|
Name |
Accession |
Description |
Interval |
E-value |
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
184-709 |
0e+00 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 685.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 184 ELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQEETFRLEA 263
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 264 AKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKLLEEK 343
Cdd:pfam05622 81 ARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLGDLRRQVKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 344 NTMYMQNTVSLEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKET 423
Cdd:pfam05622 161 NAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRET 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 424 IEELRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKINQEGSDNEKIALLQSLLDDANLRK 503
Cdd:pfam05622 241 NEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLGQEGSYRERLTELQQLLEDANRRK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 504 NELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDSVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFN-NSSLR 582
Cdd:pfam05622 321 NELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDsNLAQK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 583 IEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQLQERDRLFHSLEKEYEKTKTQRDMEE 662
Cdd:pfam05622 401 IDELQEALRKKDEDMKAMEERYKKYVEKAKSVIKTLDPKQNPASPPEIQALKNQLLEKDKKIEHLERDFEKSKLQREQEE 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 209869999 663 KYIVSAWYNMGMTLHKKAAEDRLASTGS-GQSFLARQRQATSTRRSYP 709
Cdd:pfam05622 481 KLIVTAWYNMGMALHRKAIEERLAGLSSpGQSFLARQRQATNARRGLS 528
|
|
| HkD_Hook3 |
cd22226 |
Hook domain found in protein Hook 3 (Hook3) and similar proteins; Hook3 is an adaptor protein ... |
8-160 |
1.65e-104 |
|
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: 315.75 E-value: 1.65e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 8 ERVELCESLLTWIQTFNVDTPCQTVEDLTNGVVMSQVLQKIDPAYFDDNWLNRIKTEVGDNWRLKISNLKKILKGILDYN 87
Cdd:cd22226 1 DRAELCESLLTWIQTFNVDAPCQTVEDLTSGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 209869999 88 HEILGQQINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQELMSK 160
Cdd:cd22226 81 HEILGQQINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMSK 153
|
|
| HOOK_N |
pfam19047 |
HOOK domain; This domain is found at the N-terminus of HOOK proteins. |
11-161 |
9.29e-96 |
|
HOOK domain; This domain is found at the N-terminus of HOOK proteins.
Pssm-ID: 465958 Cd Length: 151 Bit Score: 292.77 E-value: 9.29e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 11 ELCESLLTWIQTFNVDTPCQTVEDLTNGVVMSQVLQKIDPAYFDDNWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEI 90
Cdd:pfam19047 1 ELCDSLLTWLQTFNVPAPCATVEDLTDGVAMAQVLHQIDPSWFTEAWLSRIKEDVGDNWRLKVSNLKKILQSVVDYYQDV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 209869999 91 LGQQINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQELMSKE 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 |
4.15e-91 |
|
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: 280.67 E-value: 4.15e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 13 CESLLTWIQTFNVDTPCQTVEDLTNGVVMSQVLQKIDPAYFDDNWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEILG 92
Cdd:cd22222 1 CDSLLQWLQTFNLIAPHATAEDLSDGVAIAQVLNQIDPEYFSDSWLSKIKPDVGDNWRLKVSNLKKILKGIVDYYSEVLG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 209869999 93 QQINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQELMS 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 |
1.67e-81 |
|
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: 255.55 E-value: 1.67e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 12 LCESLLTWIQTFNVDTPCQTVEDLTNGVVMSQVLQKIDPAYFDDNWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEIL 91
Cdd:cd22225 1 LCDSLIIWLQTFNTAAPCQTVQDLTSGVAMAQVLHQIDSSWFDESWLSRIKEDVGDNWRIKMSNLKKILQGIVDYYHEFL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 92 GQQINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQELMSKE 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 |
4.68e-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: 228.22 E-value: 4.68e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 11 ELCESLLTWIQTFNVDTPCQTVEDLTNGVVMSQVLQKIDPAYFDDNWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEI 90
Cdd:cd22227 1 ELCDSLLTWLQTFQVPSPCSSYQDLTSGVAIAQVLNRIDPSWFNEAWLGRIKEDTGDNWRLKVSNLKKILQSLLEYYQDV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 91 LGQQINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQELMSK 160
Cdd:cd22227 81 LGHQVSEDHLPDVNLIGEFSDDTELGKLLQLVLGCAISCEKKQEHIQQIMTLEESVQHVVMEAIQELLTK 150
|
|
| HkD_SF |
cd22211 |
Hook domain-containing proteins superfamily; The Hook domain superfamily includes Hook adaptor ... |
14-159 |
5.75e-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: 184.79 E-value: 5.75e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 14 ESLLTWIQTFNVDTPCQTVEDLTNGVVMSQVLQKIDPAYFDDNWLNriKTEVGDNWRLKISNLKKILKGILDYNHEILGQ 93
Cdd:cd22211 2 AALLAWINTFPLSSPVESLDDLSDGVVLAEILSQIDPSYFDSEWLE--SRDSSDNWVLKLNNLKKLYRSLSKYYREVLGQ 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 209869999 94 QINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQELMS 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 |
1.86e-25 |
|
Hook domain found in the Hook-related protein (HkRP) family; The HkRP family includes Daple, Girdin and Gipie. Daple, also called Dvl-associating protein with a high frequency of leucine residues, or coiled-coil domain-containing protein 88C (CCDC88C), or Hook-related protein 2 (HkRP2), is a novel non-receptor nucleotide exchange factor (GEF) required for activation of guanine nucleotide-binding proteins (G-proteins) during non-canonical Wnt signaling. Girdin, also called Akt phosphorylation enhancer (APE), or coiled-coil domain-containing protein 88A (CCDC88A), or G alpha-interacting vesicle-associated protein (GIV), or Girders of actin filament, or Hook-related protein 1 (HkRP1), is a bifunctional modulator of guanine nucleotide-binding proteins (G proteins). It acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein G(i) alpha subunits. It also acts as a guanine nucleotide dissociation inhibitor for guanine nucleotide-binding protein G(s) subunit alpha GNAS. In addition, Girdin plays an essential role in cell migration. Gipie, also called GRP78-interacting protein induced by ER stress, or coiled-coil domain-containing protein 88B (CCDC88B), or brain leucine zipper domain-containing protein, or Hook-related protein 3 (HkRP3), is a novel actin cytoskeleton-binding protein and Akt substrate that regulates cell migratory responses in various biological contexts. It acts as a positive regulator of T-cell maturation and inflammatory function. As a microtubule-binding protein, Gipie regulates lytic granule clustering and NK cell killing. All family members contain a conserved globular Hook domain which folds as a variant of the helical calponin homology (CH) domain.
Pssm-ID: 411794 Cd Length: 149 Bit Score: 102.67 E-value: 1.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 12 LCESLLTWIQTFNVDTPCQ-TVEDLTNGVVMSQVLQKIDPAYFDDnwlnRIKTEVGDNWRLKISNLKKILKGILDYNHEI 90
Cdd:cd22223 2 LSSPLVTWAKTFADDGSAElSYTDLVDGVFLNNVMLQIDPRPFSE----VSNRNVDDDVNARIQNLDLLLRNIKSFYQEV 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 209869999 91 LGQQINdFTLPDVNLIGEHSDA----AELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQEL 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 |
9.89e-17 |
|
Hook domain found in Daple (Dvl-associating protein with a high frequency of leucine residues) and similar proteins; Protein Daple, also called coiled-coil domain-containing protein 88C (CCDC88C), or Hook-related protein 2 (HkRP2), is a novel non-receptor nucleotide exchange factor (GEF) required for activation of guanine nucleotide-binding proteins (G-proteins) during non-canonical Wnt signaling.
Pssm-ID: 411799 Cd Length: 153 Bit Score: 77.66 E-value: 9.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 16 LLTWIQTFNV-----DTPCQTVEDLTNGVVMSQVLQKIDPAYFDdnwlNRIKTEVGDNWRLKISNLKKILKGILDYNHEI 90
Cdd:cd22228 6 LVTWVKTFGPlgfgsEDKLSMYMDLVDGVFLNKIMLQIDPRPTN----QRVNKHVNNDVNLRIQNLTILVRHIKTYYQEV 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 209869999 91 LgQQINDFTLPDVNLIGEH----SDAAELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQEL 157
Cdd:cd22228 82 L-QQLIVMNLPNVLMIGKDplsgKSMEEIKKMLLLVLGCAVQCERKEEFIERIKQLDIETQAAIVSHIQEV 151
|
|
| HkD_Girdin |
cd22229 |
Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation ... |
16-157 |
4.49e-13 |
|
Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation enhancer (APE), or coiled-coil domain-containing protein 88A (CCDC88A), or G alpha-interacting vesicle-associated protein (GIV), or Girders of actin filament, or Hook-related protein 1 (HkRP1), is a bifunctional modulator of guanine nucleotide-binding proteins (G proteins). It acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein G(i) alpha subunits. It also acts as a guanine nucleotide dissociation inhibitor for guanine nucleotide-binding protein G(s) subunit alpha GNAS. In addition, Girdin plays an essential role in cell migration.
