|
Name |
Accession |
Description |
Interval |
E-value |
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
184-711 |
0e+00 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 677.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 184 ELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQEETFRLEA 263
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 264 AKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKLLEEK 343
Cdd:pfam05622 81 ARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLGDLRRQVKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 344 NTMYMQNTVSLEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKET 423
Cdd:pfam05622 161 NAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRET 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 424 IEELRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKLNQEDSDNEKIALLQSLLDDANLRK 503
Cdd:pfam05622 241 NEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLGQEGSYRERLTELQQLLEDANRRK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 504 NELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDaiSVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFN-NSS 582
Cdd:pfam05622 321 NELETQNRLANQRILELQQQVEELQKALQEQGSKAED--SSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDsNLA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 583 LRIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQLQERDRLFHSLEKEYEKTKSQRDM 662
Cdd:pfam05622 399 QKIDELQEALRKKDEDMKAMEERYKKYVEKAKSVIKTLDPKQNPASPPEIQALKNQLLEKDKKIEHLERDFEKSKLQREQ 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 568954153 663 EEKYIVSAWYNMGMTLHKKAAEDRLASTGS-GQSFLARQRQATSTRRSYP 711
Cdd:pfam05622 479 EEKLIVTAWYNMGMALHRKAIEERLAGLSSpGQSFLARQRQATNARRGLS 528
|
|
| HkD_Hook3 |
cd22226 |
Hook domain found in protein Hook 3 (Hook3) and similar proteins; Hook3 is an adaptor protein ... |
8-160 |
2.99e-104 |
|
Hook domain found in protein Hook 3 (Hook3) and similar proteins; Hook3 is an adaptor protein for microtubule-dependent intracellular vesicle and protein trafficking. It is involved in Golgi and endosome transport. It acts as a scaffold for the opposite-polarity microtubule-based motors cytoplasmic dynein-1 and the kinesin KIF1C. It may participate in the turnover of the endocytosed scavenger receptor. Hook3 is a component of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex.
Pssm-ID: 411797 Cd Length: 153 Bit Score: 314.98 E-value: 2.99e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 8 ERVELCESLLTWIQTFNVDAPCQTAEDLTNGVVMSQVLQKIDPVYFDDNWLNRIKTEVGDNWRLKISNLKKILKGILDYN 87
Cdd:cd22226 1 DRAELCESLLTWIQTFNVDAPCQTVEDLTSGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568954153 88 HEILGQQINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQELMSK 160
Cdd:cd22226 81 HEILGQQINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMSK 153
|
|
| HOOK_N |
pfam19047 |
HOOK domain; This domain is found at the N-terminus of HOOK proteins. |
11-161 |
1.71e-95 |
|
HOOK domain; This domain is found at the N-terminus of HOOK proteins.
Pssm-ID: 465958 Cd Length: 151 Bit Score: 292.00 E-value: 1.71e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 11 ELCESLLTWIQTFNVDAPCQTAEDLTNGVVMSQVLQKIDPVYFDDNWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEI 90
Cdd:pfam19047 1 ELCDSLLTWLQTFNVPAPCATVEDLTDGVAMAQVLHQIDPSWFTEAWLSRIKEDVGDNWRLKVSNLKKILQSVVDYYQDV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568954153 91 LGQQINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQELMSKE 161
Cdd:pfam19047 81 LGQQISDFLLPDVNLIGEHSDPAELGRLLQLILGCAVNCEKKQEYIQQIMTLEESVQHVVMTAIQELMSKD 151
|
|
| HkD_Hook |
cd22222 |
Hook domain found in Hook family of microtubule-binding proteins; The Hook family includes ... |
13-159 |
3.18e-91 |
|
Hook domain found in Hook family of microtubule-binding proteins; The Hook family includes Hook1-3. Hook1 is a microtubule-binding protein required for spermatid differentiation. Hook2, also a microtubule-binding protein, contributes to the establishment and maintenance of centrosome function. It may function in the positioning or formation of aggresomes, which are pericentriolar accumulations of misfolded proteins, proteasomes and chaperones. Hook3 is an adaptor protein for microtubule-dependent intracellular vesicle and protein trafficking. It is involved in Golgi and endosome transport. It acts as a scaffold for the opposite-polarity microtubule-based motors cytoplasmic dynein-1 and the kinesin KIF1C. It may participate in the turnover of the endocytosed scavenger receptor. Hook proteins are components of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex. Hook adaptor proteins share an N-terminal conserved globular Hook domain, which folds as a variant of the helical calponin homology (CH) domain, and contacts the helix alpha1 of dynein light intermediate chain 1 (LIC1) in a hydrophobic groove.
Pssm-ID: 411793 Cd Length: 147 Bit Score: 280.67 E-value: 3.18e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 13 CESLLTWIQTFNVDAPCQTAEDLTNGVVMSQVLQKIDPVYFDDNWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEILG 92
Cdd:cd22222 1 CDSLLQWLQTFNLIAPHATAEDLSDGVAIAQVLNQIDPEYFSDSWLSKIKPDVGDNWRLKVSNLKKILKGIVDYYSEVLG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568954153 93 QQINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQELMS 159
Cdd:cd22222 81 QQISGFTMPDVNAIAEKEDPKELGRLLQLVLGCAVNCERKEEYIQAIMGLEESVQHVVMEAIQELMS 147
|
|
| HkD_Hook1 |
cd22225 |
Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a ... |
12-161 |
3.35e-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: 252.08 E-value: 3.35e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 12 LCESLLTWIQTFNVDAPCQTAEDLTNGVVMSQVLQKIDPVYFDDNWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEIL 91
Cdd:cd22225 1 LCDSLIIWLQTFNTAAPCQTVQDLTSGVAMAQVLHQIDSSWFDESWLSRIKEDVGDNWRIKMSNLKKILQGIVDYYHEFL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 92 GQQINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQELMSKE 161
Cdd:cd22225 81 DQQISEFLLPDLNRIAEHSDPVELGRLLQLILGCAVNCEKKQEHIQNIMTLEESVQHVVMTAIQELMSKE 150
|
|
| HkD_Hook2 |
cd22227 |
Hook domain found in protein Hook 2 (Hook2) and similar proteins; Hook2 is a ... |
11-160 |
6.56e-71 |
|
Hook domain found in protein Hook 2 (Hook2) and similar proteins; Hook2 is a microtubule-binding protein that contributes to the establishment and maintenance of centrosome function. It may function in the positioning or formation of aggresomes, which are pericentriolar accumulations of misfolded proteins, proteasomes and chaperones. Hook2 is a component of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex.
