|
Name |
Accession |
Description |
Interval |
E-value |
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
184-735 |
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: 670.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 184 ELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQEETFRLEA 263
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 264 AKDDYRIRCEELEKEIAELRQQTEELTTLAEEAQSLKDEIDVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQVKLLEEK 343
Cdd:pfam05622 81 ARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLGDLRRQVKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 344 NTMYMQNTVSLEEELRKANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERDSLKET 423
Cdd:pfam05622 161 NAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRET 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 424 IEELRCVQAQEGQLTTTGLMPLGRQEPSDSLAAEIITPEIKEKLIRLQHENKMLKLNQEGSDNEKIALLQSLLDDANLRK 503
Cdd:pfam05622 241 NEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLGQEGSYRERLTELQQLLEDANRRK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 504 NELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDflllaavllytnvisvswhglllkaiSVLLKKKLEEHLEKLHE 583
Cdd:pfam05622 321 NELETQNRLANQRILELQQQVEELQKALQEQGSKAED--------------------------SSLLKQKLEEHLEKLHE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 584 ANNELQKKRAIIEDLEPRCN-NSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQ 662
Cdd:pfam05622 375 AQSELQKKKEQIEELEPKQDsNLAQKIDELQEALRKKDEDMKAMEERYKKYVEKAKSVIKTLDPKQNPASPPEIQALKNQ 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2006390933 663 LQERDRMFHSLEKEYEKTKSQREMEEKFIVSAWYNMGMTLHKKAAEDRLASTGS-GQSFLARQRQATSTRRSYP 735
Cdd:pfam05622 455 LLEKDKKIEHLERDFEKSKLQREQEEKLIVTAWYNMGMALHRKAIEERLAGLSSpGQSFLARQRQATNARRGLS 528
|
|
| HkD_Hook3 |
cd22226 |
Hook domain found in protein Hook 3 (Hook3) and similar proteins; Hook3 is an adaptor protein ... |
8-160 |
4.73e-102 |
|
Hook domain found in protein Hook 3 (Hook3) and similar proteins; Hook3 is an adaptor protein for microtubule-dependent intracellular vesicle and protein trafficking. It is involved in Golgi and endosome transport. It acts as a scaffold for the opposite-polarity microtubule-based motors cytoplasmic dynein-1 and the kinesin KIF1C. It may participate in the turnover of the endocytosed scavenger receptor. Hook3 is a component of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex.
Pssm-ID: 411797 Cd Length: 153 Bit Score: 309.98 E-value: 4.73e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 8 ERAELGESLLTWIQTFNVEAPCQTVEDLTSGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKVSNLKKILKGILDYN 87
Cdd:cd22226 1 DRAELCESLLTWIQTFNVDAPCQTVEDLTSGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2006390933 88 HEILGQQINDFTLPDVNLIGEHADAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMSK 160
Cdd:cd22226 81 HEILGQQINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMSK 153
|
|
| HOOK_N |
pfam19047 |
HOOK domain; This domain is found at the N-terminus of HOOK proteins. |
11-161 |
1.10e-93 |
|
HOOK domain; This domain is found at the N-terminus of HOOK proteins.
Pssm-ID: 465958 Cd Length: 151 Bit Score: 288.15 E-value: 1.10e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 11 ELGESLLTWIQTFNVEAPCQTVEDLTSGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKVSNLKKILKGILDYNHEI 90
Cdd:pfam19047 1 ELCDSLLTWLQTFNVPAPCATVEDLTDGVAMAQVLHQIDPSWFTEAWLSRIKEDVGDNWRLKVSNLKKILQSVVDYYQDV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2006390933 91 LGQQINDFTLPDVNLIGEHADAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMSKE 161
Cdd:pfam19047 81 LGQQISDFLLPDVNLIGEHSDPAELGRLLQLILGCAVNCEKKQEYIQQIMTLEESVQHVVMTAIQELMSKD 151
|
|
| HkD_Hook |
cd22222 |
Hook domain found in Hook family of microtubule-binding proteins; The Hook family includes ... |
14-159 |
4.24e-90 |
|
Hook domain found in Hook family of microtubule-binding proteins; The Hook family includes Hook1-3. Hook1 is a microtubule-binding protein required for spermatid differentiation. Hook2, also a microtubule-binding protein, contributes to the establishment and maintenance of centrosome function. It may function in the positioning or formation of aggresomes, which are pericentriolar accumulations of misfolded proteins, proteasomes and chaperones. Hook3 is an adaptor protein for microtubule-dependent intracellular vesicle and protein trafficking. It is involved in Golgi and endosome transport. It acts as a scaffold for the opposite-polarity microtubule-based motors cytoplasmic dynein-1 and the kinesin KIF1C. It may participate in the turnover of the endocytosed scavenger receptor. Hook proteins are components of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex. Hook adaptor proteins share an N-terminal conserved globular Hook domain, which folds as a variant of the helical calponin homology (CH) domain, and contacts the helix alpha1 of dynein light intermediate chain 1 (LIC1) in a hydrophobic groove.
Pssm-ID: 411793 Cd Length: 147 Bit Score: 278.75 E-value: 4.24e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 14 ESLLTWIQTFNVEAPCQTVEDLTSGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKVSNLKKILKGILDYNHEILGQ 93
Cdd:cd22222 2 DSLLQWLQTFNLIAPHATAEDLSDGVAIAQVLNQIDPEYFSDSWLSKIKPDVGDNWRLKVSNLKKILKGIVDYYSEVLGQ 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2006390933 94 QINDFTLPDVNLIGEHADAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMS 159
Cdd:cd22222 82 QISGFTMPDVNAIAEKEDPKELGRLLQLVLGCAVNCERKEEYIQAIMGLEESVQHVVMEAIQELMS 147
|
|
| HkD_Hook1 |
cd22225 |
Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a ... |
12-161 |
2.72e-80 |
|
Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a microtubule-binding protein required for spermatid differentiation. It is a component of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex.
Pssm-ID: 411796 Cd Length: 150 Bit Score: 253.23 E-value: 2.72e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 12 LGESLLTWIQTFNVEAPCQTVEDLTSGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKVSNLKKILKGILDYNHEIL 91
Cdd:cd22225 1 LCDSLIIWLQTFNTAAPCQTVQDLTSGVAMAQVLHQIDSSWFDESWLSRIKEDVGDNWRIKMSNLKKILQGIVDYYHEFL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 92 GQQINDFTLPDVNLIGEHADAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMSKE 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 |
7.67e-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: 7.67e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 11 ELGESLLTWIQTFNVEAPCQTVEDLTSGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKVSNLKKILKGILDYNHEI 90
Cdd:cd22227 1 ELCDSLLTWLQTFQVPSPCSSYQDLTSGVAIAQVLNRIDPSWFNEAWLGRIKEDTGDNWRLKVSNLKKILQSLLEYYQDV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 91 LGQQINDFTLPDVNLIGEHADAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMSK 160
Cdd:cd22227 81 LGHQVSEDHLPDVNLIGEFSDDTELGKLLQLVLGCAISCEKKQEHIQQIMTLEESVQHVVMEAIQELLTK 150
|
|
| HkD_SF |
cd22211 |
Hook domain-containing proteins superfamily; The Hook domain superfamily includes Hook adaptor ... |
13-159 |
5.59e-53 |
|
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: 179.78 E-value: 5.59e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 13 GESLLTWIQTFNVEAPCQTVEDLTSGVVMAQVLQKIDPAYFDENWLNriKTEVGDNWRLKVSNLKKILKGILDYNHEILG 92
Cdd:cd22211 1 EAALLAWINTFPLSSPVESLDDLSDGVVLAEILSQIDPSYFDSEWLE--SRDSSDNWVLKLNNLKKLYRSLSKYYREVLG 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2006390933 93 QQINDFTLPDVNLIGEHADAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMS 159
Cdd:cd22211 79 QQLSDLPLPDLSAIARDGDEEEIVKLLELVLGAAVQCENKEEYIARIQQLDESTQAELMLIIQEVLE 145
|
|
| HkD_HkRP |
cd22223 |
Hook domain found in the Hook-related protein (HkRP) family; The HkRP family includes Daple, ... |
15-157 |
1.05e-23 |
|
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: 97.66 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 15 SLLTWIQTFNVEAPCQ-TVEDLTSGVVMAQVLQKIDPAYFDEnwlnRIKTEVGDNWRLKVSNLKKILKGILDYNHEILGQ 93
Cdd:cd22223 5 PLVTWAKTFADDGSAElSYTDLVDGVFLNNVMLQIDPRPFSE----VSNRNVDDDVNARIQNLDLLLRNIKSFYQEVLQQ 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2006390933 94 QINdFTLPDVNLIGEHADA----AELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQEL 157
Cdd:cd22223 81 LIV-MKLPDILTIGREPESeqslEELEKLLLLLLGCAVQCERKEEFIERIKNLDLEVQHALVACIQEV 147
|
|
| HkD_Daple |
cd22228 |
Hook domain found in Daple (Dvl-associating protein with a high frequency of leucine residues) ... |
12-157 |
5.37e-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: 78.81 E-value: 5.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 12 LGESLLTWIQTFNV-----EAPCQTVEDLTSGVVMAQVLQKIDPAYFDEnwlnRIKTEVGDNWRLKVSNLKKILKGILDY 86
Cdd:cd22228 2 LQSPLVTWVKTFGPlgfgsEDKLSMYMDLVDGVFLNKIMLQIDPRPTNQ----RVNKHVNNDVNLRIQNLTILVRHIKTY 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2006390933 87 NHEILgQQINDFTLPDVNLIGEH----ADAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQEL 157
Cdd:cd22228 78 YQEVL-QQLIVMNLPNVLMIGKDplsgKSMEEIKKMLLLVLGCAVQCERKEEFIERIKQLDIETQAAIVSHIQEV 151
|
|
| HkD_Girdin |
cd22229 |
Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation ... |
16-157 |
2.37e-12 |
|
Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation enhancer (APE), or coiled-coil domain-containing protein 88A (CCDC88A), or G alpha-interacting vesicle-associated protein (GIV), or Girders of actin filament, or Hook-related protein 1 (HkRP1), is a bifunctional modulator of guanine nucleotide-binding proteins (G proteins). It acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein G(i) alpha subunits. It also acts as a guanine nucleotide dissociation inhibitor for guanine nucleotide-binding protein G(s) subunit alpha GNAS. In addition, Girdin plays an essential role in cell migration.