Pssm-ID: 411800 Cd Length: 156 Bit Score: 67.51 E-value: 4.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 16 LLTWIQTF-----NVDTPCQTVEDLTNGVVMSQVLQKIDPAYFDdnwlNRIKTEVGDNWRLKISNLKKILKGILDYNHEI 90
Cdd:cd22229 9 LVTWVKTFgplatGNGTPLDEYVALVDGVFLNEVMLQINPKSSN----QRVNKKVNNDASLRIQNLSILVKQIKLYYQET 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 209869999 91 LgQQINDFTLPDVNLIGEH--SDAA--ELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQEL 157
Cdd:cd22229 85 L-QQLIMMSLPNVLVLGRNplSEQGteEMKKLLLLLLGCAVQCERKEEFIERIQTLDFDTKAAVAAHIQEV 154
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
260-591 |
3.76e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.09 E-value: 3.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 260 RLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDK-VSKLEGQVESYKKKLEDL----GDLR 334
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdLARLEAEVEQLEERIAQLskelTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 335 RQVKLLEEKNTMYMQNTVSLEEEL----RKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEK 410
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIeeleAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 411 DRLRTERDSLKETIEELRCVQAQEGQLTTQglmplgSQESSDSLAAEIVTPEIREKLIRLQHENKMLKINQEGSDN---- 486
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEE------LESELEALLNERASLEEALALLRSELEELSEELRELESKRselr 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 487 EKIALLQSLLDDANLRKNELEtenrlvnQRLLEVQSQV-EELQKSLQDQGSKAEDSVLLKKKLEEHLEKLHEANNELQK- 564
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLE-------VRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPv 987
|
330 340 350
....*....|....*....|....*....|
gi 209869999 565 -KRAI--IEDLEPRFNNSSLRIEELQEALR 591
Cdd:TIGR02168 988 nLAAIeeYEELKERYDFLTAQKEDLTEAKE 1017
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
154-649 |
1.87e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.78 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 154 IQELMSKESPVSAGNDAYVDLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSI 233
Cdd:PRK03918 209 INEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 234 EdpnsPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSS--- 310
Cdd:PRK03918 289 K----EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHely 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 311 DKVSKLEGQVESYKKKLEDL--GDLRRQVKLLEEKNTmymqntvSLEEELRKANAARGQLET----YKRQVVELQ----- 379
Cdd:PRK03918 365 EEAKAKKEELERLKKRLTGLtpEKLEKELEELEKAKE-------EIEEEISKITARIGELKKeikeLKKAIEELKkakgk 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 380 ----NRLSDESKKAD----------KLDFEYKRLKEKVDGLQKEKDRLRTERD------SLKETIEELRCVQAQegqltt 439
Cdd:PRK03918 438 cpvcGRELTEEHRKElleeytaelkRIEKELKEIEEKERKLRKELRELEKVLKkeseliKLKELAEQLKELEEK------ 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 440 qglmpLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLK--INQEGSDNEKIALLQSLLDDANLRKNELETE-NRLVNQR 516
Cdd:PRK03918 512 -----LKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKkeLEKLEELKKKLAELEKKLDELEEELAELLKElEELGFES 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 517 LLEVQSQVEELQK----------SLQDQGSKAEDSVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNnsslriEEL 586
Cdd:PRK03918 587 VEELEERLKELEPfyneylelkdAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS------EEE 660
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 209869999 587 QEALRKKEEEMKQMEERYKKYLEKAKSVIRTLdpkqnqgaAPEIQALKNQLQERDRLFHSLEK 649
Cdd:PRK03918 661 YEELREEYLELSRELAGLRAELEELEKRREEI--------KKTLEKLKEELEEREKAKKELEK 715
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
130-663 |
1.90e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.40 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 130 EQKQEYIQAIMMMEESVQHVVMTAIQELMSKESPVSAGNDAYVDLDRQLKKTTEELNEALSAKEEIAqrchELDMQVAAL 209
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIE----ELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 210 QEEKSSLLAENQILMERLNQSDS-IEDPNSPAGR---------RHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEI 279
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKeIEELEEKVKElkelkekaeEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 280 SELRQQNDELTTLADEAQSLKDEIDVLRHSS---DKVSKLEGQVESYKKKLEDL--GDLRRQVKLLEEKNTmymqntvSL 354
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEELEERHelyEEAKAKKEELERLKKRLTGLtpEKLEKELEELEKAKE-------EI 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 355 EEELRKANAARGQLET----YKRQVVELQ---------NRLSDESKKAD----------KLDFEYKRLKEKVDGLQKEKD 411
Cdd:PRK03918 404 EEEISKITARIGELKKeikeLKKAIEELKkakgkcpvcGRELTEEHRKElleeytaelkRIEKELKEIEEKERKLRKELR 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 412 RLRTERD------SLKETIEELRCVQAQegqlttqglmpLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKinqegSD 485
Cdd:PRK03918 484 ELEKVLKkeseliKLKELAEQLKELEEK-----------LKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLK-----KE 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 486 NEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQ-SQVEELQKSLQDQGSKAEDSVLLK---KKLEEHLEKLHEANNE 561
Cdd:PRK03918 548 LEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKdaeKELEREEKELKKLEEE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 562 LQKKRAIIEDLEPRFNNSSLRIEELQealrkKEEEMKQMEERYKKYLEKAKSVirtldpkqnQGAAPEIQALKNQLQERD 641
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELEELE-----KKYSEEEYEELREEYLELSREL---------AGLRAELEELEKRREEIK 693
|
570 580
....*....|....*....|..
gi 209869999 642 RLFHSLEKEYEKTKTQRDMEEK 663
Cdd:PRK03918 694 KTLEKLKEELEEREKAKKELEK 715
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
153-655 |
1.44e-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: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 153 AIQELMSKESPVSAGNDAYVDLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSds 232
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL-- 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 233 iEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQ----SLKDEIDVLRH 308
Cdd:TIGR02168 315 -ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEeqleTLRSKVAQLEL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 309 ssdKVSKLEGQVESYKKKLEDLGdlRRQVKLLEEkntmymQNTVSLEEELRKANAARGQLETYKRQVVELQNRLSDESKK 388
Cdd:TIGR02168 394 ---QIASLNNEIERLEARLERLE--DRRERLQQE------IEELLKKLEEAELKELQAELEELEEELEELQEELERLEEA 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 389 ADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTQ-----GLMPLGSQ----ESSDSLAAEIV 459
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNqsglsGILGVLSElisvDEGYEAAIEAA 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 460 TPEIREKLI---------------------------------RLQHENKMLKINQEG-----SDNEKIA-----LLQSLL 496
Cdd:TIGR02168 543 LGGRLQAVVvenlnaakkaiaflkqnelgrvtflpldsikgtEIQGNDREILKNIEGflgvaKDLVKFDpklrkALSYLL 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 497 ---------DDANLRKNELETENRLV--------------------NQRLLEVQSQVEELQKSLQDQGSKAEDsvlLKKK 547
Cdd:TIGR02168 623 ggvlvvddlDNALELAKKLRPGYRIVtldgdlvrpggvitggsaktNSSILERRREIEELEEKIEELEEKIAE---LEKA 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 548 LEEHLEKLHEANNELQKKRAIIEDLEPRFNN---SSLRIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQ 624
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISAlrkDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
|
570 580 590
....*....|....*....|....*....|....*..
gi 209869999 625 GAA------PEIQALKNQLQERDRLFHSLEKEYEKTK 655
Cdd:TIGR02168 780 AEAeieeleAQIEQLKEELKALREALDELRAELTLLN 816
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
355-659 |
2.60e-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: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 355 EEELRKANAARGQLETYKRQVVEL---QNRLSDESKKADKldfeYKRLKEKVDGLQK-----EKDRLRTERDSLKETIEE 426
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELerqLKSLERQAEKAER----YKELKAELRELELallvlRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 427 LrcvqaqegqlttqglmplgsQESSDSLAAEIVTPEIREKLIRLQHenkmlkinqeGSDNEKIALLQSLLDDANLRKNEL 506
Cdd:TIGR02168 251 A--------------------EEELEELTAELQELEEKLEELRLEV----------SELEEEIEELQKELYALANEISRL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 507 ETENRLVNQRLLEVQSQVEELQKSLQDQGSK----AEDSVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLR 582
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKldelAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 209869999 583 IEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQLQERDRLFHSLEKEYEKTKTQRD 659
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE 457
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
153-590 |
3.00e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.52 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 153 AIQELMSKESPVSAGNDAYVDLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDS 232
Cdd:PRK02224 207 RLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 233 IEDpnspagrrhlqlqtqleqlqeetfRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQslkdeiDVLRHSSDK 312
Cdd:PRK02224 287 RLE------------------------ELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELR------DRLEECRVA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 313 VSKLEGQVESYKKKLEDlgdlrrqvklLEEKNTMYMQNTVSLEEELRkanAARGQLETYKRQVVELQNRLSDESKKADKL 392
Cdd:PRK02224 337 AQAHNEEAESLREDADD----------LEERAEELREEAAELESELE---EAREAVEDRREEIEELEEEIEELRERFGDA 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 393 DFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTpEIREKLIRLQH 472
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIE-EDRERVEELEA 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 473 ENKMLKINQEGSDN--EKIALLQSLLDDANLRKNELETENRLVNQR---LLEVQSQVEELQKSLQDQGSKAEDSVLLKKK 547
Cdd:PRK02224 483 ELEDLEEEVEEVEErlERAEDLVEAEDRIERLEERREDLEELIAERretIEEKRERAEELRERAAELEAEAEEKREAAAE 562
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 209869999 548 LEEHLEKLHEANNELQKKRAIIEDLEPRFNnsslRIEELQEAL 590
Cdd:PRK02224 563 AEEEAEEAREEVAELNSKLAELKERIESLE----RIRTLLAAI 601
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
282-652 |
4.72e-09 |
|
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: 60.13 E-value: 4.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 282 LRQQNDELTTLADEAQSLKDEIDVLRHSSDkvSKLEGQVESYKKKLEDL-GDLRRQVKLLEEKNTMYMQNTVSLEEELRK 360
Cdd:pfam15921 226 LRELDTEISYLKGRIFPVEDQLEALKSESQ--NKIELLLQQHQDRIEQLiSEHEVEITGLTEKASSARSQANSIQSQLEI 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 361 -ANAARGQLETYKRQVVELQNRLSDESKKADkldfEYKRLKE-KVDGLQK-------EKDRLRTERDSLketieelrcvq 431
Cdd:pfam15921 304 iQEQARNQNSMYMRQLSDLESTVSQLRSELR----EAKRMYEdKIEELEKqlvlansELTEARTERDQF----------- 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 432 aqegqlttqglmplgSQES---SDSLAAEIVTPEIREKLIRLQHENKMLKINQEGSDNEKIALLQSLLDDANLRKNELET 508
Cdd:pfam15921 369 ---------------SQESgnlDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 509 enrLVNQRLLEVQSQVEELQKSLQDQGSKAEDSVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLRIEELQE 588
Cdd:pfam15921 434 ---LLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKER 510
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 209869999 589 ALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNqgAAPEIQALKNQLQERDRLFHSLEKEYE 652
Cdd:pfam15921 511 AIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRN--VQTECEALKLQMAEKDKVIEILRQQIE 572
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
173-532 |
8.07e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.31 E-value: 8.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 173 DLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLaENQILMERLnqsdsIEDPNSPAGRRHLQLQTQLE 252
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEK-----REYEGYELLKEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 253 QLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTT-----LADEAQSLKDEIDVLrhsSDKVSKLEGQVESYKKKL 327
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKkikdlGEEEQLRVKEKIGEL---EAEIASLERSIAEKEREL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 328 EDLGDLRRQVKLLEEKNTMYMQNtvsLEEELRKANAARGQLET----YKRQVVELQNRLSDESKKADKLDFEYKRLKEKV 403
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEE---LEREIEEERKRRDKLTEeyaeLKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 404 DGLQKEKDRLRTERDSLKETIEELRCVQAQ-EGQLTTQGLMPLGSQESSDSLAAEIvtPEIREKLIRLQheNKMLKINQE 482
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADlNAAIAGIEAKINELEEEKEDKALEI--KKQEWKLEQLA--ADLSKYEQE 470
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 209869999 483 GSD-NEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQ 532
Cdd:TIGR02169 471 LYDlKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
274-611 |
8.16e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.30 E-value: 8.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 274 ELEKEISELRQQndeLTTLADEAQSLKDEIDVLRhssDKVSKLEGQVESYKKKLEDLgdlRRQVKLLEEkntmymqntvS 353
Cdd:TIGR02168 674 ERRREIEELEEK---IEELEEKIAELEKALAELR---KELEELEEELEQLRKELEEL---SRQISALRK----------D 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 354 LEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEELRC-VQA 432
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAeLTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 433 QEGQLTTQGLMPLGSQESSDSLAAEIVtpEIREKLIRLQHEnkMLKINQEgsdnekIALLQSLLDDANLRKNELETENRL 512
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLE--DLEEQIEELSED--IESLAAE------IEELEELIEELESELEALLNERAS 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 513 VNQRLLEVQSQVEELQKSLQDQGSKAEDsvlLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLRIEELQEALRK 592
Cdd:TIGR02168 885 LEEALALLRSELEELSEELRELESKRSE---LRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALEN 961
|
330
....*....|....*....