Pssm-ID: 411798 Cd Length: 150 Bit Score: 227.84 E-value: 6.56e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 11 ELCESLLTWIQTFNVDAPCQTAEDLTNGVVMSQVLQKIDPVYFDDNWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEI 90
Cdd:cd22227 1 ELCDSLLTWLQTFQVPSPCSSYQDLTSGVAIAQVLNRIDPSWFNEAWLGRIKEDTGDNWRLKVSNLKKILQSLLEYYQDV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 91 LGQQINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQELMSK 160
Cdd:cd22227 81 LGHQVSEDHLPDVNLIGEFSDDTELGKLLQLVLGCAISCEKKQEHIQQIMTLEESVQHVVMEAIQELLTK 150
|
|
| HkD_SF |
cd22211 |
Hook domain-containing proteins superfamily; The Hook domain superfamily includes Hook adaptor ... |
14-159 |
2.44e-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: 180.55 E-value: 2.44e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 14 ESLLTWIQTFNVDAPCQTAEDLTNGVVMSQVLQKIDPVYFDDNWLNriKTEVGDNWRLKISNLKKILKGILDYNHEILGQ 93
Cdd:cd22211 2 AALLAWINTFPLSSPVESLDDLSDGVVLAEILSQIDPSYFDSEWLE--SRDSSDNWVLKLNNLKKLYRSLSKYYREVLGQ 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568954153 94 QINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQELMS 159
Cdd:cd22211 80 QLSDLPLPDLSAIARDGDEEEIVKLLELVLGAAVQCENKEEYIARIQQLDESTQAELMLIIQEVLE 145
|
|
| HkD_HkRP |
cd22223 |
Hook domain found in the Hook-related protein (HkRP) family; The HkRP family includes Daple, ... |
12-157 |
2.67e-24 |
|
Hook domain found in the Hook-related protein (HkRP) family; The HkRP family includes Daple, Girdin and Gipie. Daple, also called Dvl-associating protein with a high frequency of leucine residues, or coiled-coil domain-containing protein 88C (CCDC88C), or Hook-related protein 2 (HkRP2), is a novel non-receptor nucleotide exchange factor (GEF) required for activation of guanine nucleotide-binding proteins (G-proteins) during non-canonical Wnt signaling. Girdin, also called Akt phosphorylation enhancer (APE), or coiled-coil domain-containing protein 88A (CCDC88A), or G alpha-interacting vesicle-associated protein (GIV), or Girders of actin filament, or Hook-related protein 1 (HkRP1), is a bifunctional modulator of guanine nucleotide-binding proteins (G proteins). It acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein G(i) alpha subunits. It also acts as a guanine nucleotide dissociation inhibitor for guanine nucleotide-binding protein G(s) subunit alpha GNAS. In addition, Girdin plays an essential role in cell migration. Gipie, also called GRP78-interacting protein induced by ER stress, or coiled-coil domain-containing protein 88B (CCDC88B), or brain leucine zipper domain-containing protein, or Hook-related protein 3 (HkRP3), is a novel actin cytoskeleton-binding protein and Akt substrate that regulates cell migratory responses in various biological contexts. It acts as a positive regulator of T-cell maturation and inflammatory function. As a microtubule-binding protein, Gipie regulates lytic granule clustering and NK cell killing. All family members contain a conserved globular Hook domain which folds as a variant of the helical calponin homology (CH) domain.
Pssm-ID: 411794 Cd Length: 149 Bit Score: 99.20 E-value: 2.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 12 LCESLLTWIQTFNVDAPCQTA-EDLTNGVVMSQVLQKIDPVYFDDnwlnRIKTEVGDNWRLKISNLKKILKGILDYNHEI 90
Cdd:cd22223 2 LSSPLVTWAKTFADDGSAELSyTDLVDGVFLNNVMLQIDPRPFSE----VSNRNVDDDVNARIQNLDLLLRNIKSFYQEV 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568954153 91 LGQQINdFTLPDVNLIGEHSDA----AELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQEL 157
Cdd:cd22223 78 LQQLIV-MKLPDILTIGREPESeqslEELEKLLLLLLGCAVQCERKEEFIERIKNLDLEVQHALVACIQEV 147
|
|
| HkD_Daple |
cd22228 |
Hook domain found in Daple (Dvl-associating protein with a high frequency of leucine residues) ... |
16-157 |
7.14e-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: 78.43 E-value: 7.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 16 LLTWIQTFnvdAPCQTAE--------DLTNGVVMSQVLQKIDPVYFDdnwlNRIKTEVGDNWRLKISNLKKILKGILDYN 87
Cdd:cd22228 6 LVTWVKTF---GPLGFGSedklsmymDLVDGVFLNKIMLQIDPRPTN----QRVNKHVNNDVNLRIQNLTILVRHIKTYY 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568954153 88 HEILgQQINDFTLPDVNLIGEH----SDAAELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQEL 157
Cdd:cd22228 79 QEVL-QQLIVMNLPNVLMIGKDplsgKSMEEIKKMLLLVLGCAVQCERKEEFIERIKQLDIETQAAIVSHIQEV 151
|
|
| HkD_Girdin |
cd22229 |
Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation ... |
16-157 |
4.64e-13 |
|
Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation enhancer (APE), or coiled-coil domain-containing protein 88A (CCDC88A), or G alpha-interacting vesicle-associated protein (GIV), or Girders of actin filament, or Hook-related protein 1 (HkRP1), is a bifunctional modulator of guanine nucleotide-binding proteins (G proteins). It acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein G(i) alpha subunits. It also acts as a guanine nucleotide dissociation inhibitor for guanine nucleotide-binding protein G(s) subunit alpha GNAS. In addition, Girdin plays an essential role in cell migration.
Pssm-ID: 411800 Cd Length: 156 Bit Score: 67.51 E-value: 4.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 16 LLTWIQTFNVDAPC---QTAE--DLTNGVVMSQVLQKIDPvyfdDNWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEI 90
Cdd:cd22229 9 LVTWVKTFGPLATGngtPLDEyvALVDGVFLNEVMLQINP----KSSNQRVNKKVNNDASLRIQNLSILVKQIKLYYQET 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568954153 91 LgQQINDFTLPDVNLIGEH--SDAA--ELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQEL 157
Cdd:cd22229 85 L-QQLIMMSLPNVLVLGRNplSEQGteEMKKLLLLLLGCAVQCERKEEFIERIQTLDFDTKAAVAAHIQEV 154
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
154-665 |
2.52e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.48 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 154 IQELMSKESPVSAGHDAYVDLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSI 233
Cdd:PRK03918 209 INEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 234 EdpnsPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSS--- 310
Cdd:PRK03918 289 K----EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHely 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 311 DKVSKLEGQVESYKKKLEDL--GDLRRQVKLLEEKNTmymqntvSLEEELRKANAARGQLET----YKRQVVELQ----- 379
Cdd:PRK03918 365 EEAKAKKEELERLKKRLTGLtpEKLEKELEELEKAKE-------EIEEEISKITARIGELKKeikeLKKAIEELKkakgk 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 380 ----NRLSDESKKAD----------KLDFEYKRLKEKVDGLQKEKDRLRTERD------SLKETIEELRCVQAQegqltt 439
Cdd:PRK03918 438 cpvcGRELTEEHRKElleeytaelkRIEKELKEIEEKERKLRKELRELEKVLKkeseliKLKELAEQLKELEEK------ 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 440 qglmpLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKlnqedSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLE 519
Cdd:PRK03918 512 -----LKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLK-----KELEKLEELKKKLAELEKKLDELEEELAELLKELEE 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 520 VQ-SQVEELQKSLQDQGSKAEDAISVL-LKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLRIEELQealrkKEE 597
Cdd:PRK03918 582 LGfESVEELEERLKELEPFYNEYLELKdAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELE-----KKY 656