Pssm-ID: 411800 Cd Length: 156 Bit Score: 65.20 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 16 LLTWIQTFNVEAPCQTVE-----DLTSGVVMAQVLQKIDPAYFDEnwlnRIKTEVGDNWRLKVSNLKKILKGILDYNHEI 90
Cdd:cd22229 9 LVTWVKTFGPLATGNGTPldeyvALVDGVFLNEVMLQINPKSSNQ----RVNKKVNNDASLRIQNLSILVKQIKLYYQET 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2006390933 91 LgQQINDFTLPDVNLIG-----EHAdAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQEL 157
Cdd:cd22229 85 L-QQLIMMSLPNVLVLGrnplsEQG-TEEMKKLLLLLLGCAVQCERKEEFIERIQTLDFDTKAAVAAHIQEV 154
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
130-690 |
9.16e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.47 E-value: 9.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 130 EQKQEYIQTIMMMEESVQHVVMTAIQELMSKESPVSVGNDAYVDLDRQLKKTTEELNEALATKEEIAqrchELDMQVAAL 209
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIE----ELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 210 QEEKSSLLAENQILMERLNQSDS-IEDPNSPAGR---------RHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEI 279
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKeIEELEEKVKElkelkekaeEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 280 AELRQQTEELTTLAEEAQSLKDEIDVLRHSS---DKVAKLESQVESYKKKLEDL--GDLRRQVKLLEEKNTmymqntvSL 354
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEELEERHelyEEAKAKKEELERLKKRLTGLtpEKLEKELEELEKAKE-------EI 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 355 EEELRKANAARSQLETYKRQavelQNRLSEESKKADKLDYECKRL---KEKVDSLQKEKDRLRTERDSLKETIEELRCVQ 431
Cdd:PRK03918 404 EEEISKITARIGELKKEIKE----LKKAIEELKKAKGKCPVCGRElteEHRKELLEEYTAELKRIEKELKEIEEKERKLR 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 432 AQEGQLTTTgLMPLGRQEPSDSLAAEIItpEIKEKLIRLQHEnkmlKLNQEGSDNEKI--------ALLQSLLDDANlRK 503
Cdd:PRK03918 480 KELRELEKV-LKKESELIKLKELAEQLK--ELEEKLKKYNLE----ELEKKAEEYEKLkekliklkGEIKSLKKELE-KL 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 504 NELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDFLLLAAVLLYtnvisvSWHGLLLKAISVllKKKLEEHLEKLHE 583
Cdd:PRK03918 552 EELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELE------PFYNEYLELKDA--EKELEREEKELKK 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 584 ANNELQKKRAIIEDLEPRCNNSSLKIEELQealrkKEEEMKQMEERYKKYLEKAKSVirtldpkqnQGAAPEIQALKNQL 663
Cdd:PRK03918 624 LEEELDKAFEELAETEKRLEELRKELEELE-----KKYSEEEYEELREEYLELSREL---------AGLRAELEELEKRR 689
|
570 580
....*....|....*....|....*..
gi 2006390933 664 QERDRMFHSLEKEYEKTKSQREMEEKF 690
Cdd:PRK03918 690 EEIKKTLEKLKEELEEREKAKKELEKL 716
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
260-599 |
3.15e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 260 RLEAAKDDY---RIRCEELEKEIAELRQQTEelttLAEEAQSLKDEIDVLrhssdkvaKLESQVESYKKKLEDLGDLRRQ 336
Cdd:COG1196 180 KLEATEENLerlEDILGELERQLEPLERQAE----KAERYRELKEELKEL--------EAELLLLKLRELEAELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 337 VKLLEEKNTMYMQNTVSLEEELRKANAARSQLEtykRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTE 416
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELE---LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 417 RDSLKETIEELrcvQAQEGQLTTTglmpLGRQEPSDSLAAEIITpEIKEKLIRLQHENKMLKLNQEGSDNEKIALLQSLL 496
Cdd:COG1196 325 LAELEEELEEL---EEELEELEEE----LEEAEEELEEAEAELA-EAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 497 DDANLRKNELETENRLvNQRLLEVQSQVEELQKSLQDQGSKAEDfLLLAAVLLYTNVISVSWHGLLLKAISVLLKKKLEE 576
Cdd:COG1196 397 ELAAQLEELEEAEEAL-LERLERLEEELEELEEALAELEEEEEE-EEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
330 340
....*....|....*....|...
gi 2006390933 577 HLEKLHEANNELQKKRAIIEDLE 599
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLL 497
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
260-533 |
6.22e-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: 62.77 E-value: 6.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 260 RLEAAKDDYrircEELEKEIAELRQQTEELTTLAEEAQSlkdEIDVLRhssDKVAKLESQVESYKKKLEDLGdlrrqvkl 339
Cdd:TIGR02168 233 RLEELREEL----EELQEELKEAEEELEELTAELQELEE---KLEELR---LEVSELEEEIEELQKELYALA-------- 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 340 lEEKNTmymqntvsLEEELRKANAARSQLEtykRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERDS 419
Cdd:TIGR02168 295 -NEISR--------LEQQKQILRERLANLE---RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 420 LKETIEEL-RCVQAQEGQLTT--TGLMPLGRQEpsDSLAAEIItpEIKEKLIRLQHENKMLKLNQEGSDNE----KIALL 492
Cdd:TIGR02168 363 LEAELEELeSRLEELEEQLETlrSKVAQLELQI--ASLNNEIE--RLEARLERLEDRRERLQQEIEELLKKleeaELKEL 438
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2006390933 493 QSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQD 533
Cdd:TIGR02168 439 QAELEELEEELEELQEELERLEEALEELREELEEAEQALDA 479
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
173-532 |
9.19e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.39 E-value: 9.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 173 DLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLaENQILMERLnqsdsIEDPNSPAGRRHLQLQTQLE 252
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEK-----REYEGYELLKEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 253 QLQEETFRLEAAKDDYRIRCEELEKEIAELRQQTEELTT-----LAEEAQSLKDEIDVLrhsSDKVAKLESQVESYKKKL 327
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKkikdlGEEEQLRVKEKIGEL---EAEIASLERSIAEKEREL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 328 EDLGDLRRQVKLLEEKNTMYMQNtvsLEEELRKANAARSQLET--YKRQAV--ELQNRLSEESKKADKLDYECKRLKEKV 403
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEE---LEREIEEERKRRDKLTEeyAELKEEleDLRAELEEVDKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 404 DSLQKEKDRLRTERDSLKETIEELRCVQAQegqltttglmplgrqepsdsLAAEIitPEIKEKLIRLQHENKMLKLNQEg 483
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELAD--------------------LNAAI--AGIEAKINELEEEKEDKALEIK- 451
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2006390933 484 SDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQ 532
Cdd:TIGR02169 452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAR 500
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
260-532 |
1.00e-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: 62.38 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 260 RLEAAKDDYRIRCEELEKEIAELRQQTEELTTLAEEAQSLKDEIDVLRHSSDK-VAKLESQVESYKKKLEDL----GDLR 334
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdLARLEAEVEQLEERIAQLskelTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 335 RQVKLLEEKNTMYMQNTVSLEEEL----RKANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEK 410
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIeeleAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 411 DRLRTERDSLKETIEELRCVQAQEGQLTTTglmplgRQEPSDSLAAEIITPEIKEKLIRLQHENKMLKLNQEGSDN---- 486
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEE------LESELEALLNERASLEEALALLRSELEELSEELRELESKRselr 914
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2006390933 487 EKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQ 532
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALE 960
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
173-428 |
1.66e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.61 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 173 DLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSdsiEDPNSPAGRRHLQLQTQLE 252
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL---ERQLEELEAQLEELESKLD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 253 QLQEETFRLEAAKDDYRIRCEELEKEIAELRQQTEELTTLAEEAQ----SLKDEIDVLRHssdKVAKLESQVESYKKKLE 328
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEeqleTLRSKVAQLEL---QIASLNNEIERLEARLE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 329 DLGdlRRQVKLLEEkntmymQNTVSLEEELRKANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQK 408
Cdd:TIGR02168 411 RLE--DRRERLQQE------IEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
|
250 260
....*....|....*....|
gi 2006390933 409 EKDRLRTERDSLKETIEELR 428
Cdd:TIGR02168 483 ELAQLQARLDSLERLQENLE 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
174-428 |
2.04e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 174 LDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDPNSpagRRHLQLQTQLEQ 253
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE---ERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 254 LQEETFRLEAAKDDYRIRCEELEKEIAELRQQTEELttLAEEAQSLKDEIDVLRHSSDKVAKLESQVESYKKKLEDLGDL 333
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEA--EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 334 RRQVKLLEEKNTMYMQNTVSLEEELRKANAARSQLEtykRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRL 413
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELE---EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
250
....*....|....*
gi 2006390933 414 RTERDSLKETIEELR 428
Cdd:COG1196 476 EAALAELLEELAEAA 490
|
|
| HkD_Gipie |
cd22230 |
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar ... |
12-157 |
6.81e-09 |
|
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: 55.61 E-value: 6.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 12 LGESLLTWIQTF-------------NVEAPCQTVED-------LTSGVVMAQVLQKIDPAYFDENWLNRikteVGDNWRL 71
Cdd:cd22230 4 MSGALVTWALGFeglvgeeedslgfPEEEEEEGTLDaekrflrLSNGDLLNRVMGIIDPSPRGGPRMRG----DDGPAAH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 72 KVSNLKKILKGILDYNHEILgQQINDFTLPDVNLIGEH----ADAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQ 147
Cdd:cd22230 80 RVQNLHILWGRLRDFYQEEL-QQLILSPPPDLQVMGRDpfteEAVQELEKLLRLLLGAAVQCERRELFIRHIQGLDLDVQ 158
|
170
....*....|
gi 2006390933 148 HVVMTAIQEL 157
Cdd:cd22230 159 AELAEAIQEV 168
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
173-689 |
8.22e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 8.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 173 DLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLA-----ENQILMERLNQSDSIEDpnspAGRRHLQL 247
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAelarlEQDIARLEERRRELEER----LEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 248 QTQLEQLQEETFRLEAAKDDYRIRCEELEKEIAELRQQTEELTTLAEEAQSLKDEIDVLRhsSDKVAKLESQVESYKKKL 327
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA--EELLEALRAAAELAAQLE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 328 EDLGDLRRQVKLLEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQ 407
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 408 KEKDRLRTERDSLKETIEElrcvQAQEGQLTTTGLMPLGRQEPSDSLAAEIITPEIKEKLIRLQHENKMLKLNQEGSDNE 487
Cdd:COG1196 484 EELAEAAARLLLLLEAEAD----YEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVA 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 488 KIALlqSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDFLLLAAVLLYTNVISVSWHGLLLKAIS 567
Cdd:COG1196 560 AAAI--EYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALR 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 568 VLLKKKLEEHLEKLH---------EANNELQKKRAIIEDLEPRCNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAK 638
