEAEAELA 375
|
170
....*....|....*...
gi 2090181558 648 SLEKEYEKTKSQREMEEK 665
Cdd:COG1196 376 EAEEELEELAEELLEALR 393
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
501-665 |
1.40e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 501 LRKNELETENRLVN-----QRLLEVQSQVEELQKSLQDQGSKAEDAISV----------LLKKKLEEHLEKLHEANNELQ 565
Cdd:TIGR02168 170 YKERRKETERKLERtrenlDRLEDILNELERQLKSLERQAEKAERYKELkaelrelelaLLVLRLEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 566 KKRAIIEDLEPRFNNSSLKIEELQEALRKkeeemkqmeerykkyLEKAKSVIRtldpKQNQGAAPEIQALKNQLQERDRQ 645
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVSE---------------LEEEIEELQ----KELYALANEISRLEQQKQILRER 310
|
170 180
....*....|....*....|
gi 2090181558 646 FHSLEKEYEKTKSQREMEEK 665
Cdd:TIGR02168 311 LANLERQLEELEAQLEELES 330
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
260-438 |
1.43e-03 |
|
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: 41.67 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 260 RLEAAKDDYRIRCEELEKEISELRQQNDELTT-LADDAQSLKDEIDVL-RHSSDKVSKLEGQVESYKKKLEDLGDLRRQV 337
Cdd:COG4942 66 ALARRIRALEQELAALEAELAELEKEIAELRAeLEAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 338 KLLEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLdfeYKRLKEKVDSLQKEKDRLRSER 417
Cdd:COG4942 146 PARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL---LARLEKELAELAAELAELQQEA 222
|
170 180
....*....|....*....|.
gi 2090181558 418 DSLKETIEELRCVQAQEGQLT 438
Cdd:COG4942 223 EELEALIARLEAEAAAAAERT 243
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
360-639 |
1.44e-03 |
|
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: 41.67 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 360 KANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRSERDSLKETIEELrcvQAQEGQLtt 439
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL---EKEIAEL-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 440 qglmplgsqessdslaaeivtpeiREKLIRLQHE-NKMLKINQEGSDNEKIALL--QSLLDDANLRKNELETENRLVNQR 516
Cdd:COG4942 96 ------------------------RAELEAQKEElAELLRALYRLGRQPPLALLlsPEDFLDAVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 517 LLEVQSQVEELQKslqdqgskaedaisvlLKKKLEEHLEKLHEANNELQKKRAIIEDLEprfNNSSLKIEELQEALRKKE 596
Cdd:COG4942 152 AEELRADLAELAA----------------LRAELEAERAELEALLAELEEERAALEALK---AERQKLLARLEKELAELA 212
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2090181558 597 EEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQL 639
Cdd:COG4942 213 AELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
273-657 |
2.02e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.54 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 273 EELEKEI----SELRQQNDELTTLADdaqSLKDEIDVLRHSSDKVSKLEGQVESYKKKLED----LGDLRRQVKLLEEKN 344
Cdd:TIGR04523 36 KQLEKKLktikNELKNKEKELKNLDK---NLNKDEEKINNSNNKIKILEQQIKDLNDKLKKnkdkINKLNSDLSKINSEI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 345 TMYMQNTVSLEEELRKAnaaRSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRSERDSLKETI 424
Cdd:TIGR04523 113 KNDKEQKNKLEVELNKL---EKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 425 eelrcvqaqegqlttqglmplgsqessdslaaeivtpeireKLIRLQHENKMLKINQEGSDNEKIALLQSLLDDANLRKN 504
Cdd:TIGR04523 190 -----------------------------------------DKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 505 ELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDAISVLLKK--KLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSS 582
Cdd:TIGR04523 229 QLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKqkELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDW 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 583 LK-----IEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNqgaapEIQALKNQLQERDRQFHSLEKEYEKTK 657