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568954153 598 EMKQMEERYKKYLEKAKSVirtldpkqnQGAAPEIQALKNQLQERDRLFHSLEKEYEKTKSQRDMEEK 665
Cdd:PRK03918 657 SEEEYEELREEYLELSREL---------AGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
260-635 |
3.38e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 260 RLEAAKDDY---RIRCEELEKEISELRQQndelTTLADEAQSLKDEIDVLrhssdkvsKLEGQVESYKKKLEDLGDLRRQ 336
Cdd:COG1196 180 KLEATEENLerlEDILGELERQLEPLERQ----AEKAERYRELKEELKEL--------EAELLLLKLRELEAELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 337 VKLLEEKNTMYMQNTVSLEEELRKANAARGQLEtykRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTE 416
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELE---LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 417 RDSLKETIEELrcvQAQEGQLTTQGLMplgSQESSDSLAAEIVtpEIREKLIRLQHENKMLKLNQEDSDNEKIALLQSLL 496
Cdd:COG1196 325 LAELEEELEEL---EEELEELEEELEE---AEEELEEAEAELA--EAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 497 DDANLRKNELETENRLvNQRLLEVQSQVEELQKSLQDQGSKAEDAisvllKKKLEEHLEKLHEANNELQKKRAIIEDLEP 576
Cdd:COG1196 397 ELAAQLEELEEAEEAL-LERLERLEEELEELEEALAELEEEEEEE-----EEALEEAAEEEAELEEEEEALLELLAELLE 470
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 568954153 577 RFNNSSLRIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQAL 635
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL 529
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
260-593 |
4.27e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.62 E-value: 4.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 260 RLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDK-VSKLEGQVESYKKKLEDL----GDLR 334
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdLARLEAEVEQLEERIAQLskelTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 335 RQVKLLEEKNTMYMQNTVSLEEEL----RKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEK 410
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIeeleAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 411 DRLRTERDSLKETIEELRCVQAQEGQLTTQglmplgSQESSDSLAAEIVTPEIREKLIRLQHENKMLKLNQEDSDN---- 486
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEE------LESELEALLNERASLEEALALLRSELEELSEELRELESKRselr 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 487 EKIALLQSLLDDANLRKNELETENRLVNQRLLEVQS----QVEELQKSLQDQGSKAEDAIsvllkKKLEEHLEKLHEANN 562
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSltleEAEALENKIEDDEEEARRRL-----KRLENKIKELGPVNL 989
|
330 340 350
....*....|....*....|....*....|...
gi 568954153 563 ElqkkrAI--IEDLEPRFNNSSLRIEELQEALR 593
Cdd:TIGR02168 990 A-----AIeeYEELKERYDFLTAQKEDLTEAKE 1017
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
153-661 |
5.07e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.22 E-value: 5.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 153 AIQELMSKESPVSAGHDAYVDLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDS 232
Cdd:PRK02224 207 RLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 233 IEDpnspagrrhlqlqtqleqlqeetfRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQslkdeiDVLRHSSDK 312
Cdd:PRK02224 287 RLE------------------------ELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELR------DRLEECRVA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 313 VSKLEGQVESYKKKLEDLgdlrrqvkllEEKNTMYMQNTVSLEEELRkanAARGQLETYKRQVVELQNRLSDESKKADKL 392
Cdd:PRK02224 337 AQAHNEEAESLREDADDL----------EERAEELREEAAELESELE---EAREAVEDRREEIEELEEEIEELRERFGDA 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 393 DFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTpEIREKLIRLQH 472
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIE-EDRERVEELEA 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 473 ENKMLKLNQEDSDN--EKIALLQSLLDDANLRKNELETENRLVNQR---LLEVQSQVEELQKSLQDQGSKAEDAISVLLK 547
Cdd:PRK02224 483 ELEDLEEEVEEVEErlERAEDLVEAEDRIERLEERREDLEELIAERretIEEKRERAEELRERAAELEAEAEEKREAAAE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 548 KKL--EEHLEKLHEANNELQKKRAIIEDLEpRFNNSSLRIEELQ---EALRKKEEEMKQMEERYKKYLEKAKSVIRTLDP 622
Cdd:PRK02224 563 AEEeaEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEdeiERLREKREALAELNDERRERLAEKRERKRELEA 641
|
490 500 510
....*....|....*....|....*....|....*....
gi 568954153 623 KQNQGAapeIQALKNQLQERDRLFHSLEKEYEKTKSQRD 661
Cdd:PRK02224 642 EFDEAR---IEEAREDKERAEEYLEQVEEKLDELREERD 677
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
355-661 |
3.64e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.54 E-value: 3.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 355 EEELRKANAARGQLETYKRQVVEL---QNRLSDESKKADKldfeYKRLKEKVDGLQK-----EKDRLRTERDSLKETIEE 426
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELerqLKSLERQAEKAER----YKELKAELRELELallvlRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 427 LrcvqaqegqlttqglmplgsQESSDSLAAEIVTPEIREKLIRLQHENkmlklnqedsDNEKIALLQSLLDDANLRKNEL 506
Cdd:TIGR02168 251 A--------------------EEELEELTAELQELEEKLEELRLEVSE----------LEEEIEELQKELYALANEISRL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 507 ETENRLVNQRLLEVQSQVEELQKSLQDQGSKAED--AISVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLR 584
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDElaEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568954153 585 IEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQLQERDRLFHSLEKEYEKTKSQRD 661
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE 457
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
274-613 |
2.32e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.84 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 274 ELEKEISELRQQndeLTTLADEAQSLKDEIDVLRhssDKVSKLEGQVESYKKKLEDLgdlRRQVKLLEEkntmymqntvS 353
Cdd:TIGR02168 674 ERRREIEELEEK---IEELEEKIAELEKALAELR---KELEELEEELEQLRKELEEL---SRQISALRK----------D 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 354 LEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEELRC-VQA 432
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAeLTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 433 QEGQLTTQGLMPLGSQESSDSLAAEIVtpEIREKLIRLQHENKMLKLNQEDSDnEKIALLQSLLDDANLRKNELETENRL 512
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLE--DLEEQIEELSEDIESLAAEIEELE-ELIEELESELEALLNERASLEEALAL 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 513 VNQRLLEVQSQVEELQKSLQDqgskaedaisvlLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLRIEELQEAL 592
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSE------------LRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEAL 959
|
330 340
....*....|....*....|.
gi 568954153 593 RKKEEEMKQMEERYKKYLEKA 613
Cdd:TIGR02168 960 ENKIEDDEEEARRRLKRLENK 980
|
|
| HkD_Gipie |
cd22230 |
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar ... |
15-157 |
9.36e-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: 55.22 E-value: 9.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 15 SLLTWIQTF----------------NVDAPCQTAED----LTNGVVMSQVLQKIDPVyfddNWLNRIKTEVGDNWRLKIS 74
Cdd:cd22230 7 ALVTWALGFeglvgeeedslgfpeeEEEEGTLDAEKrflrLSNGDLLNRVMGIIDPS----PRGGPRMRGDDGPAAHRVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 75 NLKKILKGILDYNHEILgQQINDFTLPDVNLIGEH----SDAAELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVV 150
Cdd:cd22230 83 NLHILWGRLRDFYQEEL-QQLILSPPPDLQVMGRDpfteEAVQELEKLLRLLLGAAVQCERRELFIRHIQGLDLDVQAEL 161
|
....*..