Cdd:COG1196 638 RAVTLAGRLREVTLEgeggsaggsLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERL 717
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2006390933 639 SVIRTLDPKQNQGAAPEIQALKNQLQERDRMFHSLEKEYEKTKSQREMEEK 689
Cdd:COG1196 718 EEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERE 768
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
169-689 |
1.33e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 169 DAYVDLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQ--------SDSIEDPNSPA 240
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPElreeleklEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 241 GRRHLQLQTQLEQLQEETfRLEAAKDDYRIRCEELEKEIAELRQQTEELTTLAEEAQS-------LKDEIDVLRHSSDKV 313
Cdd:PRK03918 238 EEIEELEKELESLEGSKR-KLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiklsefYEEYLDELREIEKRL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 314 AKLESQVESYKKKLEDLGDLRRQVKLLEEKntmymqntvsLEEELRKANAARSQLETYKRqAVELQNRLseESKKADKLD 393
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEKEERLEELKKK----------LKELEKRLEELEERHELYEE-AKAKKEEL--ERLKKRLTG 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 394 YECKRLKEKVDSLQKEKDRLRTERDSLKETIEELRcvqaQEGQLTTTGLMPLGRQEPSDSLAAEIITPEIKEKLIRLQHe 473
Cdd:PRK03918 384 LTPEKLEKELEELEKAKEEIEEEISKITARIGELK----KEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYT- 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 474 nkmLKLNQEGSDNEKIALLQSllddaNLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDFLLLAAVLLYTNV 553
Cdd:PRK03918 459 ---AELKRIEKELKEIEEKER-----KLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKL 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 554 ISVSwhGLLLKAISVLLK--KKLEEHLEKLHEANNELQKKRAIIEDLEPRCNNSSLK-IEELQEALRKKEEEmkqmeerY 630
Cdd:PRK03918 531 KEKL--IKLKGEIKSLKKelEKLEELKKKLAELEKKLDELEEELAELLKELEELGFEsVEELEERLKELEPF-------Y 601
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2006390933 631 KKYLEkAKSVIRTLDPKQNqgaapEIQALKNQLQERDRMFHSLEKEYEKTKSQREMEEK 689
Cdd:PRK03918 602 NEYLE-LKDAEKELEREEK-----ELKKLEEELDKAFEELAETEKRLEELRKELEELEK 654
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
260-540 |
3.61e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.97 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 260 RLEAAKDDYRIRCEELEKEIAEL----RQQTEELTTLAEEAQSLKDEIDVLRHSSDKVAKLESQVESYKKKLED-LGDLR 334
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREELaeevRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDrLEECR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 335 RQVKLLEEKNTMYMQNTVSLEE---ELR--------KANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKV 403
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDLEEraeELReeaaelesELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 404 DSLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTTGLMPLGRQEPSDSLAAEIITpEIKEKLIRLQHENKMLKLNQEG 483
Cdd:PRK02224 415 EELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIE-EDRERVEELEAELEDLEEEVEE 493
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2006390933 484 SDN--EKIALLQSLLDDANLRKNELETENRLVNQR---LLEVQSQVEELQKSLQDQGSKAED 540
Cdd:PRK02224 494 VEErlERAEDLVEAEDRIERLEERREDLEELIAERretIEEKRERAEELRERAAELEAEAEE 555
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
174-471 |
4.22e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 4.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 174 LDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDsiedpnspagRRHLQLQTQLEQ 253
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK----------ERLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 254 LQEETFRLEAAKDDYRIRCEELEKEIAELRQQTEELTtlAEEAQSLKDEI-DVLRHSSDKVAKLESQVESYKKKLEDlgd 332
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE--ARLSHSRIPEIqAELSKLEEEVSRIEARLREIEQKLNR--- 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 333 lRRQVKLLEEKNTMYMQNTVSLEEELRKANAAR-----SQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQ 407
Cdd:TIGR02169 824 -LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEienlnGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2006390933 408 KEKDRLRTERDSLKETIEELRC-VQAQEGQLTTTG-LMPLGRQEPSDSLAAEIITPEIKEKLIRLQ 471
Cdd:TIGR02169 903 RKIEELEAQIEKKRKRLSELKAkLEALEEELSEIEdPKGEDEEIPEEELSLEDVQAELQRVEEEIR 968
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
365-685 |
7.87e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 7.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 365 RSQLETYKRQAV------ELQNRLSEESKKADKLDYEckRLKEKVDSLQKEKDRLRTERDSLKETIEELrcvqaqEGQLT 438
Cdd:TIGR02168 199 ERQLKSLERQAEkaerykELKAELRELELALLVLRLE--ELREELEELQEELKEAEEELEELTAELQEL------EEKLE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 439 TtglmplgrqepsdslaaeiitpeikeklIRLQHenkmlklnqeGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLL 518
Cdd:TIGR02168 271 E----------------------------LRLEV----------SELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 519 EVQSQVEELQKSLQDQGSKAEDflllaavllytnvisvswhgllLKAISVLLKKKLEEHLEKLHEANNELQKKRAIIEDL 598
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDE----------------------LAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 599 EPRCNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQLQERDRMFHSLEKEYE 678
Cdd:TIGR02168 371 ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELE 450
|
....*..
gi 2006390933 679 KTKSQRE 685
Cdd:TIGR02168 451 ELQEELE 457
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
176-689 |
1.99e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 176 RQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQ 255
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 256 EETFRLEAAKDDYRIRCEELEKEIAELRQQTEELTTLAEEAQS-------LKDEIDVLRHSSDKVAKLESQVESYKKKLE 328
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiklsefYEEYLDELREIEKRLSRLEEEINGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 329 DLGDLRRQVKLLEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQAVELQNRLSEE-SKKADKLDYECKRLKEKVDSLQ 407
Cdd:PRK03918 332 ELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKlEKELEELEKAKEEIEEEISKIT 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 408 KEKDRLRTERDSLKETIEELRcvqaqegqlTTTGLMPLGRQEPSDSLAAEIIT------PEIKEKLIRLQHENKML---- 477
Cdd:PRK03918 412 ARIGELKKEIKELKKAIEELK---------KAKGKCPVCGRELTEEHRKELLEeytaelKRIEKELKEIEEKERKLrkel 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 478 -KLNQEGSDNEKIALLQSLLDDANLRKNELE-----------TENRLVNQRLLEVQSQVEELQKSLqdqgSKAEDfllla 545
Cdd:PRK03918 483 rELEKVLKKESELIKLKELAEQLKELEEKLKkynleelekkaEEYEKLKEKLIKLKGEIKSLKKEL----EKLEE----- 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 546 avllytnvisvswhgllLKAISVLLKKKLEEHLEKLHEANNELQKK--------RAIIEDLEP------RCNNSSLKIEE 611
Cdd:PRK03918 554 -----------------LKKKLAELEKKLDELEEELAELLKELEELgfesveelEERLKELEPfyneylELKDAEKELER 616
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2006390933 612 LQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQLQERDRMFHSLEKEYEKTKSQREMEEK 689
Cdd:PRK03918 617 EEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKK 694
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
173-427 |
2.75e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 173 DLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAE-------------NQILMERLNQSDSIEDPNSP 239
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlshsripeiqaelSKLEEEVSRIEARLREIEQK 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 240 AGRRHLQLQTQLEQLQEETFRLEAAKDdyriRCEELEKEIAELRQQTEELTTLAEEAQ-SLKDEIDVLRHSSDKVAKLES 318
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQRIDLKE----QIKSIEKEIENLNGKKEELEEELEELEaALRDLESRLGDLKKERDELEA 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 319 QVESYKKKLEDLG----DLRRQVKLLEEKNTMYMQNTVSLEEELRK---ANAARSQLETYKRQAVELQNRLSEESKKADK 391
Cdd:TIGR02169 897 QLRELERKIEELEaqieKKRKRLSELKAKLEALEEELSEIEDPKGEdeeIPEEELSLEDVQAELQRVEEEIRALEPVNML 976
|
250 260 270
....*....|....*....|....*....|....*.
gi 2006390933 392 LDYECKRLKEKVDSLQKEKDRLRTERDSLKETIEEL 427
Cdd:TIGR02169 977 AIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
260-428 |
4.37e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 260 RLEAAKDDYRIRCEELEKEIAELRQQTEELTTLAE-------------EAQSLKDEIDVLRHSSDKVAKLESQVESYKKK 326
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeidvasaerEIAELEAELERLDASSDDLAALEEQLEELEAE 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 327 LEDL----GDLRRQVKLLEEKNTmymqntvSLEEELRKANAARSQLETYKRQAV--ELQNRLSEESKKAdkldyeckRLK 400
Cdd:COG4913 701 LEELeeelDELKGEIGRLEKELE-------QAEEELDELQDRLEAAEDLARLELraLLEERFAAALGDA--------VER 765
|
170 180
....*....|....*....|....*...
gi 2006390933 401 EKVDSLQKEKDRLRTERDSLKETIEELR 428
Cdd:COG4913 766 ELRENLEERIDALRARLNRAEEELERAM 793
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
273-426 |
4.80e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 4.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 273 EELEKEIAELRqqtEELTTLAEEAQSLKDEIDVLRHSSDKVAKLESQVESykkkLEDLGDLRRQVklleekntmymqntV 352
Cdd:COG4913 613 AALEAELAELE---EELAEAEERLEALEAELDALQERREALQRLAEYSWD----EIDVASAEREI--------------A 671
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2006390933 353 SLEEELRKANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERDSLKETIEE 426
Cdd:COG4913 672 ELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
213-689 |
6.24e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 6.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 213 KSSLLA-ENQILMERLNQSdsIEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEIAELRQQTEELTT 291
Cdd:COG4717 36 KSTLLAfIRAMLLERLEKE--ADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 292 LAEEAQSLKDEIDVLRHSSD------KVAKLESQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEELRkaNAAR 365
Cdd:COG4717 114 LREELEKLEKLLQLLPLYQElealeaELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLS--LATE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 366 SQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKdrlrtERDSLKETIEELRCVQAQEGQ---LTTTGL 442
Cdd:COG4717 192 EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL-----EAAALEERLKEARLLLLIAAAllaLLGLGG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 443 MPLGRQEPSDSLAAEIITPEIKEKLIRLQHENKMLKLNQEGSDNEKIALLQSLLDDANLRKNELETEnrLVNQRLLEVQS 522
Cdd:COG4717 267 SLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPD--LSPEELLELLD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 523 QVEELQKSLQDQGSKAEDFLLLAavllytnvisvswhglLLKAISVLLKK---KLEEHLEKLHEANNELQKKRAIIEDLE 599
Cdd:COG4717 345 RIEELQELLREAEELEEELQLEE----------------LEQEIAALLAEagvEDEEELRAALEQAEEYQELKEELEELE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 600 PRCNNSSLKIEELQEALrkkeeemkqMEERYKKYLEKAKSVIRTLDPKQNQgAAPEIQALKNQLQ--ERDRMFHSLEKEY 677
Cdd:COG4717 409 EQLEELLGELEELLEAL---------DEEELEEELEELEEELEELEEELEE-LREELAELEAELEqlEEDGELAELLQEL 478
|
490
....*....|..