gi 209869999 593 KEEEMKQMEERYKKYLEKA 611
Cdd:TIGR02168 962 KIEDDEEEARRRLKRLENK 980
|
|
| HkD_Gipie |
cd22230 |
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar ... |
35-157 |
2.31e-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: 54.07 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 35 LTNGVVMSQVLQKIDPAyfddNWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEILgQQINDFTLPDVNLIGEH----S 110
Cdd:cd22230 47 LSNGDLLNRVMGIIDPS----PRGGPRMRGDDGPAAHRVQNLHILWGRLRDFYQEEL-QQLILSPPPDLQVMGRDpfteE 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 209869999 111 DAAELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQEL 157
Cdd:cd22230 122 AVQELEKLLRLLLGAAVQCERRELFIRHIQGLDLDVQAELAEAIQEV 168
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
368-659 |
4.16e-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: 56.99 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 368 LETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTQglmplgs 447
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ------- 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 448 qESSDSLAAEIVTPEIREKLIRLQHENKMLKINQEgSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEEL 527
Cdd:TIGR02168 752 -LSKELTELEAEIEELEERLEEAEEELAEAEAEIE-ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 528 QKSLQDQGSKAEDSVLLKKKLEEHLEKLHEANNELQKKRAIIEDleprfnnsslRIEELQEALRKKEEEMKQMEERYkky 607
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES----------ELEALLNERASLEEALALLRSEL--- 896
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 209869999 608 lEKAKSVIRTLDPKqnqgaapeIQALKNQLQERDRLFHSLEKEYEKTKTQRD 659
Cdd:TIGR02168 897 -EELSEELRELESK--------RSELRRELEELREKLAQLELRLEGLEVRID 939
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
168-575 |
4.56e-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: 4.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 168 NDAYVDLDRQLKKtteelneaLSAKEEIAQRCHELDMQVAALQeeKSSLLAENQILMERLNQSDSIEDpnspagrrhlql 247
Cdd:TIGR02168 192 EDILNELERQLKS--------LERQAEKAERYKELKAELRELE--LALLVLRLEELREELEELQEELK------------ 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 248 qtqleQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSlkdeidvlrhssdKVSKLEGQVESYKKKL 327
Cdd:TIGR02168 250 -----EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN-------------EISRLEQQKQILRERL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 328 EdlgDLRRQVKLLEEkntmymqntvSLEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQ 407
Cdd:TIGR02168 312 A---NLERQLEELEA----------QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 408 KEKDRLRTERDSLKETIEelrcvqaqegqlttqglmplgsqessdSLAAEIVtpEIREKLIRLQHENKMLKINQEGSDNE 487
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIA---------------------------SLNNEIE--RLEARLERLEDRRERLQQEIEELLKK 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 488 ----KIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDS---VLLKKKLEEHLEKLHEANN 560
Cdd:TIGR02168 430 leeaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLqarLDSLERLQENLEGFSEGVK 509
|
410
....*....|....*
gi 209869999 561 ELQKKRAIIEDLEPR 575
Cdd:TIGR02168 510 ALLKNQSGLSGILGV 524
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
260-706 |
4.69e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 4.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 260 RLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLkdeidvLRHSSDKVSKLEGQVESYKKKLEDLgdLRRQVKL 339
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAE------EYELLAELARLEQDIARLEERRREL--EERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 340 LEEkntmymqntvsLEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDS 419
Cdd:COG1196 322 EEE-----------LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 420 LKETIEELRcVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKINQEGSDNEKIALLQSLLDDa 499
Cdd:COG1196 391 ALRAAAELA-AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL- 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 500 nLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDSVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEprfnns 579
Cdd:COG1196 469 -LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE------ 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 580 slriEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQN-QGAAPEIQALKNQLQERDRLFHSLEKEYEKTKTQR 658
Cdd:COG1196 542 ----AALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKiRARAALAAALARGAIGAAVDLVASDLREADARYYV 617
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 209869999 659 DME---EKYIVSAWYNMGMTLHKKAAEDRLASTGSGQSFLARQRQATSTRR 706
Cdd:COG1196 618 LGDtllGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR 668
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
283-591 |
4.79e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.61 E-value: 4.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 283 RQQNDELTTLADEAQSLKDEIDVLRhssDKVSKLEGQVESYKKKLED----LGDLRRQVKLLEEKNTMYMQNTVSLEEEL 358
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQ---SELRRIENRLDELSQELSDasrkIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 359 RKANAARgqlETYKRQVVELQNRLSDESKKADKL-----DFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEELrcvqaq 433
Cdd:TIGR02169 747 SSLEQEI---ENVKSELKELEARIEELEEDLHKLeealnDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREI------ 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 434 EGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENkmlkinqegsDNEKIALLQSLLDDANLRKNELETENRLV 513
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN----------LNGKKEELEEELEELEAALRDLESRLGDL 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 514 NQRLLEVQSQVEELQKSLQDQGSKAEDSVLLKKKLEEHLEKLHEANNELQkkRAIIEDLEPRFNNSSL-----RIEELQE 588
Cdd:TIGR02169 888 KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE--DPKGEDEEIPEEELSLedvqaELQRVEE 965
|
...
gi 209869999 589 ALR 591
Cdd:TIGR02169 966 EIR 968
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
174-471 |
4.92e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.61 E-value: 4.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 174 LDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDsiedpnspagRRHLQLQTQLEQ 253
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK----------ERLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 254 LQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTtlADEAQSLKDEI-DVLRHSSDKVSKLEGQVESYKKKLEDlgd 332
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE--ARLSHSRIPEIqAELSKLEEEVSRIEARLREIEQKLNR--- 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 333 lRRQVKLLEEKNTMYMQNTVSLEEELRKANAAR-----GQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQ 407
Cdd:TIGR02169 824 -LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEienlnGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 209869999 408 KEKDRLRTERDSLKETIEELRC-VQAQEGQLTTQG-LMPLGSQESSDSLAAEIVTPEIREKLIRLQ 471
Cdd:TIGR02169 903 RKIEELEAQIEKKRKRLSELKAkLEALEEELSEIEdPKGEDEEIPEEELSLEDVQAELQRVEEEIR 968
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
173-643 |
6.60e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 6.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 173 DLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLA-----ENQILMERLNQSDSIEDpnspAGRRHLQL 247
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAelarlEQDIARLEERRRELEER----LEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 248 QTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRhsSDKVSKLEGQVESYKKKL 327
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA--EELLEALRAAAELAAQLE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 328 EDLGDLRRQVKLLEEKNTMYMQNTVSLEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQ 407
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 408 KEKDRLRTERDSLKETIEE----LRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLK----I 479
Cdd:COG1196 484 EELAEAAARLLLLLEAEADyegfLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVaaaaI 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 480 NQEGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDSVLLKKKLEEHLEKLHEAN 559
Cdd:COG1196 564 EYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLA 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 560 NELQKKRAIIEDLEPRFNNSSLRIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQLQE 639
Cdd:COG1196 644 GRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEE 723
|
....
gi 209869999 640 RDRL 643
Cdd:COG1196 724 EALE 727
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
213-666 |
9.79e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 9.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 213 KSSLLA-ENQILMERLNQSdsIEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTT 291
Cdd:COG4717 36 KSTLLAfIRAMLLERLEKE--ADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 292 LADEAQSLKDEIDVLRHSSD------KVSKLEGQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEELRkaNAAR 365
Cdd:COG4717 114 LREELEKLEKLLQLLPLYQElealeaELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLS--LATE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 366 GQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKdrlrtERDSLKETIEELR----------CVQAQEG 435
Cdd:COG4717 192 EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL-----EAAALEERLKEARlllliaaallALLGLGG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 436 QLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKIN-QEGSDNEKIALLQSLLDDANLRKNELETENRLVN 514
Cdd:COG4717 267 SLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPaLEELEEEELEELLAALGLPPDLSPEELLELLDRI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 515 QRLLEVQSQVEELQKSLQDQGSKAEDSVLLKK---KLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLRIEELQEALr 591
Cdd:COG4717 347 EELQELLREAEELEEELQLEELEQEIAALLAEagvEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL- 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 209869999 592 kkeeemkqMEERYKKYLEKAKSVIRTLDPKQNQgAAPEIQALKNQLQ--ERDRLFHSLEKEYEKTKTQ-RDMEEKYIV 666
Cdd:COG4717 426 --------DEEELEEELEELEEELEELEEELEE-LREELAELEAELEqlEEDGELAELLQELEELKAElRELAEEWAA 494
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
336-558 |
3.93e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 336 QVKLLEEKNTMYMQNTVSLEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRT 415
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 416 ERDSLKETIEELrcVQAQEGQLTTQGLMPLGSQESSDSLAA-----EIVTPEIREKLIRLQHENKMLKINQEGSDNEKiA 490
Cdd:COG4942 98 ELEAQKEELAEL--LRALYRLGRQPPLALLLSPEDFLDAVRrlqylKYLAPARREQAEELRADLAELAALRAELEAER-A 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 209869999 491 LLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDSVLLKKKLEEHLEKLHEA 558
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
173-427 |
4.63e-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: 53.53 E-value: 4.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 173 DLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAE-------------NQILMERLNQSDSIEDPNSP 239
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlshsripeiqaelSKLEEEVSRIEARLREIEQK 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 240 AGRRHLQLQTQLEQLQEetfrLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQ-SLKDEIDVLRHSSDKVSKLEG 318
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQE----LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEaALRDLESRLGDLKKERDELEA 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 319 QVESYKKKLEDLG----DLRRQVKLLEEKNTMYMQNTVSLEEELRK---ANAARGQLETYKRQVVELQNRLSDESKKADK 391
Cdd:TIGR02169 897 QLRELERKIEELEaqieKKRKRLSELKAKLEALEEELSEIEDPKGEdeeIPEEELSLEDVQAELQRVEEEIRALEPVNML 976
|
250 260 270
....*....|....*....|....*....|....*.