gi 568954153 151 MTAIQEL 157
Cdd:cd22230 162 AEAIQEV 168
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
173-532 |
1.03e-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: 58.93 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 173 DLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLaENQILMERLnqsdsIEDPNSPAGRRHLQLQTQLE 252
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEK-----REYEGYELLKEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 253 QLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTT-----LADEAQSLKDEIDVLrhsSDKVSKLEGQVESYKKKL 327
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKkikdlGEEEQLRVKEKIGEL---EAEIASLERSIAEKEREL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 328 EDLGDLRRQVKLLEEKNTMYMQNtvsLEEELRKANAARGQLET----YKRQVVELQNRLSDESKKADKLDFEYKRLKEKV 403
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEE---LEREIEEERKRRDKLTEeyaeLKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 404 DGLQKEKDRLRTERDSLKETIEELRCVQAQ-EGQLTTQGLMPLGSQESSDSLAAEIvtPEIREKLIRLQheNKMLKLNQE 482
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADlNAAIAGIEAKINELEEEKEDKALEI--KKQEWKLEQLA--ADLSKYEQE 470
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 568954153 483 DSD-NEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQ 532
Cdd:TIGR02169 471 LYDlKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
169-577 |
1.53e-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: 58.14 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 169 DAYVDLDRQLKKtteelneaLSAKEEIAQRCHELDMQVAALQeeKSSLLAENQILMERLNQSDSIEDpnspagrrhlqlq 248
Cdd:TIGR02168 193 DILNELERQLKS--------LERQAEKAERYKELKAELRELE--LALLVLRLEELREELEELQEELK------------- 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 249 tqleQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSlkdeidvlrhssdKVSKLEGQVESYKKKLE 328
Cdd:TIGR02168 250 ----EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN-------------EISRLEQQKQILRERLA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 329 dlgDLRRQVKLLEEkntmymqntvSLEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQK 408
Cdd:TIGR02168 313 ---NLERQLEELEA----------QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 409 EKDRLRTERDSLKETIEelrcvqaqegqlttqglmplgsqessdSLAAEIVtpEIREKLIRLQHENKMLKLNQEDSDNE- 487
Cdd:TIGR02168 380 QLETLRSKVAQLELQIA---------------------------SLNNEIE--RLEARLERLEDRRERLQQEIEELLKKl 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 488 ---KIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDAISVL-LKKKLEEHLEKLHEANNE 563
Cdd:TIGR02168 431 eeaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLdSLERLQENLEGFSEGVKA 510
|
410
....*....|....
gi 568954153 564 LQKKRAIIEDLEPR 577
Cdd:TIGR02168 511 LLKNQSGLSGILGV 524
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
130-654 |
3.34e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 57.05 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 130 EQKQEYIQAIMMMEESVQHVVMT--AIQELMSKESpvsaghDAYVDLDRQLKKTTEELNEALSAKEEIaqrcheLDMQVA 207
Cdd:pfam15921 103 KQKFYLRQSVIDLQTKLQEMQMErdAMADIRRRES------QSQEDLRNQLQNTVHELEAAKCLKEDM------LEDSNT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 208 ALQEEKSSLLAENQILMERLNQSDSIEDPNSPAGRRHlqlqtqlEQLQEETFRLEAAKDDYRIRceELEKEISELRQQ-- 285
Cdd:pfam15921 171 QIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEH-------DSMSTMHFRSLGSAISKILR--ELDTEISYLKGRif 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 286 --NDELTTLADEAQSlKDEIdVLRHSSDKVSKLEGQVEsykkkLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEelrkana 363
Cdd:pfam15921 242 pvEDQLEALKSESQN-KIEL-LLQQHQDRIEQLISEHE-----VEITGLTEKASSARSQANSIQSQLEIIQEQ------- 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 364 ARGQLETYKRQVVELQNRLSDESKKADkldfEYKRLKE-KVDGLQK-------EKDRLRTERDSLketieelrcvqaqeg 435
Cdd:pfam15921 308 ARNQNSMYMRQLSDLESTVSQLRSELR----EAKRMYEdKIEELEKqlvlansELTEARTERDQF--------------- 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 436 qlttqglmplgSQES---SDSLAAEIVTPEIREKLIRLQHENKMLKLNQEDSDNEKIALLQSLLDDANLRKNELETenrL 512
Cdd:pfam15921 369 -----------SQESgnlDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEA---L 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 513 VNQRLLEVQSQVEELQKSLQDQGSKAEDAISvlLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLRIEELQEAL 592
Cdd:pfam15921 435 LKAMKSECQGQMERQMAAIQGKNESLEKVSS--LTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAI 512
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568954153 593 RKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNqgAAPEIQALKNQLQERDRLFHSLEKEYE 654
Cdd:pfam15921 513 EATNAEITKLRSRVDLKLQELQHLKNEGDHLRN--VQTECEALKLQMAEKDKVIEILRQQIE 572
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
304-605 |
5.58e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 5.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 304 DVLRHSSDKVSKLEGQVES------YKKKLEDL------GDLRRQVKLLEEKNTMYMQNTVSLEEELRKANAARGQLETY 371
Cdd:TIGR02168 193 DILNELERQLKSLERQAEKaerykeLKAELRELelallvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 372 KRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTQglmplgSQESS 451
Cdd:TIGR02168 273 RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE------LEEKL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 452 DSLAAEIVtpEIREKLIRLQHENKMLKLNQEDSDNEkiallqslLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSL 531
Cdd:TIGR02168 347 EELKEELE--SLEAELEELEAELEELESRLEELEEQ--------LETLRSKVAQLELQIASLNNEIERLEARLERLEDRR 416
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568954153 532 QDQGSKAEDAISVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLRIEELQEALRKKEEEMKQMEER 605
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
174-471 |
5.86e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.23 E-value: 5.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 174 LDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDsiedpnspagRRHLQLQTQLEQ 253
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK----------ERLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 254 LQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTtlADEAQSLKDEI-DVLRHSSDKVSKLEGQVESYKKKLEDlgd 332
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE--ARLSHSRIPEIqAELSKLEEEVSRIEARLREIEQKLNR--- 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 333 lRRQVKLLEEKNTMYMQNTVSLEEELRKANAAR-----GQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQ 407
Cdd:TIGR02169 824 -LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEienlnGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568954153 408 KEKDRLRTERDSLKETIEELRC-VQAQEGQLTTQG-LMPLGSQESSDSLAAEIVTPEIREKLIRLQ 471
Cdd:TIGR02169 903 RKIEELEAQIEKKRKRLSELKAkLEALEEELSEIEdPKGEDEEIPEEELSLEDVQAELQRVEEEIR 968
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
269-667 |
8.32e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 8.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 269 RIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHS----SDKVSKLEGQVESYKKKLEDLGDLRRQVKLLEEKN 344
Cdd:PRK03918 213 SSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSkrklEEKIRELEERIEELKKEIEELEEKVKELKELKEKA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 345 TMYMQNTVSLEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLdfeyKRLKEKVDGLQKEKDRLRT---ERDSLK 421
Cdd:PRK03918 293 EEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL----EELKKKLKELEKRLEELEErheLYEEAK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 422 ETIEELRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKLNQE----------------DSD 485
Cdd:PRK03918 369 AKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEelkkakgkcpvcgrelTEE 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 486 NEKIALLQSLLDDANLRKNELETENRL--VNQRLLEVQSQVEEL-----QKSLQDQGSKAEDAISVLLKKKLE---EHLE 555
Cdd:PRK03918 449 HRKELLEEYTAELKRIEKELKEIEEKErkLRKELRELEKVLKKEselikLKELAEQLKELEEKLKKYNLEELEkkaEEYE 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 556 KLHEANNELQKKRAIIED----LEPRFNNSSLRIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNqgaapE 631
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKelekLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYN-----E 603
|
410 420 430
....*....|....*....|....*....|....*.