gi 2006390933 678 EKTKSQREMEEK 689
Cdd:COG4717 479 EELKAELRELAE 490
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
179-466 |
7.52e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 7.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 179 KKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDsiEDPNSPAGRRHLQLQTQLEQLQEET 258
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE--EKKKAEEAKKAEEDKNMALRKAEEA 1586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 259 FRLEAAKDDYRIRCEELEKEI-AELRQQTEELTTLAEEAQSLKDEIDVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQV 337
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEEKKMkAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 338 KLLEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKdrlrtER 417
Cdd:PTZ00121 1667 AKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEA-----EE 1741
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2006390933 418 DslKETIEELRCVQAQEGQLTTTGLMPLGRQEPSDSLAAEIITPEIKEK 466
Cdd:PTZ00121 1742 D--KKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEE 1788
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
260-426 |
1.20e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.31 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 260 RLEAAKDDYRIRCEELEKEIAELRQQTEELTTLAEEAQSLKDEIDV-LRHSSDKVAKLESQVESYKKKLEDLGDLRRQVK 338
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKeIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 339 LLEEKNTMYMQNTVsLEEELRKANAarsQLETYKRQAVELQNRLSEeskKADKLDYECKRLKEKVDSLQKEKDRLRTERD 418
Cdd:COG1579 94 LQKEIESLKRRISD-LEDEILELME---RIEELEEELAELEAELAE---LEAELEEKKAELDEELAELEAELEELEAERE 166
|
....*...
gi 2006390933 419 SLKETIEE 426
Cdd:COG1579 167 ELAAKIPP 174
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
191-440 |
1.34e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.96 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 191 TKEEIAQRCHELDMQVAALQEEKSSL---LAENQILMERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDD 267
Cdd:PRK02224 469 TIEEDRERVEELEAELEDLEEEVEEVeerLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAE 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 268 YRIRCEELEKEIAELRQQTEE----LTTLAEEAQSLKDEIDVL---RHSSDKVAKLESQVESYKKKLEDLGDLRRQVK-L 339
Cdd:PRK02224 549 LEAEAEEKREAAAEAEEEAEEareeVAELNSKLAELKERIESLeriRTLLAAIADAEDEIERLREKREALAELNDERReR 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 340 LEEKNTMYMQNTVSLEEE-LRKANAARSQLETYKRQAVElqnRLSEESKKADKLDYECKRLKEKVDSLqkekDRLRTERD 418
Cdd:PRK02224 629 LAEKRERKRELEAEFDEArIEEAREDKERAEEYLEQVEE---KLDELREERDDLQAEIGAVENELEEL----EELRERRE 701
|
250 260
....*....|....*....|..
gi 2006390933 419 SLKETIEELRCVQAQEGQLTTT 440
Cdd:PRK02224 702 ALENRVEALEALYDEAEELESM 723
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
173-470 |
2.39e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 173 DLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAE----NQILMERLNQSDSIEDPNSPAGRRHLQLQ 248
Cdd:TIGR02168 723 ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERleeaEEELAEAEAEIEELEAQIEQLKEELKALR 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 249 TQLEQLQEETFRLEAAKDDYRIRCEELEKEIAELRQqteELTTLAEEAQSLKDEIDVLRHSsdkVAKLESQVESYKKKLE 328
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAATER---RLEDLEEQIEELSEDIESLAAE---IEELEELIEELESELE 876
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 329 DLGDLRRqvklleekntmymqntvSLEEELRKANAARSQLETykrqavelqnRLSEESKKADKLDYECKRLKEKVDSLQK 408
Cdd:TIGR02168 877 ALLNERA-----------------SLEEALALLRSELEELSE----------ELRELESKRSELRRELEELREKLAQLEL 929
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2006390933 409 EKDRLRTERDSLKETIEElrcvqaqEGQLTTTGLMPLGRQEPSDSLAAEIITPEIKEKLIRL 470
Cdd:TIGR02168 930 RLEGLEVRIDNLQERLSE-------EYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
336-548 |
2.93e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 336 QVKLLEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRT 415
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 416 ERDSLKETIEELRCVQAQEGQLTTTGLMpLGRQEPSDSLAA----EIITPEIKEKLIRLQHENKMLKLNQEGSDNEKiAL 491
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALL-LSPEDFLDAVRRlqylKYLAPARREQAEELRADLAELAALRAELEAER-AE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2006390933 492 LQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDFLLLAAVL 548
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
304-617 |
3.62e-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: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 304 DVLRHSSDKVAKLESQVESYKkkleDLGDLRRQVK--LLEEKNTM--------YMQNTVSLEEELRKANAARSQLEtykr 373
Cdd:COG4913 184 RRLGIGSEKALRLLHKTQSFK----PIGDLDDFVReyMLEEPDTFeaadalveHFDDLERAHEALEDAREQIELLE---- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 374 QAVELQNRLSEESKKADKLDYECKRLK-----EKVDSLQKEKDRLRTERDSLKETIEELrcvQAQEGQLtttglmplgrq 448
Cdd:COG4913 256 PIRELAERYAAARERLAELEYLRAALRlwfaqRRLELLEAELEELRAELARLEAELERL---EARLDAL----------- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 449 epsdslaaeiitpeiKEKLIRLQHEnkmlklnQEGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQ 528
Cdd:COG4913 322 ---------------REELDELEAQ-------IRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASA 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 529 KSLQDQGSKAEDFLLLaavllytnvisvswhgllLKAISVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRCNNSSLK 608
Cdd:COG4913 380 EEFAALRAEAAALLEA------------------LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPAR 441
|
....*....
gi 2006390933 609 IEELQEALR 617
Cdd:COG4913 442 LLALRDALA 450
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
263-428 |
3.71e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.40 E-value: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 263 AAKDDYRIRCEELEKEIAELRQQTEELTT-LAEEAQSLKDEIDVLRHSSDKVAKLESQVESYKK--KLEDLGDL----RR 335
Cdd:PHA02562 213 ENIARKQNKYDELVEEAKTIKAEIEELTDeLLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKviKMYEKGGVcptcTQ 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 336 QVKLLEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRT 415
Cdd:PHA02562 293 QISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQA 372
|
170
....*....|...
gi 2006390933 416 ERDSLKETIEELR 428
Cdd:PHA02562 373 EFVDNAEELAKLQ 385
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
260-683 |
3.91e-06 |
|
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: 50.61 E-value: 3.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 260 RLEAAKDDYRIRCEELEKEIAELRQQTE-ELTTLAEEAQSLKDEIDVLrhSSDKVAKLESQVESYKKKLEDLGDLRRQVK 338
Cdd:pfam12128 280 ERQETSAELNQLLRTLDDQWKEKRDELNgELSAADAAVAKDRSELEAL--EDQHGAFLDADIETAAADQEQLPSWQSELE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 339 LLEEKNTMYMQNTVSLEEELRKANAARSQleTYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDS-----LQKEKDRL 413
Cdd:pfam12128 358 NLEERLKALTGKHQDVTAKYNRRRSKIKE--QNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESelreqLEAGKLEF 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 414 RTERDSLKETIEELRCVQAQEgqltttglmplgrqepsdslaaeIITPEIKEKLIRLQHENKMLKLNQEGSdNEKIALLQ 493
Cdd:pfam12128 436 NEEEYRLKSRLGELKLRLNQA-----------------------TATPELLLQLENFDERIERAREEQEAA-NAEVERLQ 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 494 SLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDFL--------------LLAAVLLYTNVISVSWH 559
Cdd:pfam12128 492 SELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLrkeapdweqsigkvISPELLHRTDLDPEVWD 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 560 G------------LLLKAISVLLKKKLEEHLE-KLHEANNELQKKRAIIEDLEPRCNNSSLKIEELQEALRKKEEEMKQM 626
Cdd:pfam12128 572 GsvggelnlygvkLDLKRIDVPEWAASEEELReRLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNA 651
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2006390933 627 EERykkyLEKAKSVIRTLDPKQNQGAAPEIQALKNQLQERDRMFHSLEKEYEKTKSQ 683
Cdd:pfam12128 652 RLD----LRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEE 704
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
260-540 |
9.48e-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: 49.30 E-value: 9.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 260 RLEAAKDDY---RIRCEELEKEIAELRQQTEELTTLAEEA------QSLKDEIDVLRHSSDK-------------VAKLE 317
Cdd:TIGR02169 171 KKEKALEELeevEENIERLDLIIDEKRQQLERLRREREKAeryqalLKEKREYEGYELLKEKealerqkeaierqLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 318 SQVESYKKKLEDLGD-LRRQVKLLEEKNTMYMQNT----VSLEEELRKANA----ARSQLETYKRQAVELQNRLSEESKK 388
Cdd:TIGR02169 251 EELEKLTEEISELEKrLEEIEQLLEELNKKIKDLGeeeqLRVKEKIGELEAeiasLERSIAEKERELEDAEERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 389 ADKLDYECKRLKEKVDSLQKEKDRLRTERDSLKETIEELRC-VQAQEGQLTTTGLMPLGRQEPSDSLAAEIitPEIKEKL 467
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAeLEEVDKEFAETRDELKDYREKLEKLKREI--NELKREL 408
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2006390933 468 IRLQHENKmlKLNQEGSD-NEKIALLQSllddanlRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAED 540
Cdd:TIGR02169 409 DRLQEELQ--RLSEELADlNAAIAGIEA-------KINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD 473
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
264-427 |
1.13e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 48.70 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 264 AKDDYRIRCEELEKEIAElRQQTEEL-------TTLAEEAQSLKDEIDVLRHSSDKVAKLESQVESYKKKlEDLGDLRRQ 336
Cdd:COG2433 344 AYDAYKNKFERVEKKVPP-DVDRDEVkarvirgLSIEEALEELIEKELPEEEPEAEREKEHEERELTEEE-EEIRRLEEQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 337 VKLLEEKNtmymqntVSLEEELRKANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTE 416
Cdd:COG2433 422 VERLEAEV-------EELEAELEEKDERIERLERELSEARSEERREIRKDREISRLDREIERLERELEEERERIEELKRK 494
|
170
....*....|.