Cdd:TIGR04523 309 NKelkseLKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES-----ENSEKQRELEEKQNEIEKLKKENQSYK 383
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
273-669 |
2.48e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 273 EELEKEISELR----QQNDELTTLADDAQSLKDEIDVLRHSSDK----VSKLEGQVESYKKKL-EDLGDLRRQVKLLEEK 343
Cdd:TIGR04523 78 KILEQQIKDLNdklkKNKDKINKLNSDLSKINSEIKNDKEQKNKleveLNKLEKQKKENKKNIdKFLTEIKKKEKELEKL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 344 NTMYmQNTVSLEEELRKanaarsQLETYKRQVVELQNRLSEESKKADKLD---FEYKRLKEKVDSLQKEKDRLRSERDSL 420
Cdd:TIGR04523 158 NNKY-NDLKKQKEELEN------ELNLLEKEKLNIQKNIDKIKNKLLKLElllSNLKKKIQKNKSLESQISELKKQNNQL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 421 KETIEELR---CVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIRE---KLIRLQHENKMLKINQEGSDNEK----IA 490
Cdd:TIGR04523 231 KDNIEKKQqeiNEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISDLNNQKeqdwNK 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 491 LLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDaisvlLKKKLEEHLEKLHEANNELQKKRAI 570
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSE-----KQRELEEKQNEIEKLKKENQSYKQE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 571 IEDLEPRFNNSSLKIE-------ELQEALRKKEEEMKQMEERYKKYLE---KAKSVIRTLDpKQNQGAAPEIQALKNQLQ 640
Cdd:TIGR04523 386 IKNLESQINDLESKIQnqeklnqQKDEQIKKLQQEKELLEKEIERLKEtiiKNNSEIKDLT-NQDSVKELIIKNLDNTRE 464
|
410 420
....*....|....*....|....*....
gi 2090181558 641 ERDRQFHSLEKEYEKTKSQREMEEKYIVS 669
Cdd:TIGR04523 465 SLETQLKVLSRSINKIKQNLEQKQKELKS 493
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
273-663 |
2.84e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 273 EELEKEISELRQQNDELTTLADDAQSLKD----EIDVLRHSSDKVS----KLEGQVESYKKKLEDLGDLRRQVKLLEEKN 344
Cdd:TIGR00606 712 KSTESELKKKEKRRDEMLGLAPGRQSIIDlkekEIPELRNKLQKVNrdiqRLKNDIEEQETLLGTIMPEEESAKVCLTDV 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 345 TMYMQNTVSLEEELRK--ANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRSERDSLKE 422
Cdd:TIGR00606 792 TIMERFQMELKDVERKiaQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKS 871
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 423 TIEELRCVQAQEGQLttqglmplgsQESSDSLAAEIvtpeirEKLIRLQHENKmlkinqegsdnEKIALLQSLLDDANLR 502
Cdd:TIGR00606 872 EKLQIGTNLQRRQQF----------EEQLVELSTEV------QSLIREIKDAK-----------EQDSPLETFLEKDQQE 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 503 KNEL----ETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDAISVLLKKKlEEHLEKLHEANNELQKKRAIIEDlEPRF 578
Cdd:TIGR00606 925 KEELisskETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQK-ETELNTVNAQLEECEKHQEKINE-DMRL 1002
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 579 NNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQLQERDRQ---FHSLEKEYEK 655
Cdd:TIGR00606 1003 MRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNhvlALGRQKGYEK 1082
|
....*...
gi 2090181558 656 TKSQREME 663
Cdd:TIGR00606 1083 EIKHFKKE 1090
|
|
| Taf7 |
COG5414 |
TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation ... |
380-575 |
4.07e-03 |
|
TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation complex [Transcription];
Pssm-ID: 227701 Cd Length: 392 Bit Score: 40.07 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 380 NRLSEESKKADKLDFEYKRLKEKVdslqkEKDRLRSERDSLKETIEELRCVQAQEGQLTTQGLMPLG-SQESSDSLAAEI 458
Cdd:COG5414 210 DDLLEKDMKAESVSVVLKDEKELA-----RQERVSSWENFKEEPGEPLSRPALKKEKQGAEEEGEEGmSEEDLDVGAAEI 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 459 VTPEIREKLIRLQHENKMlkiNQEGSDNEKiallQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKA 538
Cdd:COG5414 285 ENKEVSEGDKEQQQEEVE---NAEAHKEEV----QSDRPDEIGEEKEEDDENEENERHTELLADELNELEKGIEEKRRQM 357
|
170 180 190
....*....|....*....|....*....|....*..