gi 568954153 632 IQALKNQLQERDRlfhsLEKEYEKTKSQRDMEEKYI 667
Cdd:PRK03918 604 YLELKDAEKELER----EEKELKKLEEELDKAFEEL 635
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
260-708 |
8.41e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 8.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 260 RLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLkdeidvLRHSSDKVSKLEGQVESYKKKLEDLgdLRRQVKL 339
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAE------EYELLAELARLEQDIARLEERRREL--EERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 340 LEEkntmymqntvsLEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDS 419
Cdd:COG1196 322 EEE-----------LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 420 LKETIEELRcvqaqegqlttqglmplgSQESSDSLAAEivtpEIREKLIRLQHENKMLKLNQEDSDNEKIALLQSLLDDA 499
Cdd:COG1196 391 ALRAAAELA------------------AQLEELEEAEE----ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 500 NLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDAISVLLKKKLEEHLE-------KLHEANNELQKKRAIIE 572
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgflegvkAALLLAGLRGLAGAVAV 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 573 DLEPRFNNSSLRIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQN-QGAAPEIQALKNQLQERDRLFHSLEK 651
Cdd:COG1196 529 LIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKiRARAALAAALARGAIGAAVDLVASDL 608
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 652 EYEKTKSQRDME---EKYIVSAWYNMGMTLHKKAAEDRLASTGSGQSFLARQRQATSTRR 708
Cdd:COG1196 609 READARYYVLGDtllGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR 668
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
213-668 |
1.62e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 213 KSSLLA-ENQILMERLNQSdsIEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTT 291
Cdd:COG4717 36 KSTLLAfIRAMLLERLEKE--ADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 292 LADEAQSLKDEIDVLRHSSD------KVSKLEGQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEELRkaNAAR 365
Cdd:COG4717 114 LREELEKLEKLLQLLPLYQElealeaELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLS--LATE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 366 GQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKdrlrtERDSLKETIEELR----------CVQAQEG 435
Cdd:COG4717 192 EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL-----EAAALEERLKEARlllliaaallALLGLGG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 436 QLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKLN-QEDSDNEKIALLQSLLDDANLRKNELETENRLVN 514
Cdd:COG4717 267 SLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPaLEELEEEELEELLAALGLPPDLSPEELLELLDRI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 515 QRLLEVQSQVEELQKSLQDQGskAEDAISVLLKK---KLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLRIEELQEA 591
Cdd:COG4717 347 EELQELLREAEELEEELQLEE--LEQEIAALLAEagvEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEA 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 592 LrkkeeemkqMEERYKKYLEKAKSVIRTLDPKQNQgAAPEIQALKNQLQ--ERDRLFHSLEKEYEKTKSQ-RDMEEKYIV 668
Cdd:COG4717 425 L---------DEEELEEELEELEEELEELEEELEE-LREELAELEAELEqlEEDGELAELLQELEELKAElRELAEEWAA 494
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
173-664 |
2.04e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 173 DLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLA-----ENQILMERLNQSDSIEDpnspAGRRHLQL 247
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAelarlEQDIARLEERRRELEER----LEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 248 QTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRhsSDKVSKLEGQVESYKKKL 327
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA--EELLEALRAAAELAAQLE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 328 EDLGDLRRQVKLLEEKNTMYMQNTVSLEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQ 407
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 408 KEKDRLRTERDSLKETIEE----LRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPE-----IREKLIRLQHENKMLK 478
Cdd:COG1196 484 EELAEAAARLLLLLEAEADyegfLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAalaaaLQNIVVEDDEVAAAAI 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 479 LNQEDSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDAISVLLKKKLEEHLEKLH 558
Cdd:COG1196 564 EYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLA 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 559 EANNELQKKRAIIEDLEPRFNNSSLRIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQ 638
Cdd:COG1196 644 GRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEE 723
|
490 500
....*....|....*....|....*.
gi 568954153 639 LQERDRLFHSLEKEYEKTKSQRDMEE 664
Cdd:COG1196 724 EALEEQLEAEREELLEELLEEEELLE 749
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
173-427 |
4.72e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.53 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 173 DLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAE-------------NQILMERLNQSDSIEDPNSP 239
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlshsripeiqaelSKLEEEVSRIEARLREIEQK 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 240 AGRRHLQLQTQLEQLQEetfrLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQ-SLKDEIDVLRHSSDKVSKLEG 318
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQE----LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEaALRDLESRLGDLKKERDELEA 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 319 QVESYKKKLEDLG----DLRRQVKLLEEKNTMYMQNTVSLEEELRK---ANAARGQLETYKRQVVELQNRLSDESKKADK 391
Cdd:TIGR02169 897 QLRELERKIEELEaqieKKRKRLSELKAKLEALEEELSEIEDPKGEdeeIPEEELSLEDVQAELQRVEEEIRALEPVNML 976
|
250 260 270
....*....|....*....|....*....|....*.
gi 568954153 392 LDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEEL 427
Cdd:TIGR02169 977 AIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
336-540 |
6.56e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 6.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 336 QVKLLEEKNTMYMQNTVSLEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRT 415
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 416 ERDSLKETIEELrcVQAQEGQLTTQGLMPLGSQESSDSLAA-----EIVTPEIREKLIRLQHENKMLKLNQEDSDNEKiA 490
Cdd:COG4942 98 ELEAQKEELAEL--LRALYRLGRQPPLALLLSPEDFLDAVRrlqylKYLAPARREQAEELRADLAELAALRAELEAER-A 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568954153 491 LLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAED 540
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
269-616 |
1.13e-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: 52.38 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 269 RIRCEELEKEISELRQQNDELTTLADEA-QSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLgdlRRQVKLLEEKNTMY 347
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELsQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL---EEDLSSLEQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 348 MQNTVSLEEELrkaNAARGQLETYKRQVVELQNRLSDE-----SKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKE 422
Cdd:TIGR02169 757 KSELKELEARI---EELEEDLHKLEEALNDLEARLSHSripeiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEK 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 423 TIEELRCVQAQegqlttqglmpLGSQESSDSLAAEIVTPEIREKLIRL-QHENKMLKLNQEDSDNEK-IALLQSLLDDAN 500
Cdd:TIGR02169 834 EIQELQEQRID-----------LKEQIKSIEKEIENLNGKKEELEEELeELEAALRDLESRLGDLKKeRDELEAQLRELE 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 501 LRKNELETENRLVNQRLLEVQSQVEELQkslqDQGSKAEDAISVLLKKKLEE-HLEKLHEannELQKKRAIIEDLEP--- 576
Cdd:TIGR02169 903 RKIEELEAQIEKKRKRLSELKAKLEALE----EELSEIEDPKGEDEEIPEEElSLEDVQA---ELQRVEEEIRALEPvnm 975
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 568954153 577 ----RFNNSSLRIEELQEALRKKEEEMKQMEERYKKYLEKAKSV 616
Cdd:TIGR02169 976 laiqEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
260-511 |
2.15e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 260 RLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQslkDEIDVLRHsSDKVSKLEGQVESYKKKLEDLGDLRRQVKL 339
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDALQERREALQRLAEYSW---DEIDVASA-EREIAELEAELERLDASSDDLAALEEQLEE 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 340 LEEKntmymqnTVSLEEELRKANAARGQLET----YKRQVVELQNRLSDESKKADKLDFEY-----------KRLKEKVD 404
Cdd:COG4913 697 LEAE-------LEELEEELDELKGEIGRLEKeleqAEEELDELQDRLEAAEDLARLELRALleerfaaalgdAVERELRE 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 405 GLQKEKDRLRTERDSLKETIEELRcvqaqegqLTTQGLMPLGSQESSDSLAAEivtPEIREKLIRLQ------HENKMLK 478
Cdd:COG4913 770 NLEERIDALRARLNRAEEELERAM--------RAFNREWPAETADLDADLESL---PEYLALLDRLEedglpeYEERFKE 838
|
250 260 270
....*....|....*....|....*....|...