gi 2006390933 417 RDSLKETIEEL 427
Cdd:COG2433 495 LERLKELWKLE 505
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
173-665 |
1.35e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 173 DLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDpnsPAGRRHLQLQTQLE 252
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA---EAEEELEELAEELL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 253 QLQEETFRLEAAKDDYRIRCEELEKEIAELRQQTEEL-TTLAEEAQSLKDEIDVLRHSSDKVAKLESQVESYKKKLEDLG 331
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELeEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 332 DLRRQVKLLEEKNTMYMQNTVSLEEELRKANAARSQ-LETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEK 410
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGfLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 411 DRLRTERDSLKETIEELRcvQAQEGQLTttgLMPLGRQEPSDSLAAEIITPEIKEKLIRLQHENKmlklnqegSDNEKIA 490
Cdd:COG1196 550 NIVVEDDEVAAAAIEYLK--AAKAGRAT---FLPLDKIRARAALAAALARGAIGAAVDLVASDLR--------EADARYY 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 491 LLQSLLDDANLRKNELETENRLVnQRLLEVQSQVEELQKSLQDQGSKAEDFLLLAAVLLytnvisvswhgLLLKAISVLL 570
Cdd:COG1196 617 VLGDTLLGRTLVAARLEAALRRA-VTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL-----------LEAEAELEEL 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 571 KKKLEEHLEKLHEANNELQKKRAIIEDLEPRCNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQ 650
Cdd:COG1196 685 AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEE 764
|
490
....*....|....*
gi 2006390933 651 gAAPEIQALKNQLQE 665
Cdd:COG1196 765 -LERELERLEREIEA 778
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
271-691 |
1.57e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 271 RCEELEKEIAELRQQTEELTTLAEE---AQSLKDEIDVLRHSSD--KVAKLESQVESYKKKLEDLGDLRRQVKLLEEKNT 345
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKAAAAkkkADEAKKKAEEKKKADEakKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 346 MymQNTVSLEEELRKANAARSQLETYKRQAVELQNRlSEESKKADKLDY--------ECKRLKEKVDSLQKEKDRLRTER 417
Cdd:PTZ00121 1472 A--DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA-AEAKKKADEAKKaeeakkadEAKKAEEAKKADEAKKAEEKKKA 1548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 418 DSLKETiEELRcvQAQEGQLTTTGLMPLGRQEPSDSLAAEIITPEIK--EKLIRLQHENKMLKLNQEGSDNEkiallqsl 495
Cdd:PTZ00121 1549 DELKKA-EELK--KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAriEEVMKLYEEEKKMKAEEAKKAEE-------- 1617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 496 lddANLRKNELETENrlvnqrllEVQSQVEELQKSLQDQGSKAEDflllaavllytnvisVSWHGLLLKAISVLLKKKLE 575
Cdd:PTZ00121 1618 ---AKIKAEELKKAE--------EEKKKVEQLKKKEAEEKKKAEE---------------LKKAEEENKIKAAEEAKKAE 1671
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 576 EHLEKLHEANNELQKKRAIIEDLEpRCNNSSLKIEElqeaLRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAApE 655
Cdd:PTZ00121 1672 EDKKKAEEAKKAEEDEKKAAEALK-KEAEEAKKAEE----LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK-K 1745
|
410 420 430
....*....|....*....|....*....|....*.
gi 2006390933 656 IQALKNQLQERDRMFHSLEKEYEKTKSQREMEEKFI 691
Cdd:PTZ00121 1746 AEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
283-640 |
2.59e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.76 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 283 RQQTEELTTLAEEAQSLKDEIDVLRhssDKVAKLESQVESYKKKLED----LGDLRRQVKLLEEKNTMYMQNTVSLEEEL 358
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQ---SELRRIENRLDELSQELSDasrkIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 359 ----RKANAARSQLETYKRQAVELQNRLSEESKKADKLdyECKRLKEKVDSLQKEKDRLRTERDSLKETIEELRcvqaqe 434
Cdd:TIGR02169 747 ssleQEIENVKSELKELEARIEELEEDLHKLEEALNDL--EARLSHSRIPEIQAELSKLEEEVSRIEARLREIE------ 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 435 gqltttglMPLGRQEPSDSLAAEIITpEIKEKLIRLQHENKMLKLNQEgSDNEKIALLQSLLDDANLRKNELETENRLVN 514
Cdd:TIGR02169 819 --------QKLNRLTLEKEYLEKEIQ-ELQEQRIDLKEQIKSIEKEIE-NLNGKKEELEEELEELEAALRDLESRLGDLK 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 515 QRLLEVQSQVEELQKSLQDQGSKAEDFLLLAAVLLYTNVISVSWHGLLLKAISVLLKKKLEE-HLEKLHEannELQKKRA 593
Cdd:TIGR02169 889 KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEElSLEDVQA---ELQRVEE 965
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2006390933 594 IIEDLEPRCN-------NSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSV 640
Cdd:TIGR02169 966 EIRALEPVNMlaiqeyeEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
273-528 |
2.88e-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: 47.81 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 273 EELEKEIAELRQQTEELTTLAEEAQSLKDE-------IDVLRHSSD----KVAKLESQVESYKKKLEdlGDLRRQVKLLE 341
Cdd:pfam15921 377 DQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDdrnmEVQRLEALLKAMKSECQ--GQMERQMAAIQ 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 342 EKN------TMYMQNTVSLEEELRKA----NAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKD 411
Cdd:pfam15921 455 GKNeslekvSSLTAQLESTKEMLRKVveelTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQ 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 412 RLRTERDSLKETieelrcvqaqegqltttglmplgrQEPSDSLAAEIITPEIKEKLIRLQHENKMLKLNQEGSDNEKI-- 489
Cdd:pfam15921 535 HLKNEGDHLRNV------------------------QTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMqv 590
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2006390933 490 --ALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQ 528
Cdd:pfam15921 591 ekAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLE 631
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
273-605 |
2.92e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.66 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 273 EELEKEIAELRQQTEELTTLAEEAQSLKDEIDVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTV 352
Cdd:pfam02463 206 AKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 353 SLEEEL-RKANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERDSLKETIEELRCVQ 431
Cdd:pfam02463 286 EELKLLaKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQ 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 432 AQEgqltttglmplgRQEPSDSLAAEIITPEIKEKLIRLQHENKMLKLNQEGSDNEKIALLQSLLDDANLRKNELETEnR 511
Cdd:pfam02463 366 EKL------------EQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEI-L 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 512 LVNQRLLEVQSQVEELQKSLQDQGSKAEDFLLLAAVLLYTNVISVSWHGLLLKAISVLLKKKLEEHLEKLHEANNELQKK 591
Cdd:pfam02463 433 EEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVL 512
|
330
....*....|....
gi 2006390933 592 RAIIEDLEPRCNNS 605
Cdd:pfam02463 513 LALIKDGVGGRIIS 526
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
260-428 |
3.40e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 260 RLEAAKDDYRIRCEELEKEIAELRQQTEELTTLAEeaqslkdEIDVLRhssDKVAKLESQVESYKkklEDLGDLRRQVKL 339
Cdd:PRK02224 224 RYEEQREQARETRDEADEVLEEHEERREELETLEA-------EIEDLR---ETIAETEREREELA---EEVRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 340 LEEKNTmYMQNTVSLEEELRKANAARsqLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERDS 419
Cdd:PRK02224 291 LEEERD-DLLAEAGLDDADAEAVEAR--REELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAE 367
|
....*....
gi 2006390933 420 LKETIEELR 428
Cdd:PRK02224 368 LESELEEAR 376
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
260-410 |
4.55e-05 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 46.16 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 260 RLEAAKDDYRIRC-------EELEKEIAELRQQ----TEELTTLAEEAQSLKDEIDVLRHSSDKVAKLESQVESYKKklE 328
Cdd:smart00787 127 RLEAKKMWYEWRMklleglkEGLDENLEGLKEDykllMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDP--T 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 329 DLGDLRRQVKLLEEKNTMYMQNTVSLEEELRKANAArsqLETYKRQAVELQNRLSEESKKADKLD----YECKRLKEKVD 404
Cdd:smart00787 205 ELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESK---IEDLTNKKSELNTEIAEAEKKLEQCRgftfKEIEKLKEQLK 281
|
....*.
gi 2006390933 405 SLQKEK 410
Cdd:smart00787 282 LLQSLT 287
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
144-709 |
7.70e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 7.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 144 ESVQHVVMTAIQELMSKESPVSVGNDAYVDLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAE---- 219
Cdd:TIGR02168 284 EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEleel 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 220 NQILMERLNQSDSIEDP---------------NSPAGRR-----------HLQLQTQLEQLQEETFRLEAAKDDYRIRCE 273
Cdd:TIGR02168 364 EAELEELESRLEELEEQletlrskvaqlelqiASLNNEIerlearlerleDRRERLQQEIEELLKKLEEAELKELQAELE 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 274 ELEKEIAELRQQTEELTTLAEEAQSLKDEI-DVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQVK-LLEEKNTMY---- 347
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAeQALDAAERELAQLQARLDSLERLQENLEGFSEGVKaLLKNQSGLSgilg 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 348 -MQNTVSLEEELRKA-----------------NAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKE 409
Cdd:TIGR02168 524 vLSELISVDEGYEAAieaalggrlqavvvenlNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGV 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 410 KDRLRTERDSLKETIEEL--RCVQAQEGQLTTTGLMPLGRQEPSDSLAAEIITP-------EIKEKLIRLQHENKMLKLN 480
Cdd:TIGR02168 604 AKDLVKFDPKLRKALSYLlgGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPggvitggSAKTNSSILERRREIEELE 683
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 481 QEGSDNE-KIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDFLLLAAVLLYTNvisvswh 559
Cdd:TIGR02168 684 EKIEELEeKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL------- 756
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 560 gLLLKAISVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRCNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKS 639
Cdd:TIGR02168 757 -TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2006390933 640 VIRTLDPKQNQgaapeiqaLKNQLQERDRMFHSLEK-EYEKTKSQREMEEKFIVSAWYNMGMTLHKKAAED 709
Cdd:TIGR02168 836 TERRLEDLEEQ--------IEELSEDIESLAAEIEElEELIEELESELEALLNERASLEEALALLRSELEE 898
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
182-441 |
7.84e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 7.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 182 TEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQsdsiedpnspagrrhlqlqtqleqlqeetfrL 261
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA-------------------------------L 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 262 EAAKDDYRIRCEELEKEIAELRQQTEELTT-LAEEAQSLKDEIDVL-RHSSDKVAKLESQVESYKKKLEDLGDLRRQVKL 339
Cdd:COG4942 68 ARRIRALEQELAALEAELAELEKEIAELRAeLEAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 340 LEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQAVELQNRLSEESKKADKLDyecKRLKEKVDSLQKEKDRLRTERDS 419
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLL---ARLEKELAELAAELAELQQEAEE 224
|
250 260
....*....|....*....|..