gi 2090181558 539 EDAISVLLKKKLEEHLEKLHEannELQKKRAIIEDLE 575
Cdd:COG5414 358 ESATNPILQKRFESQLNVLLK---ELELKRKQLEMEE 391
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
457-590 |
4.44e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.30 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 457 EIVTP-EIREKLIRLQHENKMLKIN--QEGSDNEKIALLQSLLDDANLRKNELET---ENRLVNQRLLEVQSQ-VEELQK 529
Cdd:PRK05771 10 LIVTLkSYKDEVLEALHELGVVHIEdlKEELSNERLRKLRSLLTKLSEALDKLRSylpKLNPLREEKKKVSVKsLEELIK 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2090181558 530 SLQDQGSKAEDAISVLLkkkleehlEKLHEANNELQKKRAIIEDLEPrFNNSSLKIEELQE 590
Cdd:PRK05771 90 DVEEELEKIEKEIKELE--------EEISELENEIKELEQEIERLEP-WGNFDLDLSLLLG 141
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
139-667 |
4.76e-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: 40.44 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 139 IMVMEESVQHVVMTAIQELMSK----ESPVSAGNDAYVDLDRQLKKTSEELNEALSAKEEIAQRCHELDLQVAALQEEKS 214
Cdd:TIGR02169 281 IKDLGEEEQLRVKEKIGELEAEiaslERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYA 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 215 SLLAENQVLMERLNQSDSiedpnsPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLAD 294
Cdd:TIGR02169 361 ELKEELEDLRAELEEVDK------EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEA 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 295 DAQSLKDEIDVLRhssDKVSKLEGQVESYKkklEDLGDLRRQVKLLEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQ 374
Cdd:TIGR02169 435 KINELEEEKEDKA---LEIKKQEWKLEQLA---ADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 375 VVELQNRLSEESKKADKLDFEYKRLKEK------VDSLQKEKDRLRSERDSLKETIEELRCVQAqeGQLTTQGLMPLGSQ 448
Cdd:TIGR02169 509 GRAVEEVLKASIQGVHGTVAQLGSVGERyataieVAAGNRLNNVVVEDDAVAKEAIELLKRRKA--GRATFLPLNKMRDE 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 449 ESSDSLAAE-------------------IVTPEIREKLI--------RLQHENKMLKINQE----------GSDNEKIAL 491
Cdd:TIGR02169 587 RRDLSILSEdgvigfavdlvefdpkyepAFKYVFGDTLVvedieaarRLMGKYRMVTLEGElfeksgamtgGSRAPRGGI 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 492 LQSLLDDANL-----RKNELETENRLVNQRLLEVQSQVEELQKSLQDqgskaedaisvlLKKKLEEHLEKLHEANNELQK 566
Cdd:TIGR02169 667 LFSRSEPAELqrlreRLEGLKRELSSLQSELRRIENRLDELSQELSD------------ASRKIGEIEKEIEQLEQEEEK 734
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 567 KRAIIEDLEPRFNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQLQERDRQF 646
Cdd:TIGR02169 735 LKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARL 814
|
570 580
....*....|....*....|.
gi 2090181558 647 HSLEKEYEKTKSQREMEEKYI 667
Cdd:TIGR02169 815 REIEQKLNRLTLEKEYLEKEI 835
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
266-376 |
6.01e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.06 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 266 DDYRIRCEELEKEISELRQQNDELTtlADDAQSLKDEIDVLRhssDKVSKLEGQVESYKKKLEDLGDLRRQvklLEEKNt 345
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEQDEAS--FERLAELRDELAELE---EELEALKARWEAEKELIEEIQELKEE---LEQRY- 484
|
90 100 110
....*....|....*....|....*....|.