gi 568954153 479 LNQEDSDNEKIALLQSLLDDANLRKNELETENR 511
Cdd:COG4913 839 LLNENSIEFVADLLSKLRRAIREIKERIDPLND 871
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
171-685 |
2.19e-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: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 171 YVDLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDsiedpnspagrrHLQLQTQ 250
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE------------DRRERLQ 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 251 LEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEID-VLRHSSDKVSKLEGQVESYKKKLED 329
Cdd:TIGR02168 421 QEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEqALDAAERELAQLQARLDSLERLQEN 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 330 LGDLRRQVK-LLEEKNTMY-----MQNTVSLEEELRKA-----------------NAARGQLETYKRQVVELQNRLSDES 386
Cdd:TIGR02168 501 LEGFSEGVKaLLKNQSGLSgilgvLSELISVDEGYEAAieaalggrlqavvvenlNAAKKAIAFLKQNELGRVTFLPLDS 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 387 KKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEEL--RCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTP--- 461
Cdd:TIGR02168 581 IKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLlgGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPggv 660
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 462 ----EIREKLIRLQHENKMLKLNQE-DSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGS 536
Cdd:TIGR02168 661 itggSAKTNSSILERRREIEELEEKiEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA 740
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 537 KAE----------------DAISVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLRIEELQEALRKKEEEMK 600
Cdd:TIGR02168 741 EVEqleeriaqlskeltelEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 601 QMEERYKKYLEKAKSVIRTLDPKQNQgaapeiqaLKNQLQERDRLFHSLEK-EYEKTKSQRDMEEKYIVSAWYNMGMTLH 679
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQ--------IEELSEDIESLAAEIEElEELIEELESELEALLNERASLEEALALL 892
|
....*.
gi 568954153 680 KKAAED 685
Cdd:TIGR02168 893 RSELEE 898
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
304-593 |
2.48e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 304 DVLRHSSDKVSKLEGQVESYKkkleDLGDLRRQVK--LLEEKNTM--------YMQNTVSLEEELRKANAARGQLEtykr 373
Cdd:COG4913 184 RRLGIGSEKALRLLHKTQSFK----PIGDLDDFVReyMLEEPDTFeaadalveHFDDLERAHEALEDAREQIELLE---- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 374 QVVELQNRLSDESKKADKLD-----FEYKRLKEKVDGLQKEKDRLRTERDSLKETIEELrcvQAQEGQLttqglmplgsq 448
Cdd:COG4913 256 PIRELAERYAAARERLAELEylraaLRLWFAQRRLELLEAELEELRAELARLEAELERL---EARLDAL----------- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 449 essdslaaeivtpeiREKLIRLQHEnkmlklnQEDSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQ 528
Cdd:COG4913 322 ---------------REELDELEAQ-------IRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASA 379
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568954153 529 KSLQDQGSKAEDAISVL------LKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLRIEELQEALR 593
Cdd:COG4913 380 EEFAALRAEAAALLEALeeeleaLEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
173-641 |
3.44e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 173 DLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDpnsPAGRRHLQLQTQLE 252
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA---EAEEELEELAEELL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 253 QLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDEL-TTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLG 331
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELeEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 332 DLRRQVKLLEEKNTMYMQNTVSLEEELRKANA-ARGQLETYKR-QVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKE 409
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEAdYEGFLEGVKAaLLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 410 KDRLRTERDsLKETIEELRcvQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKLNQEDSDNEKI 489
Cdd:COG1196 550 NIVVEDDEV-AAAAIEYLK--AAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRT 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 490 aLLQSLLDDANLRKNELETENRLVNQ--RLLEVQSQVEELQKSLQDQGSKAEDAISVLLKKKLEEHLEKLHEANNELQKK 567
Cdd:COG1196 627 -LVAARLEAALRRAVTLAGRLREVTLegEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEE 705
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568954153 568 RAIIEDLEPRFNNSSLRIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQgAAPEIQALKNQLQE 641
Cdd:COG1196 706 ERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEE-LERELERLEREIEA 778
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
364-643 |
3.61e-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: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 364 ARGQLETYKRQVVELQNRLSDeskkadkldfeykrLKEKVDGLQKEKDRLRTERDSLkETIEELRcvqaqegqlttqglm 443
Cdd:COG4913 608 NRAKLAALEAELAELEEELAE--------------AEERLEALEAELDALQERREAL-QRLAEYS--------------- 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 444 plgsqessdslAAEIVTPEIREKLIRLQHEnkmlkLNQEDSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQ 523
Cdd:COG4913 658 -----------WDEIDVASAEREIAELEAE-----LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE 721
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 524 V---EELQKSLQDQGSKAEDAISVLLKKKLEEHLEKLHEANNELQKKRAI---IEDLEPRFNNSSLRIEELQEAlrkkee 597
Cdd:COG4913 722 LeqaEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLeerIDALRARLNRAEEELERAMRA------ 795
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 568954153 598 emkqmeerykkYLEKAKSVIRTLDPkqNQGAAPEIQALKNQLQERD 643
Cdd:COG4913 796 -----------FNREWPAETADLDA--DLESLPEYLALLDRLEEDG 828
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
350-592 |
3.87e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 3.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 350 NTVSLEEELRKANAargQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEELRc 429
Cdd:TIGR02169 668 FSRSEPAELQRLRE---RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELE- 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 430 vqaQEGQLTTQGLmpLGSQESSDSLAAEIvtPEIREKLIRLQHE-----------------NKMLKLNQEDSDNE----- 487
Cdd:TIGR02169 744 ---EDLSSLEQEI--ENVKSELKELEARI--EELEEDLHKLEEAlndlearlshsripeiqAELSKLEEEVSRIEarlre 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 488 -----------------KIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDaisvlLKKKL 550
Cdd:TIGR02169 817 ieqklnrltlekeylekEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD-----LKKER 891
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 568954153 551 EEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLRIEELQEAL 592
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
299-587 |
5.06e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.97 E-value: 5.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 299 LKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEEL-RKANAARGQLETYKRQVVE 377
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLaKEEEELKSELLKLERRKVD 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 378 LQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEELRCVQAQEgqlttqglmplgSQESSDSLAAE 457
Cdd:pfam02463 312 DEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKL------------EQLEEELLAKK 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 458 IVTPEIREKLIRLQHENKMLKLNQEDSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSK 537
Cdd:pfam02463 380 KLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELK 459
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 568954153 538 AEDAISVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLRIEE 587
Cdd:pfam02463 460 LLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGL 509
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
325-670 |
8.34e-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: 8.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 325 KKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEElrkanaaRGQLETYKRQVVELQN-RLSDESKKADKLDFEYKRLKEKV 403
Cdd:TIGR02169 174 KALEELEEVEENIERLDLIIDEKRQQLERLRRE-------REKAERYQALLKEKREyEGYELLKEKEALERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 404 DGLQKEKDRLRTERDSLKETIEELRCVQAQEgqltTQGLMPLGSQESSdSLAAEIVtpEIREKLIRLQHENKMLKLNQED 483
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEEL----NKKIKDLGEEEQL-RVKEKIG--ELEAEIASLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 484 SDnEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDqgskaedaisvlLKKKLEEHLEKLHEANNE 563
Cdd:TIGR02169 320 AE-ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELED------------LRAELEEVDKEFAETRDE 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 564 LQKKRAIIEDLEPRFNNSSLRIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNqgaapEIQALKNQLQERD 643
Cdd:TIGR02169 387 LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL-----EIKKQEWKLEQLA 461
|
330 340
....*....|....*....|....*..