gi 2006390933 420 LKETIEELRCVQAQEGQLTTTG 441
Cdd:COG4942 225 LEALIARLEAEAAAAAERTPAA 246
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
154-425 |
8.04e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.89 E-value: 8.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 154 IQELMSKESPVSVGNDAYVDLDRQLKKTTEELNEALATKE-----------EIAQRCHELDMQVAALQEEKSSLLAENQI 222
Cdd:pfam05557 57 IRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKEsqladarevisCLKNELSELRRQIQRAELELQSTNSELEE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 223 LMERLNQSDS----IEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRI---------RCEELEKEIAELRQQTEEL 289
Cdd:pfam05557 137 LQERLDLLKAkaseAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIvknskselaRIPELEKELERLREHNKHL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 290 TT-------LAEEAQSLKDEIDVLRHSSDKVA-------KLESQVESYKKKLEDLG-------DLRRQVKLLEEKNTMYM 348
Cdd:pfam05557 217 NEnienkllLKEEVEDLKRKLEREEKYREEAAtlelekeKLEQELQSWVKLAQDTGlnlrspeDLSRRIEQLQQREIVLK 296
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2006390933 349 QNTVSLEEELRKANAARSQLETYKRQAVelqnrlseesKKADKLDYECKRLKEKVDSLQKEKDRLRTERDSLKETIE 425
Cdd:pfam05557 297 EENSSLTSSARQLEKARRELEQELAQYL----------KKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILE 363
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
130-678 |
1.15e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.88 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 130 EQKQEYI-QTIMMMEESVQHVVMT--AIQELMSKEspvsvgNDAYVDLDRQLKKTTEELNEALATKEEIaqrcheLDMQV 206
Cdd:pfam15921 102 EKQKFYLrQSVIDLQTKLQEMQMErdAMADIRRRE------SQSQEDLRNQLQNTVHELEAAKCLKEDM------LEDSN 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 207 AALQEEKSSLLAENQILMERLNQSDSIEDPNSPAGRRHlqlqtqlEQLQEETFRLEAAKDDYRIRceELEKEIAELRQQT 286
Cdd:pfam15921 170 TQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEH-------DSMSTMHFRSLGSAISKILR--ELDTEISYLKGRI 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 287 ----EELTTLAEEAQSlKDEIdVLRHSSDKVAKLESQVEsykkkLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEelrkan 362
Cdd:pfam15921 241 fpveDQLEALKSESQN-KIEL-LLQQHQDRIEQLISEHE-----VEITGLTEKASSARSQANSIQSQLEIIQEQ------ 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 363 aARSQLETYKRQAVELQNRLSEESKKADkldyECKRLKE-KVDSLQK-------EKDRLRTERDSLKEtieelrcvqaQE 434
Cdd:pfam15921 308 -ARNQNSMYMRQLSDLESTVSQLRSELR----EAKRMYEdKIEELEKqlvlansELTEARTERDQFSQ----------ES 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 435 GQLtttglmplgrqepSDSLAAEIITPEIKEKLIRLQHENKMLKLNQEGSDNEKIALLQSLLDDANLRKNELETenrLVN 514
Cdd:pfam15921 373 GNL-------------DDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEA---LLK 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 515 QRLLEVQSQVEELQKSLQDQGSKAEDFLLLAAvllytnvisvswhglllkaisvllkkKLEEHLEKLHEANNELQKKRAI 594
Cdd:pfam15921 437 AMKSECQGQMERQMAAIQGKNESLEKVSSLTA--------------------------QLESTKEMLRKVVEELTAKKMT 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 595 IEDLEPRCNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNqgAAPEIQALKNQLQERDRMFHSLE 674
Cdd:pfam15921 491 LESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRN--VQTECEALKLQMAEKDKVIEILR 568
|
....
gi 2006390933 675 KEYE 678
Cdd:pfam15921 569 QQIE 572
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
261-422 |
2.01e-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: 44.81 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 261 LEAAKDDYRIRCEE----LEKEIAELRQQTEELTTLAEEAQSLKDEIDVlrhSSDKVAKLESQVESYKKKLED----LGD 332
Cdd:pfam10174 343 LQTEVDALRLRLEEkesfLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDV---KERKINVLQKKIENLQEQLRDkdkqLAG 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 333 LRRQVKLLEEKNTMYMQNTVSLEEEL----RKANAARSQLETYKRQAVElqnrLSEESKKadkldyECKRLKEKVDSLQK 408
Cdd:pfam10174 420 LKERVKSLQTDSSNTDTALTTLEEALsekeRIIERLKEQREREDRERLE----ELESLKK------ENKDLKEKVSALQP 489
|
170
....*....|....
gi 2006390933 409 EKDRLRTERDSLKE 422
Cdd:pfam10174 490 ELTEKESSLIDLKE 503
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
359-689 |
2.34e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 359 RKANAARSQLETYKRQAVELQNRLSEESKKADKLDYEcKRLKEKVDSLQKEKDRLR-TERDSLKETIEELRcvQAQEGQL 437
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE-REKAERYQALLKEKREYEgYELLKEKEALERQK--EAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 438 TTTGLMPLGRQEPSDSLAAEIITPEIK----EKLIRLQHENKMLKLNQE-GSDNEKIALLQSLLDDANLRKNELETENRL 512
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLleelNKKIKDLGEEEQLRVKEKiGELEAEIASLERSIAEKERELEDAEERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 513 VNQRLLEVQSQVEELQKSLQDQGSKAEDflllaavlLYTNVISvswhgllLKAISVLLKKKLEEHLEKLHEANNELQKKR 592
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDK--------LTEEYAE-------LKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 593 AIIEDLEPRCNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNqgaapEIQALKNQLQERDRMFHS 672
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL-----EIKKQEWKLEQLAADLSK 466
|
330
....*....|....*...
gi 2006390933 673 LEKEYEKTKS-QREMEEK 689
Cdd:TIGR02169 467 YEQELYDLKEeYDRVEKE 484
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
179-685 |
2.36e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 179 KKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSL----LAENQILMERLNQSDSIEDPNSPAGRRHLQLQTQLEQL 254
Cdd:PTZ00121 1243 KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKAdelkKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKK 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 255 QEETFRLEAakDDYRIRCEELEKEiAELRQQTEELTTLAEEAQSLKDEIDVLRHSSDKV--------AKLESQVESYKKK 326
Cdd:PTZ00121 1323 KAEEAKKKA--DAAKKKAEEAKKA-AEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKkadaakkkAEEKKKADEAKKK 1399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 327 LEDLGDLRRQVKLLEEKNTMyMQNTVSLEEELRKANAARSQLETyKRQAVELQNRlSEESKKADKLDYECKRlKEKVDSL 406
Cdd:PTZ00121 1400 AEEDKKKADELKKAAAAKKK-ADEAKKKAEEKKKADEAKKKAEE-AKKADEAKKK-AEEAKKAEEAKKKAEE-AKKADEA 1475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 407 QK------EKDRLRTERDSLKETIEELRcvQAQEGQLTTTGLMPLGRQEPSDSL--------AAEIITPEIKEKLIRLQH 472
Cdd:PTZ00121 1476 KKkaeeakKADEAKKKAEEAKKKADEAK--KAAEAKKKADEAKKAEEAKKADEAkkaeeakkADEAKKAEEKKKADELKK 1553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 473 ENKMLKLNQEGSDNEKiallQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDFLLLAAVLLYTN 552
Cdd:PTZ00121 1554 AEELKKAEEKKKAEEA----KKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 553 VIsvswhglllKAISVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRCNNSSLKIEELQEAlrkkEEEMKQMEERYKK 632
Cdd:PTZ00121 1630 EE---------KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA----EEDEKKAAEALKK 1696
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2006390933 633 YLEKAKSVIRTldPKQNQGAAPEIQALKNQLQERDRMFHSLEKEYEKTKSQRE 685
Cdd:PTZ00121 1697 EAEEAKKAEEL--KKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
173-427 |
2.83e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 173 DLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQ-----------SDSIEDPNSPAG 241
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaanlrerLESLERRIAATE 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 242 RRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEIAELrqqTEELTTLAEEAQSLKDEIDVLrhsSDKVAKLESQVE 321
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL---LNERASLEEALALLRSELEEL---SEELRELESKRS 911
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 322 SYKKKLEDLGDLRRQVKLLEEKNTMYMQNT---------VSLEEELRKANAARSQLETYKRQAVELQNRLSE-------- 384
Cdd:TIGR02168 912 ELRRELEELREKLAQLELRLEGLEVRIDNLqerlseeysLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaa 991
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2006390933 385 -EskkadkldyECKRLKEKVDSLQKEKDRLRTERDSLKETIEEL 427
Cdd:TIGR02168 992 iE---------EYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
259-694 |
4.25e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 259 FRLEAAKDDYRIRCEELEKEIAELRQQTEELTTLAEEAQSLKDEI--DVLRHSSDKVAKLESQVEsykkkledlgDLRRQ 336
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELeaQIRGNGGDRLEQLEREIE----------RLERE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 337 VKLLEEKNTMYMQNTVSLEEElrkANAARSQLETYKRQAVELQNRLSEESKKA----DKLDYECKRLKEKVDSLQKEKDR 412
Cdd:COG4913 354 LEERERRRARLEALLAALGLP---LPASAEEFAALRAEAAALLEALEEELEALeealAEAEAALRDLRRELRELEAEIAS 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 413 LRTERDSLKETIEELRCVQAQEGQLTTTGLMPLG---------------------------------------------- 446
Cdd:COG4913 431 LERRKSNIPARLLALRDALAEALGLDEAELPFVGelievrpeeerwrgaiervlggfaltllvppehyaaalrwvnrlhl 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 447 ------------------RQEPSDSLAAEIIT------PEIKEKLIR------------LQHENK------MLKLNQE-- 482
Cdd:COG4913 511 rgrlvyervrtglpdperPRLDPDSLAGKLDFkphpfrAWLEAELGRrfdyvcvdspeeLRRHPRaitragQVKGNGTrh 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 483 --------------GSDN-EKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKsLQDQGSKAEDFLLLAAV 547
Cdd:COG4913 591 ekddrrrirsryvlGFDNrAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQR-LAEYSWDEIDVASAERE 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 548 LLytnvisvswhglllkaisvllkkKLEEHLEKLHEANNELQKKRAIIEDLEprcnnssLKIEELQEALRKKEEEMKQME 627
Cdd:COG4913 670 IA-----------------------ELEAELERLDASSDDLAALEEQLEELE-------AELEELEEELDELKGEIGRLE 719
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2006390933 628 ERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQLQE------RDRMFHSLEKEYEKTKSQREMEEKFIVSA 694
Cdd:COG4913 720 KELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAalgdavERELRENLEERIDALRARLNRAEEELERA 792
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
260-632 |
4.60e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.81 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 260 RLEAAKDDYRIRCEELEKEIAELRQQTEELTTLAEEAQSLKDEIDVLR---HSSDKVAKLESQVESYKKKLEDLGDLR-- 334
Cdd:pfam02463 146 IIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEelkLQELKLKEQAKKALEYYQLKEKLELEEey 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 335 ----RQVKLLEEKNTMYMQNTVSLEEELRKANaARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEK 410