gi 209869999 392 LDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEEL 427
Cdd:TIGR02169 977 AIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
304-578 |
4.76e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.52 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 304 DVLRHSSDKVSKLEGQVES------YKKKLEDL------GDLRRQVKLLEEKNTMYMQNTVSLEEELRKANAARGQLETY 371
Cdd:TIGR02168 193 DILNELERQLKSLERQAEKaerykeLKAELRELelallvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 372 KRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEELR----CVQAQEGQLTTQGLMPLGS 447
Cdd:TIGR02168 273 RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELEskldELAEELAELEEKLEELKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 448 QESS----DSLAAEIVTPEIREKLIRLQHENKMLKI----NQEGSDNEKIALLQSLLDDANLRKNELETEN-----RLVN 514
Cdd:TIGR02168 353 LESLeaelEELEAELEELESRLEELEEQLETLRSKVaqleLQIASLNNEIERLEARLERLEDRRERLQQEIeellkKLEE 432
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 209869999 515 QRLLEVQSQVEELQKSLQDQGSKAEDSVLLKKKLEEHLEK----LHEANNELQKKRAIIEDLEPRFNN 578
Cdd:TIGR02168 433 AELKELQAELEELEEELEELQEELERLEEALEELREELEEaeqaLDAAERELAQLQARLDSLERLQEN 500
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
304-591 |
3.54e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 304 DVLRHSSDKVSKLEGQVESYKkkleDLGDLRRQVK--LLEEKNTM--------YMQNTVSLEEELRKANAARGQLEtykr 373
Cdd:COG4913 184 RRLGIGSEKALRLLHKTQSFK----PIGDLDDFVReyMLEEPDTFeaadalveHFDDLERAHEALEDAREQIELLE---- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 374 QVVELQNRLSDESKKADKLD-----FEYKRLKEKVDGLQKEKDRLRTERDSLKETIEELrcvQAQEGQLttqglmplgsq 448
Cdd:COG4913 256 PIRELAERYAAARERLAELEylraaLRLWFAQRRLELLEAELEELRAELARLEAELERL---EARLDAL----------- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 449 essdslaaeivtpeiREKLIRLQHEnkmlkinQEGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQ 528
Cdd:COG4913 322 ---------------REELDELEAQ-------IRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASA 379
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 209869999 529 KSLQDQGSKAEDSV--------LLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLRIEELQEALR 591
Cdd:COG4913 380 EEFAALRAEAAALLealeeeleALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
359-668 |
3.64e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 359 RKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEyKRLKEKVDGLQKEKDRLR-TERDSLKETIEELRcvQAQEGQL 437
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE-REKAERYQALLKEKREYEgYELLKEKEALERQK--EAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 438 TTQGLMPLGSQESSDSLAAEIVTPEIR----EKLIRLQHENKMLKINQE-GSDNEKIALLQSLLDDANLRKNELETENRL 512
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLleelNKKIKDLGEEEQLRVKEKiGELEAEIASLERSIAEKERELEDAEERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 513 VNQRLLEVQSQVEELQKSLQDQG-----------SKAEDSVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSL 581
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERkrrdklteeyaELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 582 RIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNqgaapEIQALKNQLQERDRLFHSLEKEYEKTKTQRDME 661
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL-----EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
|
....*..
gi 209869999 662 EKYIVSA 668
Cdd:TIGR02169 482 EKELSKL 488
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
327-663 |
4.10e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 327 LEDL-GDLRRQVKlleekntmymqntvSLEEELRKANAARgqleTYKRQVVELQNRLSdeSKKADKLDFEYKRLKEKVDG 405
Cdd:COG1196 191 LEDIlGELERQLE--------------PLERQAEKAERYR----ELKEELKELEAELL--LLKLRELEAELEELEAELEE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 406 LQKEKDRLRTERDSLKETIEELRCVQAQEgqlttqglmplgSQESSDSLAAEIvtpEIREKLIRLQHENKMLKinqegsd 485
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEEL------------ELELEEAQAEEY---ELLAELARLEQDIARLE------- 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 486 nEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDsvlLKKKLEEHLEKLHEANNELQKK 565
Cdd:COG1196 309 -ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE---AEEALLEAEAELAEAEEELEEL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 566 RAIIEDLEPRFNNSSLRIEELQEALRkkeeEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQLQERDRLFH 645
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEE----ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
330
....*....|....*...
gi 209869999 646 SLEKEYEKTKTQRDMEEK 663
Cdd:COG1196 461 LLELLAELLEEAALLEAA 478
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
273-427 |
1.07e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 273 EELEKEISELRQqndELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESykkkLEDLGDLRRQVklleekntmymqntV 352
Cdd:COG4913 613 AALEAELAELEE---ELAEAEERLEALEAELDALQERREALQRLAEYSWD----EIDVASAEREI--------------A 671
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 209869999 353 SLEEELRKANAARGQLETYKRQVVELQNRLsdeskkaDKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEEL 427
Cdd:COG4913 672 ELEAELERLDASSDDLAALEEQLEELEAEL-------EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
332-618 |
1.20e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.90 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 332 DLRRQVKLLEEKntmymqntvslEEELRKA-NAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEK 410
Cdd:TIGR02168 681 ELEEKIEELEEK-----------IAELEKAlAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 411 DRLRTERDSLKETIEELRCVQAQEGQLTTQGLmplgsqESSDSLAAEIVTPEIREKLIRLQHENKmlkinqegsdNEKIA 490
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAE------AEIEELEAQIEQLKEELKALREALDEL----------RAELT 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 491 LLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDSVLLKKKLEEHLEKLHEANNELQKKRAIIE 570
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 209869999 571 DLEPRFNNSSLRIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTL 618
Cdd:TIGR02168 894 SELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
260-499 |
1.68e-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: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 260 RLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQslkDEIDVLRHsSDKVSKLEGQVESYKKKLEDLGDLRRQVKL 339
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDALQERREALQRLAEYSW---DEIDVASA-EREIAELEAELERLDASSDDLAALEEQLEE 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 340 LEEKntmymqnTVSLEEELRKANAARGQLET----YKRQVVELQNRLSDESKKADKLDFEY-----------KRLKEKVD 404
Cdd:COG4913 697 LEAE-------LEELEEELDELKGEIGRLEKeleqAEEELDELQDRLEAAEDLARLELRALleerfaaalgdAVERELRE 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 405 GLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTQGLMP-LGSQESSDSLAAEIVT---PEIREKLIRLQHENKmlkin 480
Cdd:COG4913 770 NLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDAdLESLPEYLALLDRLEEdglPEYEERFKELLNENS----- 844
|
250
....*....|....*....
gi 209869999 481 qegsdNEKIALLQSLLDDA 499
Cdd:COG4913 845 -----IEFVADLLSKLRRA 858
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
259-668 |
1.71e-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: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 259 FRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEI--DVLRHSSDKVSKLEGQVEsykkkledlgDLRRQ 336
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELeaQIRGNGGDRLEQLEREIE----------RLERE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 337 VKLLEEKNTMYMQNTVSLEEElrkANAARGQLETYKRQVVELQNRLSDESKKA----DKLDFEYKRLKEKVDGLQKEKDR 412
Cdd:COG4913 354 LEERERRRARLEALLAALGLP---LPASAEEFAALRAEAAALLEALEEELEALeealAEAEAALRDLRRELRELEAEIAS 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 413 LRTERDSLKETIEELRCVQAQE---------------------------------------------------------- 434
Cdd:COG4913 431 LERRKSNIPARLLALRDALAEAlgldeaelpfvgelievrpeeerwrgaiervlggfaltllvppehyaaalrwvnrlhl 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 435 -GQLTTQGLMPLGSQE-----SSDSLAAEIVT------PEIREKLIR------------LQHENK------MLKINQE-- 482
Cdd:COG4913 511 rGRLVYERVRTGLPDPerprlDPDSLAGKLDFkphpfrAWLEAELGRrfdyvcvdspeeLRRHPRaitragQVKGNGTrh 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 483 --------------GSDN-EKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKsLQDQGSKAEDSVLLKKK 547
Cdd:COG4913 591 ekddrrrirsryvlGFDNrAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQR-LAEYSWDEIDVASAERE 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 548 ---LEEHLEKLHEANNELQKKRAIIEDLEprfnnssLRIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQ 624
Cdd:COG4913 670 iaeLEAELERLDASSDDLAALEEQLEELE-------AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 209869999 625 GAAPEIQALKNQLQE------RDRLFHSLEKEYEKTKTQRDMEEKYIVSA 668
Cdd:COG4913 743 ARLELRALLEERFAAalgdavERELRENLEERIDALRARLNRAEEELERA 792
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
260-426 |
1.81e-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: 46.84 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 260 RLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDV-LRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVK 338
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKeIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 339 LLEEKNTMYMQNTVsLEEELRKANAargQLETYKRQVVELQNRLSdesKKADKLDFEYKRLKEKVDGLQKEKDRLRTERD 418
Cdd:COG1579 94 LQKEIESLKRRISD-LEDEILELME---RIEELEEELAELEAELA---ELEAELEEKKAELDEELAELEAELEELEAERE 166
|
....*...