gi 568954153 644 RLFHSLEKEYEKTKSQRDMEEKYIVSA 670
Cdd:TIGR02169 462 ADLSKYEQELYDLKEEYDRVEKELSKL 488
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
360-543 |
1.06e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 360 KANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEELRCV-------QA 432
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElgeraraLY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 433 QEGQLTTQGLMPLGSQESSD----SLAAEIVTPEIREKLIRLQHENKMLKlNQEDSDNEKIALLQSLLDDANLRKNELET 508
Cdd:COG3883 97 RSGGSVSYLDVLLGSESFSDfldrLSALSKIADADADLLEELKADKAELE-AKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 568954153 509 ---ENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDAIS 543
Cdd:COG3883 176 qqaEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
273-427 |
1.18e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 273 EELEKEISELRQqndELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESykkkLEDLGDLRRQVklleekntmymqntV 352
Cdd:COG4913 613 AALEAELAELEE---ELAEAEERLEALEAELDALQERREALQRLAEYSWD----EIDVASAEREI--------------A 671
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568954153 353 SLEEELRKANAARGQLETYKRQVVELQNRLsdeskkaDKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEEL 427
Cdd:COG4913 672 ELEAELERLDASSDDLAALEEQLEELEAEL-------EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
273-565 |
1.55e-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: 48.58 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 273 EELEKEISELRQQNDELTTLADEAQSLKDE-------IDVLRHSSD----KVSKLEGQVESYKKKLEdlGDLRRQVKLLE 341
Cdd:pfam15921 377 DQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDdrnmEVQRLEALLKAMKSECQ--GQMERQMAAIQ 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 342 EKN------TMYMQNTVSLEEELRKA----NAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKD 411
Cdd:pfam15921 455 GKNeslekvSSLTAQLESTKEMLRKVveelTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQ 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 412 RLRTERDSLKETIEELRCVQAQEGQ---------LTTQGLMPLGSQESSDSLAAEI----VTPEIREKLIRLQhENKMLK 478
Cdd:pfam15921 535 HLKNEGDHLRNVQTECEALKLQMAEkdkvieilrQQIENMTQLVGQHGRTAGAMQVekaqLEKEINDRRLELQ-EFKILK 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 479 lnqeDSDNEKIALLQSLLDDANLRKNELETEN----RLVNQRLLEVQSQVEELQKSLQDQGSKAEDaiSVLLKKKLEEHL 554
Cdd:pfam15921 614 ----DKKDAKIRELEARVSDLELEKVKLVNAGserlRAVKDIKQERDQLLNEVKTSRNELNSLSED--YEVLKRNFRNKS 687
|
330
....*....|.
gi 568954153 555 EKLHEANNELQ 565
Cdd:pfam15921 688 EEMETTTNKLK 698
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
260-426 |
2.12e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 260 RLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDV-LRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVK 338
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKeIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 339 LLEEKNTMYMQNTVsLEEELRKANAargQLETYKRQVVELQNRLSdesKKADKLDFEYKRLKEKVDGLQKEKDRLRTERD 418
Cdd:COG1579 94 LQKEIESLKRRISD-LEDEILELME---RIEELEEELAELEAELA---ELEAELEEKKAELDEELAELEAELEELEAERE 166
|
....*...
gi 568954153 419 SLKETIEE 426
Cdd:COG1579 167 ELAAKIPP 174
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
260-505 |
3.19e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 260 RLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDL------ 333
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAeeenki 1661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 334 -RRQVKLLEEKNTMYMQNTVSLEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDR 412
Cdd:PTZ00121 1662 kAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE 1741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 413 LRTERDSLKETIEELRCVQ---------AQEGQLTTQGLMPLGSQESSDSLAAEI--VTPEIREKLIRLQHENKMLKLNQ 481
Cdd:PTZ00121 1742 DKKKAEEAKKDEEEKKKIAhlkkeeekkAEEIRKEKEAVIEEELDEEDEKRRMEVdkKIKDIFDNFANIIEGGKEGNLVI 1821
|
250 260
....*....|....*....|....
gi 568954153 482 EDSDNEKIALLQSLLDDANLRKNE 505
Cdd:PTZ00121 1822 NDSKEMEDSAIKEVADSKNMQLEE 1845
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
301-592 |
3.23e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 301 DEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEELRKANAargQLETYKRQVVELQN 380
Cdd:PRK03918 138 DAILESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEK---ELEEVLREINEISS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 381 RLSDESKKADKLDFEYKRL---KEKVDGLQKEKDRLRTERDSLKETIEELRCVQAQegqlTTQGLMPLGSQESSDSLAAE 457
Cdd:PRK03918 215 ELPELREELEKLEKEVKELeelKEEIEELEKELESLEGSKRKLEEKIRELEERIEE----LKKEIEELEEKVKELKELKE 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 458 IVTPEIREKLIRLQHENKMLKLNQEDSD-NEKIALLQSLLDDANLRKNEL-ETENRL--VNQRLLEVQSQVEELQ--KSL 531
Cdd:PRK03918 291 KAEEYIKLSEFYEEYLDELREIEKRLSRlEEEINGIEERIKELEEKEERLeELKKKLkeLEKRLEELEERHELYEeaKAK 370
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568954153 532 QDQGSKAEDAISVLLKKKLEEHLEKLHEANNELQKKraiIEDLEPRFNNSSLRIEELQEAL 592
Cdd:PRK03918 371 KEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEE---ISKITARIGELKKEIKELKKAI 428
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
173-427 |
3.55e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 173 DLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQ-----------SDSIEDPNSPAG 241
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaanlrerLESLERRIAATE 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 242 RRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDE-IDVLRHSSDKVSKLEGQV 320
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEElSEELRELESKRSELRREL 917
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 321 ESYKKKLEDLgDLRRQ---VKLLEEKNTMYMQNTVSLEEELRKANAARGQLETYKRQVVELQNRLSD---------Eskk 388
Cdd:TIGR02168 918 EELREKLAQL-ELRLEgleVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaaiE--- 993
|
250 260 270
....*....|....*....|....*....|....*....