Cdd:pfam02463 226 llylDYLKLNEERIDLLQELLRDEQEEIESSK-QEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 411 DRLRTERDSLKETIEELRCVQAQEGQLtttglmplgrQEPSDSLAAEIITPEIKEKLIRLQHENKMLKLNQEGSDNEKIA 490
Cdd:pfam02463 305 LERRKVDDEEKLKESEKEKKKAEKELK----------KEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEE 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 491 LLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSlqdqgSKAEDFLLLAAVLLYTNVISVSWHGLLLKAISVLL 570
Cdd:pfam02463 375 LLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELA-----RQLEDLLKEEKKEELEILEEEEESIELKQGKLTEE 449
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2006390933 571 KKKLEEHLEKLHEANNELQKKRAIIEDLEPRCNNSSLKIEELQEALRKKEEEMKQMEERYKK 632
Cdd:pfam02463 450 KEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKV 511
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
164-426 |
6.29e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.59 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 164 VSVGNDAYVDLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQsdsiedpnspagrr 243
Cdd:COG1340 17 IEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDE-------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 244 HLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEIAEL--RQQTEELTTlaEEAQSLKDEIDVLRHSSDKVAKLESQVE 321
Cdd:COG1340 83 LNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLewRQQTEVLSP--EEEKELVEKIKELEKELEKAKKALEKNE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 322 SYKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEELrkaNAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKE 401
Cdd:COG1340 161 KLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEM---IELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQK 237
|
250 260
....*....|....*....|....*
gi 2006390933 402 KVDSLQKEKDRLRTERDSLKETIEE 426
Cdd:COG1340 238 ELRELRKELKKLRKKQRALKREKEK 262
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
262-470 |
7.58e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.80 E-value: 7.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 262 EAAKDDYRIRCEELEKEiaelrQQTEELTTLAEEAQSLKDEIDvlRHSSDKVAKLESQVESYKKKLEDlgdlrRQVKLLE 341
Cdd:pfam17380 443 ERAREMERVRLEEQERQ-----QQVERLRQQEEERKRKKLELE--KEKRDRKRAEEQRRKILEKELEE-----RKQAMIE 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 342 EKNTMYMqntvsLEEELRKANAARSQletykrqavELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRT---ERD 418
Cdd:pfam17380 511 EERKRKL-----LEKEMEERQKAIYE---------EERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAmerERE 576
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2006390933 419 SLKETIEELRCVQAQEGQLTTTGLMPLGRQEPSdslaaEIITPEIKEKLIRL 470
Cdd:pfam17380 577 MMRQIVESEKARAEYEATTPITTIKPIYRPRIS-----EYQPPDVESHMIRF 623
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
360-547 |
8.64e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 8.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 360 KANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERDSLKETIEELRCV-------QA 432
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElgeraraLY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 433 QEGQLTTTGLMPLGRQEPSD----SLAAEIITPEIKEKLIRLQHENKMLKlNQEGSDNEKIALLQSLLDDANLRKNELET 508
Cdd:COG3883 97 RSGGSVSYLDVLLGSESFSDfldrLSALSKIADADADLLEELKADKAELE-AKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2006390933 509 ---ENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDFLLLAAV 547
Cdd:COG3883 176 qqaEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
266-376 |
1.50e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 266 DDYRIRCEELEKEIAELRQQTEELTtlAEEAQSLKDEIDVLRhssDKVAKLESQVESYKKKLEDLGDLRRQvklLEEKNt 345
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEQDEAS--FERLAELRDELAELE---EELEALKARWEAEKELIEEIQELKEE---LEQRY- 484
|
90 100 110
....*....|....*....|....*....|.
gi 2006390933 346 mymQNTVSLEEELRKANAARSQLETYKRQAV 376
Cdd:COG0542 485 ---GKIPELEKELAELEEELAELAPLLREEV 512
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
261-428 |
1.59e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 261 LEAAKDDYRIRCEELEKEIAELRQQTeELTTLAEEAQSLKDEIDVLRhssDKVAKLESQVESYKKKLEdlgDLRRQVKLL 340
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKN-GLVDLSEEAKLLLQQLSELE---SQLAEARAELAEAEARLA---ALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 341 EEKNTMYMQNTV--SLEEELRKANAARSQLET-----------YKRQAVELQNRLSEESKKA-DKLDYECKRLKEKVDSL 406
Cdd:COG3206 253 PDALPELLQSPViqQLRAQLAELEAELAELSArytpnhpdviaLRAQIAALRAQLQQEAQRIlASLEAELEALQAREASL 332
|
170 180
....*....|....*....|..
gi 2006390933 407 QKEKDRLRTERDSLKETIEELR 428
Cdd:COG3206 333 QAQLAQLEARLAELPELEAELR 354
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
169-428 |
1.64e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 169 DAYVDLDRQLKKTTEELnEALATKEEIAQRCHELDMQVAALQEEKSSLLAENqilmerlnqsdsiedpnspAGRRHLQLQ 248
Cdd:COG4913 235 DDLERAHEALEDAREQI-ELLEPIRELAERYAAARERLAELEYLRAALRLWF-------------------AQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 249 TQLEQLQEETFRLEAAKDDYRIRCEELEKEIAELRQQTEELTTlaEEAQSLKDEIDVLRhssDKVAKLESQVESYKKKLE 328
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGG--DRLEQLEREIERLE---RELEERERRRARLEALLA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 329 DLGdlrrqvklleekntmyMQNTVSLEEELRKANAARSQLETYKRQAVELQNRLseeskkaDKLDYECKRLKEKVDSLQK 408
Cdd:COG4913 370 ALG----------------LPLPASAEEFAALRAEAAALLEALEEELEALEEAL-------AEAEAALRDLRRELRELEA 426
|
250 260
....*....|....*....|
gi 2006390933 409 EKDRLRTERDSLKETIEELR 428
Cdd:COG4913 427 EIASLERRKSNIPARLLALR 446
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
274-427 |
1.93e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 274 ELEKEIAELRQQTEELTTLAEEAQSLKDEIDVLRHssdkvakLESQVESYKKKLEDLGDLRrqvklleekntmYMQNTVS 353
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIELLEP-------IRELAERYAAARERLAELE------------YLRAALR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 354 LEEELRKANAARSQLETYKRQAVELQNRLSEESKKADKLDYEC---------------KRLKEKVDSLQKEKDRLRTERD 418
Cdd:COG4913 283 LWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELdeleaqirgnggdrlEQLEREIERLERELEERERRRA 362
|
....*....
gi 2006390933 419 SLKETIEEL 427
Cdd:COG4913 363 RLEALLAAL 371
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
350-616 |
2.29e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.59 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 350 NTVSLEEELRKANAarsQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERDSLKETIEELRC 429
Cdd:TIGR02169 668 FSRSEPAELQRLRE---RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 430 ------------------VQAQEGQLTTT-GLMPLGRQEPSDSLAAEIItPEIKEKLIRLQHENKML---------KLNQ 481
Cdd:TIGR02169 745 dlssleqeienvkselkeLEARIEELEEDlHKLEEALNDLEARLSHSRI-PEIQAELSKLEEEVSRIearlreieqKLNR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 482 EGSDNE----KIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDflllaavllytnvisvs 557
Cdd:TIGR02169 824 LTLEKEylekEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD----------------- 886
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2006390933 558 whglllkaisvlLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRCNNSSLKIEELQEAL 616
Cdd:TIGR02169 887 ------------LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
260-689 |
2.78e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 260 RLEAAKDDYRIRCEELEKEIAELRQQTEELTTLAEEAQSLKDEIDVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQVKL 339
Cdd:PTZ00121 1225 KAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKA 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 340 LEEKNTmymqntvslEEELRKANAARSQLETYKRQAVELQNRlSEESKKAD--------KLDYECKRLKEKVDSLQKEKD 411
Cdd:PTZ00121 1305 DEAKKK---------AEEAKKADEAKKKAEEAKKKADAAKKK-AEEAKKAAeaakaeaeAAADEAEAAEEKAEAAEKKKE 1374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 412 RLRTERDSLKETIEELRcvQAQEGQLTTTGLMPLGrQEPSDSLAAEIITPEIKEKlirLQHENKMLKLNQEGSDNEKIAL 491
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEKK--KADEAKKKAEEDKKKA-DELKKAAAAKKKADEAKKK---AEEKKKADEAKKKAEEAKKADE 1448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 492 LQSLLDDA----NLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDFlllaavllytnvisvswhglllkais 567
Cdd:PTZ00121 1449 AKKKAEEAkkaeEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEA-------------------------- 1502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 568 vllkKKLEEHLEKLHEANNELQKKRAIiedlEPRCNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPK 647
Cdd:PTZ00121 1503 ----KKAAEAKKKADEAKKAEEAKKAD----EAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEE 1574
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2006390933 648 QNQGAAPEIQALKNQLQERDRMFHSLEKEYEKTKSQ---REMEEK 689
Cdd:PTZ00121 1575 DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEeakKAEEAK 1619
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
175-411 |
3.29e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 175 DRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSiedpnspagrrhlqlqtqleql 254
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA---------------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 255 qeetfRLEAAKDDYRIRCEELEKEIAELRQQTEELTTLAE--EAQSLKDEIDvlrhssdKVAKLESQVESYKKKLEDLGD 332
Cdd:COG3883 73 -----EIAEAEAEIEERREELGERARALYRSGGSVSYLDVllGSESFSDFLD-------RLSALSKIADADADLLEELKA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2006390933 333 LRRQVKLLEEKntmymqntvsLEEELRKANAARSQLETYKRqavELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKD 411
Cdd:COG3883 141 DKAELEAKKAE----------LEAKLAELEALKAELEAAKA---ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
183-366 |
3.68e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 183 EELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDPNSPAGRRHlqlqtqleqlqeetfRLE 262
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELE---------------ALE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 263 AAKDDYRIRCEELEKEIAELRQQTEELTTLAEEAQSLKDEIDVL--RHSSDKVAKLESQVESYKKKLEDLGDLRRQVKLL 340
Cdd:COG4717 139 AELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELleQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
170 180
....*....|....*....|....*.