gi 2090181558 346 mymQNTVSLEEELRKANAARSQLETYKRQVV 376
Cdd:COG0542 485 ---GKIPELEKELAELEEELAELAPLLREEV 512
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
260-661 |
6.82e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 39.70 E-value: 6.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 260 RLEAAKDDYRIRCEELEKEISELrqqnDELTTLADDAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKL-----EDLGDLR 334
Cdd:pfam05483 371 RLEKNEDQLKIITMELQKKSSEL----EEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELkgkeqELIFLLQ 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 335 RQVKLLEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQVVELQ---NRLSEESKK----ADKLDFEYKRLKEKVDSLQ 407
Cdd:pfam05483 447 AREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTahcDKLLLENKEltqeASDMTLELKKHQEDIINCK 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 408 KEKDRLRSERDSLKETIEELRC-VQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKINQEGSDN 486
Cdd:pfam05483 527 KQEERMLKQIENLEEKEMNLRDeLESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENK 606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 487 EKiaLLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDAISVLLKKKLEEhlEKLHEannELQK 566
Cdd:pfam05483 607 NK--NIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISE--EKLLE---EVEK 679
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 567 KRAIIEDLEPRFNNSSLKIeelQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIqALKNQLQERDRQF 646
Cdd:pfam05483 680 AKAIADEAVKLQKEIDKRC---QHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKA-ALEIELSNIKAEL 755
|
410
....*....|....*
gi 2090181558 647 HSLEKEYEKTKSQRE 661
Cdd:pfam05483 756 LSLKKQLEIEKEEKE 770
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
253-428 |
9.20e-03 |
|
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: 38.98 E-value: 9.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 253 QLQEETFRLEAAKDDYRIRCEELEKEISELRQQ----NDELTTLADDAQSLKDEIDVLRHssdKVSKLEGQVESYKKKLE 328
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRiaalARRIRALEQELAALEAELAELEK---EIAELRAELEAQKEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 329 DLgdLRRQVKLLEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQK 408
Cdd:COG4942 108 EL--LRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180
....*....|....*....|
gi 2090181558 409 EKDRLRSERDSLKETIEELR 428
Cdd:COG4942 186 ERAALEALKAERQKLLARLE 205
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
278-559 |
9.48e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 39.50 E-value: 9.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 278 EISELRQQNDELTTLADDAQsLKDEIDVLRHSSDKVSKLEgqvesyKKKLEDLGDLRrqvKLLEEKNTMYMQNTVsLEEE 357
Cdd:PLN02939 110 AIDNEQQTNSKDGEQLSDFQ-LEDLVGMIQNAEKNILLLN------QARLQALEDLE---KILTEKEALQGKINI-LEMR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 358 LRKANAaRSQLETYKRQVVELQNRLSEesKKADKLDFEYKRLKEKVDSLQKEKDRLRSERDSLKETIEELRcVQAQEGQL 437
Cdd:PLN02939 179 LSETDA-RIKLAAQEKIHVEILEEQLE--KLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLK-AELIEVAE 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090181558 438 TTQGLMPLGSQESsdslAAEIVTPEIREKLIRLQHENKMLKINQEGSDNEKIALLQSLLDDAnlrKNELEtENRLVNQRL 517
Cdd:PLN02939 255 TEERVFKLEKERS----LLDASLRELESKFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRA---TNQVE-KAALVLDQN 326
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2090181558 518 LEVQSQVEELQKSLQDQG-SKAEDAISVLLKKK---LEEHLEKLHE 559
Cdd:PLN02939 327 QDLRDKVDKLEASLKEANvSKFSSYKVELLQQKlklLEERLQASDH 372
|
|
| |