gi 209869999 419 SLKETIEE 426
Cdd:COG1579 167 ELAAKIPP 174
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
301-590 |
2.96e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 301 DEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEELRKANAargQLETYKRQVVELQN 380
Cdd:PRK03918 138 DAILESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEK---ELEEVLREINEISS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 381 RLSDESKKADKLDFEYKRL---KEKVDGLQKEKDRLRTERDSLKETIEELRcvqaqegqlttqglmplgsqessDSLAae 457
Cdd:PRK03918 215 ELPELREELEKLEKEVKELeelKEEIEELEKELESLEGSKRKLEEKIRELE-----------------------ERIE-- 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 458 ivtpEIREKLIRLQHENKMLKINQEgsDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSK 537
Cdd:PRK03918 270 ----ELKKEIEELEEKVKELKELKE--KAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL 343
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 209869999 538 AEDSVLLKKKLEEhLEKLHEANNELQKKRAIIEDLEPRFNNssLRIEELQEAL 590
Cdd:PRK03918 344 KKKLKELEKRLEE-LEERHELYEEAKAKKEELERLKKRLTG--LTPEKLEKEL 393
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
360-567 |
3.02e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 360 KANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEELRCV-------QA 432
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElgeraraLY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 433 QEGQLTTQGLMPLGSQESSDSLaaeivtpeireklirlqheNKMLKINQ-EGSDNEKIALLQSLLDDANLRKNELETENR 511
Cdd:COG3883 97 RSGGSVSYLDVLLGSESFSDFL-------------------DRLSALSKiADADADLLEELKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 209869999 512 LVNQRLLEVQSQVEELQKSLQDQGSKAEDSVLLKKKLEEHLEKLHEANNELQKKRA 567
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
173-639 |
3.04e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 173 DLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDpnsPAGRRHLQLQTQLE 252
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA---EAEEELEELAEELL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 253 QLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDEL-TTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLG 331
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELeEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 332 DLRRQVKLLEEKNTMYMQNTVSLEEELRKANA-ARGQLETYKR-QVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKE 409
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEAdYEGFLEGVKAaLLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 410 KDRLRTERDsLKETIEELRcvQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKmLKINQEGSDNEKI 489
Cdd:COG1196 550 NIVVEDDEV-AAAAIEYLK--AAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREAD-ARYYVLGDTLLGR 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 490 ALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGS----KAEDSVLLKKKLEEHLEKLHEANNELQKK 565
Cdd:COG1196 626 TLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAalleAEAELEELAERLAEEELELEEALLAEEEE 705
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 209869999 566 RAIIEDLEPRFNNSSLRIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQgAAPEIQALKNQLQE 639
Cdd:COG1196 706 ERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEE-LERELERLEREIEA 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
173-427 |
3.45e-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: 47.36 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 173 DLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQ-----------SDSIEDPNSPAG 241
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaanlrerLESLERRIAATE 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 242 RRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDE-IDVLRHSSDKVSKLEGQV 320
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEElSEELRELESKRSELRREL 917
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 321 ESYKKKLEDLgDLRRQ---VKLLEEKNTMYMQNTVSLEEELRKANAARGQLETYKRQVVELQNRLSD---------Eskk 388
Cdd:TIGR02168 918 EELREKLAQL-ELRLEgleVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaaiE--- 993
|
250 260 270
....*....|....*....|....*....|....*....
gi 209869999 389 adkldfEYKRLKEKVDGLQKEKDRLRTERDSLKETIEEL 427
Cdd:TIGR02168 994 ------EYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
260-577 |
3.64e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 260 RLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDL------ 333
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAeeenki 1661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 334 -RRQVKLLEEKNTMYMQNTVSLEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDR 412
Cdd:PTZ00121 1662 kAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE 1741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 413 LRTERDSLKETIEELRCVQAQEGQLTTQGLMPLGSQEssdSLAAEIVTPEIREKLIRLQHENKMLKIN----QEGSDNEK 488
Cdd:PTZ00121 1742 DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE---AVIEEELDEEDEKRRMEVDKKIKDIFDNfaniIEGGKEGN 1818
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 489 IALLQSLLDDANLRKNELETENRLVNQRlLEVQSQVEELQKSLQDQGSKAEDSVLLKKKLEEHLEKLHEANNELQKKRAI 568
Cdd:PTZ00121 1819 LVINDSKEMEDSAIKEVADSKNMQLEEA-DAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDD 1897
|
....*....
gi 209869999 569 IEDLEPRFN 577
Cdd:PTZ00121 1898 IEREIPNNN 1906
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
273-613 |
7.31e-05 |
|
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: 46.26 E-value: 7.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 273 EELEKEISELRQQNDELTTLADEAQSLKDE-------IDVLRHSSD----KVSKLEGQVESYKKKLEdlGDLRRQVKLLE 341
Cdd:pfam15921 377 DQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDdrnmEVQRLEALLKAMKSECQ--GQMERQMAAIQ 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 342 EKN------TMYMQNTVSLEEELRKA----NAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKD 411
Cdd:pfam15921 455 GKNeslekvSSLTAQLESTKEMLRKVveelTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQ 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 412 RLRTERDSLKETieelrcvqaqegqlttqglmplgsQESSDSLAAEIVTPEIREKLIRLQHENKMLKINQEGSDNEKI-- 489
Cdd:pfam15921 535 HLKNEGDHLRNV------------------------QTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMqv 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 490 --ALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQ---KSLQDQGSKAEDSVL-LKKKLEEHLEKLHEANNELq 563
Cdd:pfam15921 591 ekAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLElekVKLVNAGSERLRAVKdIKQERDQLLNEVKTSRNEL- 669
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 209869999 564 kkraiiedleprfNNSSLRIEELQEALRKKEEEMKQMEERYKKYLEKAKS 613
Cdd:pfam15921 670 -------------NSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQS 706
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
299-591 |
1.48e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 45.35 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 299 LKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEEL-RKANAARGQLETYKRQVVE 377
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLaKEEEELKSELLKLERRKVD 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 378 LQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEELRCVQAQEgqlttqglmplgSQESSDSLAAE 457
Cdd:pfam02463 312 DEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKL------------EQLEEELLAKK 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 458 IVTPEIREKLIRLQHENKMLKINQEGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSK 537
Cdd:pfam02463 380 KLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELK 459
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 209869999 538 AEDSVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLRIEELQEALR 591
Cdd:pfam02463 460 LLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLL 513
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
261-428 |
1.61e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 261 LEAAKDDYRIRCEELEKEISELRQQNDeLTTLADEAQSLKDEIDVLRhssDKVSKLEGQVESYKKKLEdlgDLRRQVKLL 340
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNG-LVDLSEEAKLLLQQLSELE---SQLAEARAELAEAEARLA---ALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 341 EEKNTMYMQNTV--SLEEELRKANAARGQLET-----------YKRQVVELQNRLSDESKKA-DKLDFEYKRLKEKVDGL 406
Cdd:COG3206 253 PDALPELLQSPViqQLRAQLAELEAELAELSArytpnhpdviaLRAQIAALRAQLQQEAQRIlASLEAELEALQAREASL 332
|
170 180
....*....|....*....|..
gi 209869999 407 QKEKDRLRTERDSLKETIEELR 428
Cdd:COG3206 333 QAQLAQLEARLAELPELEAELR 354
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
351-591 |
1.64e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 351 TVSLEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTE----RDSLKETIEE 426
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKvkelKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 427 LRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIvtpeirEKLIRlQHENKMLKINQEGSDNEKIALLQSLLDDAnLRKNEL 506
Cdd:COG1340 87 LNELREELDELRKELAELNKAGGSIDKLRKEI------ERLEW-RQQTEVLSPEEEKELVEKIKELEKELEKA-KKALEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 507 ETENRLVNQRLLEVQSQVEELQKSLQ---DQGSKAEDSVL-LKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLR 582
Cdd:COG1340 159 NEKLKELRAELKELRKEAEEIHKKIKelaEEAQELHEEMIeLYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKE 238
|
....*....
gi 209869999 583 IEELQEALR 591
Cdd:COG1340 239 LRELRKELK 247
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
193-439 |
1.88e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 193 EEIAQRCHELDMQVAALQEEKSSL---LAENQILMERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDDYR 269
Cdd:PRK02224 471 EEDRERVEELEAELEDLEEEVEEVeerLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELE 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 270 IRCEELEKEISELRQQNDE----LTTLADEAQSLKDEIDVL---RHSSDKVSKLEGQVESYKKKLEDLGDLRRQVK-LLE 341
Cdd:PRK02224 551 AEAEEKREAAAEAEEEAEEareeVAELNSKLAELKERIESLeriRTLLAAIADAEDEIERLREKREALAELNDERReRLA 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 342 EKNTMYMQNTVSLEEE-LRKANAARGQLETYKRQVVElqnrlsdeskKADKLDFEYKRLKEKVDGLQ---KEKDRLRTER 417
Cdd:PRK02224 631 EKRERKRELEAEFDEArIEEAREDKERAEEYLEQVEE----------KLDELREERDDLQAEIGAVEnelEELEELRERR 700
|
250 260
....*....|....*....|..
gi 209869999 418 DSLKETIEELRCVQAQEGQLTT 439
Cdd:PRK02224 701 EALENRVEALEALYDEAEELES 722
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
276-428 |
2.04e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 276 EKEISELRQQNDE--------LTTLADEAQSLKDEIDVLrhsSDKVSKLEGQVESYKKKLEDLG----DLRRQVKLLEEK 343
Cdd:PHA02562 201 NKNIEEQRKKNGEniarkqnkYDELVEEAKTIKAEIEEL---TDELLNLVMDIEDPSAALNKLNtaaaKIKSKIEQFQKV 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 344 NTMYMQNTV-----------------------SLEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLK 400
Cdd:PHA02562 278 IKMYEKGGVcptctqqisegpdritkikdklkELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLV 357
|
170 180
....*....|....*....|....*...
gi 209869999 401 EKVDGLQKEKDRLRTERDSLKETIEELR 428
Cdd:PHA02562 358 DKAKKVKAAIEELQAEFVDNAEELAKLQ 385
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
334-428 |
3.35e-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: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 334 RRQVKLLEEKNTMYMQNTVSLEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLK----------EKV 403
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARseerreirkdREI 467
|
90 100
....*....|....*....|....*
gi 209869999 404 DGLQKEKDRLRTERDSLKETIEELR 428
Cdd:COG2433 468 SRLDREIERLERELEEERERIEELK 492
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
395-663 |
3.67e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 395 EYKRLKEKVDGLQKEKDRLRTERDSLKETIEELRcVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHEN 474
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELS-QELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 475 KMLKinQEGSDNEK-IALLQslLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDsvlLKKKLEEHLE 553
Cdd:TIGR02169 754 ENVK--SELKELEArIEELE--EDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE---IEQKLNRLTL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 554 KLHEANNELQKKRAIIEDLEPRFNNSSLRIEELQEALRKKEEEmkqmeerykkyLEKAKSVIRTLDpKQNQGAAPEIQAL 633
Cdd:TIGR02169 827 EKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE-----------LEELEAALRDLE-SRLGDLKKERDEL 894
|
250 260 270
....*....|....*....|....*....|
gi 209869999 634 KNQLQErdrlfhsLEKEYEKTKTQRDMEEK 663
Cdd:TIGR02169 895 EAQLRE-------LERKIEELEAQIEKKRK 917
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
364-641 |
3.93e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 364 ARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDsLKETIEELRCVQAQEGQLTtqglm 443
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID-VASAEREIAELEAELERLD----- 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 444 plgsqESSDSLAAeivtpeireklirLQhenkmlkinqegsdnEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQ 523
Cdd:COG4913 682 -----ASSDDLAA-------------LE---------------EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE 728
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 524 VEELQKSLQDQGSKAEdsVLLKKKLEEHLEKLHEANNELQKKRAI---IEDLEPRFNNSSLRIEELQEAlrkkeeemkqm 600
Cdd:COG4913 729 LDELQDRLEAAEDLAR--LELRALLEERFAAALGDAVERELRENLeerIDALRARLNRAEEELERAMRA----------- 795
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 209869999 601 eerykkYLEKAKSVIRTLDPkqNQGAAPEIQALKNQLQERD 641
Cdd:COG4913 796 ------FNREWPAETADLDA--DLESLPEYLALLDRLEEDG 828
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
174-413 |
3.93e-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: 43.89 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 174 LDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDPnspAGRRHLQLQTQLEQ 253
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE---LRAELTLLNEEAAN 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 254 LQEETFRLEAAKDDYRIRCEELEKEISELRQQndeLTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLED-LGD 332
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSED---IESLAAEIEELEELIEELESELEALLNERASLEEALALLRSeLEE 898
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 333 LRRQVKLLEEKNTMYMQNTVSLEEELRKANAARGQLETykrQVVELQNRLSDE--------SKKADKLDFEYKRLKEKVD 404
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLELRLEGLEV---RIDNLQERLSEEysltleeaEALENKIEDDEEEARRRLK 975
|
....*....