gi 2006390933 341 EEKNTMYMQNTVSLEEELRKANAARS 366
Cdd:COG4717 219 QEELEELEEELEQLENELEAAALEER 244
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
261-543 |
3.70e-03 |
|
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: 40.98 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 261 LEAAKDDYRIRCEELEKEIAELRQQTEELTTLAEEA-QSLKDEIDVLR-----HSSDKVAKLESQVESYKKKLEDLGDLR 334
Cdd:pfam12128 609 AEEALQSAREKQAAAEEQLVQANGELEKASREETFArTALKNARLDLRrlfdeKQSEKDKKNKALAERKDSANERLNSLE 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 335 RQVKLLEEKNTMYMQNTvslEEELRKANAARSQletyKRQAVELQNRLSEESKKADKLDYECKRlKEKVDSLQKEKDR-- 412
Cdd:pfam12128 689 AQLKQLDKKHQAWLEEQ---KEQKREARTEKQA----YWQVVEGALDAQLALLKAAIAARRSGA-KAELKALETWYKRdl 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 413 ------------LRTERDSLKETIEELrcvqAQEGQLTTTGLMPLGRQEPSDSLAAEIITPEIKEKLIRLQHENKMLKLN 480
Cdd:pfam12128 761 aslgvdpdviakLKREIRTLERKIERI----AVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIAD 836
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2006390933 481 QEgSDNEKIALLQSLLDDANLRKNELETENRLVNQRL--LEVQSQVEELQKSLQDQGSKAEDFLL 543
Cdd:pfam12128 837 TK-LRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLatLKEDANSEQAQGSIGERLAQLEDLKL 900
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
264-433 |
4.13e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 264 AKDDYRIRCEELEKEIAELRQQTEELTTLAEEAQSLKDEIDVLRhssDKVAKLESQVESYKKKLEDL-GDLRRQVKLLEE 342
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQ---AELEALQAEIDKLQAEIAEAeAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 343 K-NTMYMQ-NTVSLEEELRKAN---------AARSQLETYKRQAVELQNRLSEESKKADkldyecKRLKEKVDSLQKEKD 411
Cdd:COG3883 91 RaRALYRSgGSVSYLDVLLGSEsfsdfldrlSALSKIADADADLLEELKADKAELEAKK------AELEAKLAELEALKA 164
|
170 180
....*....|....*....|..
gi 2006390933 412 RLRTERDSLKETIEELRCVQAQ 433
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQ 186
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
273-428 |
4.17e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 273 EELEKEIAELRQQTEELTTLAEEAQSLKDEI---------------DVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQV 337
Cdd:COG1340 39 KELAEKRDELNAQVKELREEAQELREKRDELnekvkelkeerdelnEKLNELREELDELRKELAELNKAGGSIDKLRKEI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 338 KLLEEKntmyMQNTV--------------SLEEELRKANAARSQLETYKR---QAVELQNRLSEESKKADKLDYECKRLK 400
Cdd:COG1340 119 ERLEWR----QQTEVlspeeekelvekikELEKELEKAKKALEKNEKLKElraELKELRKEAEEIHKKIKELAEEAQELH 194
|
170 180
....*....|....*....|....*...
gi 2006390933 401 EKVDSLQKEKDRLRTERDSLKETIEELR 428
Cdd:COG1340 195 EEMIELYKEADELRKEADELHKEIVEAQ 222
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
192-428 |
4.20e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.30 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 192 KEEIAQRCHELD-MQVAALQEEKSS-----LLAENQILMERLNQSDSIEDPNSpagrrhlqlQTQLEQLQEETFRLEAAK 265
Cdd:PRK05771 18 KDEVLEALHELGvVHIEDLKEELSNerlrkLRSLLTKLSEALDKLRSYLPKLN---------PLREEKKKVSVKSLEELI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 266 DDYRIRCEELEKEIAELrqqTEELTTLAEEAQSLKDEIDVLrhssdkvaklesqvesykKKLEDLG-DLRRqvkLLEEKN 344
Cdd:PRK05771 89 KDVEEELEKIEKEIKEL---EEEISELENEIKELEQEIERL------------------EPWGNFDlDLSL---LLGFKY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 345 TMYMQNTVSLE-EELRKANAARSQLETYKR----------QAVELQNRLSEESKKAD--KLDY-ECKRLKEKVDSLQKEK 410
Cdd:PRK05771 145 VSVFVGTVPEDkLEELKLESDVENVEYISTdkgyvyvvvvVLKELSDEVEEELKKLGfeRLELeEEGTPSELIREIKEEL 224
|
250
....*....|....*...
gi 2006390933 411 DRLRTERDSLKETIEELR 428
Cdd:PRK05771 225 EEIEKERESLLEELKELA 242
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
260-428 |
6.68e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.09 E-value: 6.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 260 RLEAAKDDYRIRCEELEKEIAELRQQT----------EELTTLAEEAQSLKDEIDVLRHSSDKVAKLESQVESYKKKLE- 328
Cdd:pfam05483 371 RLEKNEDQLKIITMELQKKSSELEEMTkfknnkevelEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREk 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 329 DLGDLRRQVKLLEEKNTMYMQNTVSLEEELRKANAARSQLeTYKRQAVELQNRlsEESKKADKLDYECKRLKEKVDSLQK 408
Cdd:pfam05483 451 EIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIEL-TAHCDKLLLENK--ELTQEASDMTLELKKHQEDIINCKK 527
|
170 180
....*....|....*....|
gi 2006390933 409 EKDRLRTERDSLKETIEELR 428
Cdd:pfam05483 528 QEERMLKQIENLEEKEMNLR 547
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
280-684 |
7.26e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.05 E-value: 7.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 280 AELRQQTEELTTLAEEAQSLKDEIDVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTV-----SL 354
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIerqlaSL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 355 EEELRKANAARSQLEtykRQAVELQNRLSEESKKADKL-DYECKRLKEKVDSLQKEKDRLrteRDSLKETIEELRCVQAQ 433
Cdd:TIGR02169 250 EEELEKLTEEISELE---KRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASL---ERSIAEKERELEDAEER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 434 EGQLtttglmplgrQEPSDSLAAEIitPEIKEKLIRLQHENKMLKlnqegsdnEKIALLQSLLDDANLRKNELETENRLV 513
Cdd:TIGR02169 324 LAKL----------EAEIDKLLAEI--EELEREIEEERKRRDKLT--------EEYAELKEELEDLRAELEEVDKEFAET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 514 NQRLLEVQSQVEELQKSLQDqgskaedflllaavllytnvisvswhgllLKAISVLLKKKLEEHLEKLHEANNELQKKRA 593
Cdd:TIGR02169 384 RDELKDYREKLEKLKREINE-----------------------------LKRELDRLQEELQRLSEELADLNAAIAGIEA 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 594 IIEDLEPRCNNSSLKIEELQEALrkkeeemkqmeERYKKYLEKAKSvirtldpkqnqgaapEIQALKNQLQERDRMFHSL 673
Cdd:TIGR02169 435 KINELEEEKEDKALEIKKQEWKL-----------EQLAADLSKYEQ---------------ELYDLKEEYDRVEKELSKL 488
|
410
....*....|.
gi 2006390933 674 EKEYEKTKSQR 684
Cdd:TIGR02169 489 QRELAEAEAQA 499
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
174-409 |
8.03e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 39.89 E-value: 8.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 174 LDRQLKKTTEELNEALATKEEIAqrcHELDMQVAALQEEKSSLLAENQILMERLnqsDSIEDPNSPAGRRHLQLQTQLEQ 253
Cdd:PLN02939 199 LEEQLEKLRNELLIRGATEGLCV---HSLSKELDVLKEENMLLKDDIQFLKAEL---IEVAETEERVFKLEKERSLLDAS 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 254 LQEETFRLEAAKDDYR----IRCEELEKEIAELRQQTEELTTLAEEAQSLKDEIDVLRhssDKVAKLESQVES---YKKK 326
Cdd:PLN02939 273 LRELESKFIVAQEDVSklspLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLR---DKVDKLEASLKEanvSKFS 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 327 LEDLGDLRRQVKLLEEKntmymqntvsleeeLRKANAA-RSQLETYKRQAVELQ---NRLSEESKKadkldyecKRLKEK 402
Cdd:PLN02939 350 SYKVELLQQKLKLLEER--------------LQASDHEiHSYIQLYQESIKEFQdtlSKLKEESKK--------RSLEHP 407
|
....*..
gi 2006390933 403 VDSLQKE 409
Cdd:PLN02939 408 ADDMPSE 414
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
311-427 |
9.49e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 36.85 E-value: 9.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390933 311 DKVAKLESQVESYKKKLEDLG--------DLRRQVKLLEEKNTMYmqntvslEEELRKANAARSQLETYKRQAVELQNRL 382
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEaqlqklqeDLEKQAEIAREAQQNY-------ERELVLHAEDIKALQALREELNELKAEI 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2006390933 383 SEESKKADKLDYEckrLKEKVDSLQKEKDRLRTERDSLKETIEEL 427
Cdd:pfam07926 74 AELKAEAESAKAE---LEESEESWEEQKKELEKELSELEKRIEDL 115
|
|
| |