gi 209869999 405 GLQKEKDRL 413
Cdd:TIGR02168 976 RLENKIKEL 984
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
176-425 |
4.01e-04 |
|
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: 43.58 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 176 RQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAE---------------NQILMERLNQSDSIEDPNSPA 240
Cdd:pfam05557 58 RLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADarevisclknelselRRQIQRAELELQSTNSELEEL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 241 GRRHLQLQTQLEQLQEETFRLEAAKD---DYRIRCEELEKEIS-------ELRQQNDELTTLAD---EAQSLKDEIDVLR 307
Cdd:pfam05557 138 QERLDLLKAKASEAEQLRQNLEKQQSslaEAEQRIKELEFEIQsqeqdseIVKNSKSELARIPElekELERLREHNKHLN 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 308 HSSDKVSKLEGQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEE-------ELRKANAARGQLETY--------- 371
Cdd:pfam05557 218 ENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKlaqdtglNLRSPEDLSRRIEQLqqreivlke 297
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 209869999 372 ------------KRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIE 425
Cdd:pfam05557 298 enssltssarqlEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILE 363
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
260-655 |
4.02e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 260 RLEAAKDdyriRCEELEKEISELRQQNDELTTLADE---AQSLKDEIDVLRHSSDKVSKLEG---QVESYKKKLEDLGDL 333
Cdd:PTZ00121 1358 EAEAAEE----KAEAAEKKKEEAKKKADAAKKKAEEkkkADEAKKKAEEDKKKADELKKAAAakkKADEAKKKAEEKKKA 1433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 334 RRQVKLLEEKNTMymQNTVSLEEELRKANAARGQLETyKRQVVELQNRlSDESKKADKLDFEYKRLKEKVDGLQKeKDRL 413
Cdd:PTZ00121 1434 DEAKKKAEEAKKA--DEAKKKAEEAKKAEEAKKKAEE-AKKADEAKKK-AEEAKKADEAKKKAEEAKKKADEAKK-AAEA 1508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 414 RTERDSLKETIEELRCVQAQEGQlttqglmplgSQESSDSL--AAEIVTPEIREKLIRLQHENKMLKINQEGSDNEkial 491
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAE----------EAKKADEAkkAEEKKKADELKKAEELKKAEEKKKAEEAKKAEE---- 1574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 492 lqslldDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDSVLLK---KKLEEHLEKLHEANNELQKKRAI 568
Cdd:PTZ00121 1575 ------DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAeelKKAEEEKKKVEQLKKKEAEEKKK 1648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 569 IEDLEPRFNNSSLRIEELQ----------EALRKKEEEMKQMEERYKKYLEKAKSVIRTldPKQNQGAAPEIQALKNQLQ 638
Cdd:PTZ00121 1649 AEELKKAEEENKIKAAEEAkkaeedkkkaEEAKKAEEDEKKAAEALKKEAEEAKKAEEL--KKKEAEEKKKAEELKKAEE 1726
|
410
....*....|....*..
gi 209869999 639 ERDRLFHSLEKEYEKTK 655
Cdd:PTZ00121 1727 ENKIKAEEAKKEAEEDK 1743
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
261-554 |
4.12e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.06 E-value: 4.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 261 LEAAKDDYRIRCEELEKEISELRQQNDELTT-LADEAQSLKDEIDVLR-----HSSDKVSKLEGQVESYKKKLEDLGDLR 334
Cdd:pfam12128 609 AEEALQSAREKQAAAEEQLVQANGELEKASReETFARTALKNARLDLRrlfdeKQSEKDKKNKALAERKDSANERLNSLE 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 335 RQVKLLEEKNTMYmqntvsLEEELRKANAARGQLETYKRQVVELQNRLSDESKKAdkLDFEYKRLKEKVDGLQKEKDR-- 412
Cdd:pfam12128 689 AQLKQLDKKHQAW------LEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAA--IAARRSGAKAELKALETWYKRdl 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 413 ------------LRTERDSLKETIEELrcvqAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKIN 480
Cdd:pfam12128 761 aslgvdpdviakLKREIRTLERKIERI----AVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIAD 836
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 209869999 481 QEgSDNEKIALLQSLLDDANLRKNELETENRLVNQRL--LEVQSQVEELQKSLQDQGSKAEDSVLLKKKLEEHLEK 554
Cdd:pfam12128 837 TK-LRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLatLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKK 911
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
261-590 |
4.18e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.66 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 261 LEAAKDDYRIRCEE----LEKEISELRQQNDELTTLADEAQSLKDEIDVlrhSSDKVSKLEGQVESYKKKLED----LGD 332
Cdd:pfam10174 343 LQTEVDALRLRLEEkesfLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDV---KERKINVLQKKIENLQEQLRDkdkqLAG 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 333 LRRQVKLLEEKNTMYMQNTVSLEEELRKANAArgqLETYKRQVVELQNRLSDESKKADKldfEYKRLKEKVDGLQKEKdr 412
Cdd:pfam10174 420 LKERVKSLQTDSSNTDTALTTLEEALSEKERI---IERLKEQREREDRERLEELESLKK---ENKDLKEKVSALQPEL-- 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 413 lrTERDSLKETIEELRCVQAQEGQLTTQGLMPLgsqessdslaaEIVTPEIREKLIRLqhENKMLKINQEGSD---NEKI 489
Cdd:pfam10174 492 --TEKESSLIDLKEHASSLASSGLKKDSKLKSL-----------EIAVEQKKEECSKL--ENQLKKAHNAEEAvrtNPEI 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 490 ALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDSVLLKKKLEEHLEKLHEANNELQKKRAII 569
Cdd:pfam10174 557 NDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQ 636
|
330 340
....*....|....*....|....*...
gi 209869999 570 EDLEPRF-------NNSSLRIEELQEAL 590
Cdd:pfam10174 637 LLEEARRrednladNSQQLQLEELMGAL 664
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
273-572 |
5.84e-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: 43.09 E-value: 5.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 273 EELEKEISELRQQNDELTTLADEAQSLKDEIDVLRH--SSDKVSKLEGQVESYKKKLEDL-----------GDLRRQVKL 339
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNqkEQDWNKELKSELKNQEKKLEEIqnqisqnnkiiSQLNEQISQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 340 LEEKNTMYMQNTVSLEEELRKANAA-----------RGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQK 408
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEieklkkenqsyKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 409 EKDRLRTERDSLKETIEELRcVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHE-----NKMLKINQEG 483
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLT-NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKElkskeKELKKLNEEK 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 484 SD-NEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEdsvllKKKLEEHLEKLHEANNEL 562
Cdd:TIGR04523 506 KElEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKE-----IDEKNKEIEELKQTQKSL 580
|
330
....*....|
gi 209869999 563 QKKRAIIEDL 572
Cdd:TIGR04523 581 KKKQEEKQEL 590
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
274-615 |
6.56e-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: 43.04 E-value: 6.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 274 ELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKLLEEKNtmymqNTVS 353
Cdd:pfam02463 663 EVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDK-----INEE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 354 LEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEELRCVQAQ 433
Cdd:pfam02463 738 LKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELL 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 434 EGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKINQEGSDNEKIALLQSLLDDANLRKNEL--ETENR 511
Cdd:pfam02463 818 EEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESkeEKEKE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 512 LVNQRLLEVQSQVEELQKSLQDQGSKAEDSVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLRIEELQEALR 591
Cdd:pfam02463 898 EKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNL 977
|
330 340
....*....|....*....|....
gi 209869999 592 KKEEEMKQMEERYKKYLEKAKSVI 615
Cdd:pfam02463 978 MAIEEFEEKEERYNKDELEKERLE 1001
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
173-594 |
7.38e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 7.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 173 DLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDPnspAGRRHLQLQTQLE 252
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE---EEEALEEAAEEEA 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 253 QLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLGD 332
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 333 LRRQVKLLEEKNTMYMQNTV--------SLEEELRKANAARG------QLETYKRQVVELQNRLSDESKKADKLDFEYKR 398
Cdd:COG1196 533 EAAYEAALEAALAAALQNIVveddevaaAAIEYLKAAKAGRAtflpldKIRARAALAAALARGAIGAAVDLVASDLREAD 612
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 399 LKEKVDGLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLK 478
Cdd:COG1196 613 ARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE 692
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 479 INQEGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDSVLLKKKLEEHLEKLHEA 558
Cdd:COG1196 693 LELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERL 772
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 209869999 559 NNELQKK-----RAIIE--DLEPRFNNSSLRIEELQEALRKKE 594
Cdd:COG1196 773 EREIEALgpvnlLAIEEyeELEERYDFLSEQREDLEEARETLE 815
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
360-628 |
9.07e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 9.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 360 KANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEELrcvQAQEGQLtt 439
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL---EKEIAEL-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 440 qglmplgsqessdslaaeivtpeiREKLIRLQHE-NKMLKINQEGSDNEKIALLQSLlDDANLRKNELETENRLVNQRll 518
Cdd:COG4942 96 ------------------------RAELEAQKEElAELLRALYRLGRQPPLALLLSP-EDFLDAVRRLQYLKYLAPAR-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 519 evQSQVEELQKSLQDQGSKAEDSVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLRIEELQEALRKKEEEMK 598
Cdd:COG4942 149 --REQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
250 260 270
....*....|....*....|....*....|
gi 209869999 599 QMEERYKKYLEKAKSVIRTLDPKQNQGAAP 628
Cdd:COG4942 227 ALIARLEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
168-428 |
9.11e-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: 42.70 E-value: 9.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 168 NDAYVDLDRQLKKTTEELNEALSAKEEIAQrchELDMQVAALQEEKSSLLAENQILM-ERLNQSDSIEDPNSPAGRRHLQ 246
Cdd:TIGR04523 379 NQSYKQEIKNLESQINDLESKIQNQEKLNQ---QKDEQIKKLQQEKELLEKEIERLKeTIIKNNSEIKDLTNQDSVKELI 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 247 LQTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKK 326
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 327 LED-LGDLRRQVK---------LLEEKNTMYMQNTVSLEEELRKANAARGQLET----YKRQVVELQNRLSDESKKADKL 392
Cdd:TIGR04523 536 KESkISDLEDELNkddfelkkeNLEKEIDEKNKEIEELKQTQKSLKKKQEEKQElidqKEKEKKDLIKEIEEKEKKISSL 615
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 209869999 393 D-------FEYKRLKEKVDGLQKEKDRLRTERDSLKETIEELR 428
Cdd:TIGR04523 616 EkelekakKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIR 658
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
190-428 |
9.31e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.61 E-value: 9.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 190 SAKEEIAQRCHELD-MQVAALQEEKSS-----LLAENQILMERLNQSDSIEDPNSpagrrhlqlQTQLEQLQEETFRLEA 263
Cdd:PRK05771 16 SYKDEVLEALHELGvVHIEDLKEELSNerlrkLRSLLTKLSEALDKLRSYLPKLN---------PLREEKKKVSVKSLEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 264 AKDDYRIRCEELEKEISELrqqNDELTTLADEAQSLKDEIDVLrhssdkvsklegqvesykKKLEDLG-DLRRqvkLLEE 342
Cdd:PRK05771 87 LIKDVEEELEKIEKEIKEL---EEEISELENEIKELEQEIERL------------------EPWGNFDlDLSL---LLGF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 343 KNTMYMQNTVSLE-EELRKANAARGQLETYKRQ-------VVELQNRLSDESKKADKLDF------EYKRLKEKVDGLQK 408
Cdd:PRK05771 143 KYVSVFVGTVPEDkLEELKLESDVENVEYISTDkgyvyvvVVVLKELSDEVEEELKKLGFerleleEEGTPSELIREIKE 222
|
250 260
....*....|....*....|
gi 209869999 409 EKDRLRTERDSLKETIEELR 428
Cdd:PRK05771 223 ELEEIEKERESLLEELKELA 242
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
260-531 |
9.65e-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: 42.52 E-value: 9.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 260 RLEAAKDDYRIRCEELEKEISELRQQ-NDELTTLADEAQSLKDEIDVLrhSSDKVSKLEGQVESYKKKLEDLGDLRRQVK 338
Cdd:pfam12128 280 ERQETSAELNQLLRTLDDQWKEKRDElNGELSAADAAVAKDRSELEAL--EDQHGAFLDADIETAAADQEQLPSWQSELE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 339 LLEEKNTMYMQNTVSLEEELRKANAARGQletykrqvvelqnrlsdeskkadkldfeykRLKEKVDGLQKEKDRLRTERD 418
Cdd:pfam12128 358 NLEERLKALTGKHQDVTAKYNRRRSKIKE------------------------------QNNRDIAGIKDKLAKIREARD 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 419 SLKETIEELrcVQAQEGQLTTQ---GLMPLGSQESSDSLAAE-----IVTPEIREKLIrLQHENKMLKIN----QEGSDN 486
Cdd:pfam12128 408 RQLAVAEDD--LQALESELREQleaGKLEFNEEEYRLKSRLGelklrLNQATATPELL-LQLENFDERIErareEQEAAN 484
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 209869999 487 EKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSL 531
Cdd:pfam12128 485 AEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQL 529
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
262-663 |
1.04e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 262 EAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSlKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLGdlrrqvKLLE 341
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE-ARKADELKKAEEKKKADEAKKAEEKKKADEAK------KKAE 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 342 EKNTMymqntvslEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLK 421
Cdd:PTZ00121 1313 EAKKA--------DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAK 1384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 422 ETIEELRcvQAQEGQLTTQGLMPlGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKINQEGSDNEKIALLQSLLDDA-N 500
Cdd:PTZ00121 1385 KKAEEKK--KADEAKKKAEEDKK-KADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAeE 1461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 501 LRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDSvllkKKLEEHLEKLHEANNELQKKRAIiedlEPRFNNSS 580
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEA----KKAAEAKKKADEAKKAEEAKKAD----EAKKAEEA 1533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 581 LRIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQLQERDRLFHSLEKEYEKTKTQRDM 660
Cdd:PTZ00121 1534 KKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
|
...
gi 209869999 661 EEK 663
Cdd:PTZ00121 1614 KAE 1616
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
273-665 |
1.24e-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: 42.31 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 273 EELEKEISELR----QQNDELTTLADEAQSLKDEIDVLRHSSDK----VSKLEGQVESYKKKL-EDLGDLRRQVKLLEEK 343
Cdd:TIGR04523 78 KILEQQIKDLNdklkKNKDKINKLNSDLSKINSEIKNDKEQKNKleveLNKLEKQKKENKKNIdKFLTEIKKKEKELEKL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 344 NTMYmQNTVSLEEELRKanaargQLETYKRQVVELQNRLSDESKKADKLD---FEYKRLKEKVDGLQKEKDRLRTERDSL 420
Cdd:TIGR04523 158 NNKY-NDLKKQKEELEN------ELNLLEKEKLNIQKNIDKIKNKLLKLElllSNLKKKIQKNKSLESQISELKKQNNQL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 421 KETIEELR---CVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIRE---KLIRLQHENKMLKINQEGSDNEK----IA 490
Cdd:TIGR04523 231 KDNIEKKQqeiNEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISDLNNQKeqdwNK 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 491 LLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSkaeDSVLLKKKLEEHLEKLHEANNELQKKRAIIE 570
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES---ENSEKQRELEEKQNEIEKLKKENQSYKQEIK 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 571 DLEPRFNNSSLRIEElQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQgaapEIQALKNQLqerdrlfHSLEKE 650
Cdd:TIGR04523 388 NLESQINDLESKIQN-QEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNS----EIKDLTNQD-------SVKELI 455
|
410
....*....|....*
gi 209869999 651 YEKTKTQRDMEEKYI 665
Cdd:TIGR04523 456 IKNLDNTRESLETQL 470
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
368-660 |
1.94e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.64 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 368 LETYKRQVVELQNRLSDESKKADKLDFEYKR----LKEKVDGLQKEKDRL----RTE-------RDSLKETIEELRCVQA 432
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNELHEKQKFYLRQsvidLQTKLQEMQMERDAMadirRREsqsqedlRNQLQNTVHELEAAKC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 433 QEGQLTTQGLMPLgSQESSDSLAAEIVTPEIREKLIRLQhENKMLKINQEgsDNEKIALLQSLLDDANLRKNELETENRL 512
Cdd:pfam15921 160 LKEDMLEDSNTQI-EQLRKMMLSHEGVLQEIRSILVDFE-EASGKKIYEH--DSMSTMHFRSLGSAISKILRELDTEISY 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 513 VNQRLLEVQSQVEELQKSLQDqgsKAEdsvLLKKKLEEHLEKL---HEAN---------------NELQKKRAIIEDLEP 574
Cdd:pfam15921 236 LKGRIFPVEDQLEALKSESQN---KIE---LLLQQHQDRIEQLiseHEVEitgltekassarsqaNSIQSQLEIIQEQAR 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 575 RFNNSSLR--------IEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAP------EIQALKNQLQER 640
Cdd:pfam15921 310 NQNSMYMRqlsdlestVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQEsgnlddQLQKLLADLHKR 389
|
330 340
....*....|....*....|
gi 209869999 641 DRLFhSLEKEYEKTKTQRDM 660
Cdd:pfam15921 390 EKEL-SLEKEQNKRLWDRDT 408
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
311-423 |
1.99e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 311 DKVSKLEGQVESYKKKLEDLGDLRRQvklLEEKNTMYMQNTVSLEEELRKANAARGQLETYKRQV-------VELQNRLS 383
Cdd:PHA02562 299 DRITKIKDKLKELQHSLEKLDTAIDE---LEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAkkvkaaiEELQAEFV 375
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 209869999 384 DESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKET 423
Cdd:PHA02562 376 DNAEELAKLQDELDKIVKTKSELVKEKYHRGIVTDLLKDS 415
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
393-591 |
2.10e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 393 DFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEEL-RCVQAQEGQLTTqglmplgSQESSDSLAAEIVtpEIREKLIRLQ 471
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELnEEYNELQAELEA-------LQAEIDKLQAEIA--EAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 472 HE-NKMLKINQEGSDNEKI--ALLQS-----LLDDANLRKNELETENRLVNQrLLEVQSQVEELQKSLQDQGSKAEDsvl 543
Cdd:COG3883 86 EElGERARALYRSGGSVSYldVLLGSesfsdFLDRLSALSKIADADADLLEE-LKADKAELEAKKAELEAKLAELEA--- 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 209869999 544 LKKKLEEHLEklhEANNELQKKRAIIEDLEPRFNNSSLRIEELQEALR 591
Cdd:COG3883 162 LKAELEAAKA---ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
274-655 |
2.14e-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: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 274 ELEKEISELRQQNDELTTLADEAQS---------------LKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVK 338
Cdd:TIGR04523 215 SLESQISELKKQNNQLKDNIEKKQQeinektteisntqtqLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLK 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 339 L-LEEKNTMYMQNTVsleeelrkaNAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQ---KEKDRLR 414
Cdd:TIGR04523 295 SeISDLNNQKEQDWN---------KELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSEsenSEKQREL 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 415 TERDSLKETIEELRCVQAQEGQLTTQGLMPLGSQ-----ESSDSLAAEIVTPEIREKLIRLQHEN---KMLKINQEGSD- 485
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKiqnqeKLNQQKDEQIKKLQQEKELLEKEIERlkeTIIKNNSEIKDl 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 486 NEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDSVLLKKKLEEHLEKLHEANNELQKK 565
Cdd:TIGR04523 446 TNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEK 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 566 raiIEDLEPRFNNSSLRIEELQEAL-----RKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQ------GAAPEIQALK 634
Cdd:TIGR04523 526 ---IEKLESEKKEKESKISDLEDELnkddfELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEkqelidQKEKEKKDLI 602
|
410 420
....*....|....*....|.
gi 209869999 635 NQLQERDRLFHSLEKEYEKTK 655
Cdd:TIGR04523 603 KEIEEKEKKISSLEKELEKAK 623
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
270-428 |
2.18e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 270 IRCEELEKEISELRQ--QNDELTTLADEAQSLKDEIDVLRhssDKVSKLEGQVESYKKKLEDLgdlRRQVKLLEEKNTMy 347
Cdd:COG2433 373 IRGLSIEEALEELIEkeLPEEEPEAEREKEHEERELTEEE---EEIRRLEEQVERLEAEVEEL---EAELEEKDERIER- 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 348 mqntvsLEEELRKAnaargqletykrqvvelqnrlSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEEL 427
Cdd:COG2433 446 ------LERELSEA---------------------RSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLERL 498
|
.
gi 209869999 428 R 428
Cdd:COG2433 499 K 499
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
269-578 |
2.74e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.11 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 269 RIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKLLEEKNTMYM 348
Cdd:pfam02463 711 ELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEE 790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 349 QNTVSLEEELRKANAARgQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEELR 428
Cdd:pfam02463 791 EKEEKLKAQEEELRALE-EELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELL 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 429 CVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQ--HENKMLKINQEGSDNEKIALLQSLLDDANLRKNEL 506
Cdd:pfam02463 870 QELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLeeKENEIEERIKEEAEILLKYEEEPEELLLEEADEKE 949
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 209869999 507 ETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDSVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNN 578
Cdd:pfam02463 950 KEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
173-597 |
3.11e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 173 DLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQilMERLNQsDSIEDPNSPAGRRHLQLQTQLE 252
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG--LDDADA-EAVEARREELEDRDEELRDRLE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 253 QLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQS-----------LKDEIDVLRHSSDKVSKLEGQVE 321
Cdd:PRK02224 332 ECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREavedrreeieeLEEEIEELRERFGDAPVDLGNAE 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 322 SYKKKL-EDLGDLRRQVKLLEEKntmymqnTVSLEEELRKANAAR--------GQ----------LETYKRQVVELQNRL 382
Cdd:PRK02224 412 DFLEELrEERDELREREAELEAT-------LRTARERVEEAEALLeagkcpecGQpvegsphvetIEEDRERVEELEAEL 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 383 SDESKKADKLDFEYKRLKEKVDgLQKEKDRLRTERDSLKETIEELRC-VQAQEGQLTT-----QGLMPLGSQESSDSLAA 456
Cdd:PRK02224 485 EDLEEEVEEVEERLERAEDLVE-AEDRIERLEERREDLEELIAERREtIEEKRERAEElreraAELEAEAEEKREAAAEA 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 457 EIVTPEIREKLIRLqhENKMLKINQEGSDNEKIALLQSLLDDA-------NLRKNELETENRLVNQRLLEVQSQVEELQK 529
Cdd:PRK02224 564 EEEAEEAREEVAEL--NSKLAELKERIESLERIRTLLAAIADAedeierlREKREALAELNDERRERLAEKRERKRELEA 641
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 209869999 530 SLQDqgSKAEDSVLLKKKLEEHLEKLHEANNELQKKRaiiedleprfnnsslriEELQEALRKKEEEM 597
Cdd:PRK02224 642 EFDE--ARIEEAREDKERAEEYLEQVEEKLDELREER-----------------DDLQAEIGAVENEL 690
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
266-376 |
3.24e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.84 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 266 DDYRIRCEELEKEISELRQQNDELTtlADEAQSLKDEIDVLRhssDKVSKLEGQVESYKKKLEDLGDLRRQvklLEEKNt 345
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEQDEAS--FERLAELRDELAELE---EELEALKARWEAEKELIEEIQELKEE---LEQRY- 484
|
90 100 110
....*....|....*....|....*....|.
gi 209869999 346 mymQNTVSLEEELRKANAARGQLETYKRQVV 376
Cdd:COG0542 485 ---GKIPELEKELAELEEELAELAPLLREEV 512
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
492-590 |
3.71e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.67 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 492 LQSLLDDANLRKnELETENRLVNQRLLEVQSQVEELQKSLQDqgskaedSVLLKKKLEEHLEKLHEANNELQK-KRAIIE 570
Cdd:PRK11281 41 VQAQLDALNKQK-LLEAEDKLVQQDLEQTLALLDKIDRQKEE-------TEQLKQQLAQAPAKLRQAQAELEAlKDDNDE 112
|
90 100
....*....|....*....|
gi 209869999 571 DLEPRFNNSSLRieELQEAL 590
Cdd:PRK11281 113 ETRETLSTLSLR--QLESRL 130
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
445-708 |
3.72e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 445 LGSQESSDSLAAEIVTPEIREKL-IRLQHENKMLKINQEGSDNEKIA-LLQSLLD---DANLRKNELETENRL--VNQRL 517
Cdd:COG3206 105 LDEDPLGEEASREAAIERLRKNLtVEPVKGSNVIEISYTSPDPELAAaVANALAEaylEQNLELRREEARKALefLEEQL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 518 LEVQSQVEELQKSLQDQGSKaEDSVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLRIEELQEALRKKEEEM 597
Cdd:COG3206 185 PELRKELEEAEAALEEFRQK-NGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSP 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 598 KQMEERYKkyLEKAKSVIRTLDpKQNQGAAPEIQALKNQL--------QERDRLFHSLEKEYEKTKTQRDMEEKYIvsaw 669
Cdd:COG3206 264 VIQQLRAQ--LAELEAELAELS-ARYTPNHPDVIALRAQIaalraqlqQEAQRILASLEAELEALQAREASLQAQL---- 336
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 209869999 670 ynmgmtlhkKAAEDRLASTGSGQSFLAR-QRQATSTRRSY 708
Cdd:COG3206 337 ---------AQLEARLAELPELEAELRRlEREVEVARELY 367
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
173-577 |
3.76e-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: 40.77 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 173 DLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQ---------------SDSIEDPN 237
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEkqneieklkkenqsyKQEIKNLE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 238 SPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSD----KV 313
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTREsletQL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 314 SKLEGQVESYKKKLED-----------LGDLRRQVKLLEEKNTMYMQNTVSLEEELRKANAARGQLEtykrqvvelqNRL 382
Cdd:TIGR04523 471 KVLSRSINKIKQNLEQkqkelkskekeLKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKE----------SKI 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 383 SDESKKADKLDFEYKR--LKEKVDGLQKEKDRLRTERDSLKETIEELrcvqaqegqlttqglmplgsQESSDSLAAEI-- 458
Cdd:TIGR04523 541 SDLEDELNKDDFELKKenLEKEIDEKNKEIEELKQTQKSLKKKQEEK--------------------QELIDQKEKEKkd 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 459 VTPEIREKLIRLQHENKMLKINQEgsDNEKialLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSK- 537
Cdd:TIGR04523 601 LIKEIEEKEKKISSLEKELEKAKK--ENEK---LSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKi 675
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 209869999 538 -----------AEDSVLLKK------------KLEEHLEKLHEANNELQKKRAIIEDLEPRFN 577
Cdd:TIGR04523 676 ddiielmkdwlKELSLHYKKyitrmirikdlpKLEEKYKEIEKELKKLDEFSKELENIIKNFN 738
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
182-441 |
4.16e-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: 40.13 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 182 TEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQsdsiedpnspagrrhlqlqtqleqlqeetfrL 261
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA-------------------------------L 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 262 EAAKDDYRIRCEELEKEISELRQQNDELTT-LADEAQSLKDEIDVL-RHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKL 339
Cdd:COG4942 68 ARRIRALEQELAALEAELAELEKEIAELRAeLEAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 340 LEEKNTMYMQNTVSLEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLdfeYKRLKEKVDGLQKEKDRLRTERDS 419
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL---LARLEKELAELAAELAELQQEAEE 224
|
250 260
....*....|....*....|..
gi 209869999 420 LKETIEELRCVQAQEGQLTTQG 441
Cdd:COG4942 225 LEALIARLEAEAAAAAERTPAA 246
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
260-437 |
5.24e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.10 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 260 RLEAAKDdyrIRcEELEKEISELRQQNDELTTLADEAQSLKDEidvLRHSSDKV----SKLEGQVESYKKKLEDLgdlRR 335
Cdd:pfam15921 644 RLRAVKD---IK-QERDQLLNEVKTSRNELNSLSEDYEVLKRN---FRNKSEEMetttNKLKMQLKSAQSELEQT---RN 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 336 QVKLLEEKNTMYMQNTVSLEEELrkaNAARGQLETYKRQVVELQNRLSDESKkadkldfEYKRLKEKVDGLQKEKDRLRT 415
Cdd:pfam15921 714 TLKSMEGSDGHAMKVAMGMQKQI---TAKRGQIDALQSKIQFLEEAMTNANK-------EKHFLKEEKNKLSQELSTVAT 783
|
170 180
....*....|....*....|..
gi 209869999 416 ERDSLKETIEELRcvqAQEGQL 437
Cdd:pfam15921 784 EKNKMAGELEVLR---SQERRL 802
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
166-422 |
9.05e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 39.50 E-value: 9.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 166 AGNDAYVDLDRQLKKTTEELNEALSA-KEEIAQR-------CHELDMQVAALQEEKSSLLAENQILMERLnqsDSIEDPN 237
Cdd:PLN02939 180 SETDARIKLAAQEKIHVEILEEQLEKlRNELLIRgateglcVHSLSKELDVLKEENMLLKDDIQFLKAEL---IEVAETE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 238 SPAGRRHLQLQTQLEQLQEETFRLEAAKDDYR----IRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRhssDKV 313
Cdd:PLN02939 257 ERVFKLEKERSLLDASLRELESKFIVAQEDVSklspLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLR---DKV 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 314 SKLEGQVES---YKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSleeelrkanaargQLETYKRQVVELQ---NRLSDESK 387
Cdd:PLN02939 334 DKLEASLKEanvSKFSSYKVELLQQKLKLLEERLQASDHEIHS-------------YIQLYQESIKEFQdtlSKLKEESK 400
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 209869999 388 K------ADKLDFEY-KRLKEKVDGLQKEKDRLRTERDSLKE 422
Cdd:PLN02939 401 KrslehpADDMPSEFwSRILLLIDGWLLEKKISNNDAKLLRE 442
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
175-411 |
9.28e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.04 E-value: 9.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 175 DRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSiedpnspagrrhlqlqtqleql 254
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA---------------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209869999 255 qeetfRLEAAKDDYRIRCEELEKEISELRQQNDELTTLAD--EAQSLKDEIDvlrhssdKVSKLEGQVESYKKKLEDLGD 332
Cdd:COG3883 73 -----EIAEAEAEIEERREELGERARALYRSGGSVSYLDVllGSESFSDFLD-------RLSALSKIADADADLLEELKA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 209869999 333 LRRQVKLLEEKntmymqntvsLEEELRKANAARGQLETYKRqvvELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKD 411
Cdd:COG3883 141 DKAELEAKKAE----------LEAKLAELEALKAELEAAKA---ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| |