gi 568954153 389 adkldfEYKRLKEKVDGLQKEKDRLRTERDSLKETIEEL 427
Cdd:TIGR02168 994 ------EYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
183-661 |
3.88e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.20 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 183 EELNEaLSAKEEIAQRcheLDMQVAALQEEKSSLLAENQILMERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQEETFRLE 262
Cdd:PRK01156 239 SALNE-LSSLEDMKNR---YESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQIL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 263 AAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDlgdlrrqvkllEE 342
Cdd:PRK01156 315 SNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEE-----------YS 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 343 KNTMYMQNTVSLEEELRKANAargqlETYKRQVVELQNRLSDeskkadkldfeykrLKEKVDGLQKEKDRLRTERDSLKE 422
Cdd:PRK01156 384 KNIERMSAFISEILKIQEIDP-----DAIKKELNEINVKLQD--------------ISSKVSSLNQRIRALRENLDELSR 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 423 TIEelrcvqaqegQLTTQGLMPLGSQESSDSLAAEIVTpEIREKLIRLQHENKMLKLNQEDSDNEKIALLQSLLDDANLR 502
Cdd:PRK01156 445 NME----------MLNGQSVCPVCGTTLGEEKSNHIIN-HYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEE 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 503 KNELETENRLVNQRLLEVQsQVEELQKSLQDQGSKAEDAISVLLKKKLEEHLEKLHEANNELQKKRAI-IEDLEPRFNNS 581
Cdd:PRK01156 514 INKSINEYNKIESARADLE-DIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVISLIdIETNRSRSNEI 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 582 SLRIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNqgaapEIQALKNQLQERDRLFHSLEKEYEKTKSQRD 661
Cdd:PRK01156 593 KKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYN-----EIQENKILIEKLRGKIDNYKKQIAEIDSIIP 667
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
351-593 |
6.36e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.67 E-value: 6.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 351 TVSLEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTE----RDSLKETIEE 426
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKvkelKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 427 LRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIvtpeirEKLIRlQHENKMLKLNQEDSDNEKIALLQSLLDDAnLRKNEL 506
Cdd:COG1340 87 LNELREELDELRKELAELNKAGGSIDKLRKEI------ERLEW-RQQTEVLSPEEEKELVEKIKELEKELEKA-KKALEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 507 ETENRLVNQRLLEVQSQVEELQKSLQDQGSKAE--DAISVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLR 584
Cdd:COG1340 159 NEKLKELRAELKELRKEAEEIHKKIKELAEEAQelHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKE 238
|
....*....
gi 568954153 585 IEELQEALR 593
Cdd:COG1340 239 LRELRKELK 247
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
260-665 |
9.54e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 9.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 260 RLEAAKDdyriRCEELEKEISELRQQNDELTTLADE---AQSLKDEIDVLRHSSDKVSKLEG---QVESYKKKLEDLGDL 333
Cdd:PTZ00121 1358 EAEAAEE----KAEAAEKKKEEAKKKADAAKKKAEEkkkADEAKKKAEEDKKKADELKKAAAakkKADEAKKKAEEKKKA 1433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 334 RRQVKLLEEKNTMymQNTVSLEEELRKANAARGQLETyKRQVVELQNRlSDESKKADKLDFEYKRLKEKVDGLQKeKDRL 413
Cdd:PTZ00121 1434 DEAKKKAEEAKKA--DEAKKKAEEAKKAEEAKKKAEE-AKKADEAKKK-AEEAKKADEAKKKAEEAKKKADEAKK-AAEA 1508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 414 RTERDSLKETIEELRCVQAQEGQLTTQglmplgsqessdslAAEIVTPEIREKLIRLQHENKMLKLNQEDSDNEKiallQ 493
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAEEAKK--------------ADEAKKAEEKKKADELKKAEELKKAEEKKKAEEA----K 1570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 494 SLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDA-ISVLLKKKLEEHLEKLHEANNELQKKRAIIE 572
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAkIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE 1650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 573 DLEPRFNNSSLRIEELQ----------EALRKKEEEMKQMEERYKKYLEKAKSVIRTldPKQNQGAAPEIQALKNQLQER 642
Cdd:PTZ00121 1651 ELKKAEEENKIKAAEEAkkaeedkkkaEEAKKAEEDEKKAAEALKKEAEEAKKAEEL--KKKEAEEKKKAEELKKAEEEN 1728
|
410 420
....*....|....*....|....*...
gi 568954153 643 DRLFHSLEKEYEKTK-----SQRDMEEK 665
Cdd:PTZ00121 1729 KIKAEEAKKEAEEDKkkaeeAKKDEEEK 1756
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
395-659 |
1.27e-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: 45.44 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 395 EYKRLKEKVDGLQKEKDRLRTERDSLKETIEELRcVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHEN 474
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELS-QELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 475 KMLKLNQEDSdNEKIALLQslLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDaisvlLKKKLEEHL 554
Cdd:TIGR02169 754 ENVKSELKEL-EARIEELE--EDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE-----IEQKLNRLT 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 555 EKLHEANNELQKKRAIIEDLEPRFNNSSLRIEELQEALRKKEEEmkqmeerykkyLEKAKSVIRTLDpKQNQGAAPEIQA 634
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE-----------LEELEAALRDLE-SRLGDLKKERDE 893
|
250 260
....*....|....*....|....*
gi 568954153 635 LKNQLQERDRLFHSLEKEYEKTKSQ 659
Cdd:TIGR02169 894 LEAQLRELERKIEELEAQIEKKRKR 918
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
276-428 |
1.96e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 276 EKEISELRQQNDE--------LTTLADEAQSLKDEIDVLrhsSDKVSKLEGQVESYKKKLEDLG----DLRRQVKLLEEK 343
Cdd:PHA02562 201 NKNIEEQRKKNGEniarkqnkYDELVEEAKTIKAEIEEL---TDELLNLVMDIEDPSAALNKLNtaaaKIKSKIEQFQKV 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 344 NTMYMQNTV-----------------------SLEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLK 400
Cdd:PHA02562 278 IKMYEKGGVcptctqqisegpdritkikdklkELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLV 357
|
170 180
....*....|....*....|....*...
gi 568954153 401 EKVDGLQKEKDRLRTERDSLKETIEELR 428
Cdd:PHA02562 358 DKAKKVKAAIEELQAEFVDNAEELAKLQ 385
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
261-428 |
1.97e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 261 LEAAKDDYRIRCEELEKEISELRQQNDeLTTLADEAQSLKDEIDVLRhssDKVSKLEGQVESYKKKLEdlgDLRRQVKLL 340
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNG-LVDLSEEAKLLLQQLSELE---SQLAEARAELAEAEARLA---ALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 341 EEKNTMYMQNTV--SLEEELRKANAARGQLET-----------YKRQVVELQNRLSDESKKA-DKLDFEYKRLKEKVDGL 406
Cdd:COG3206 253 PDALPELLQSPViqQLRAQLAELEAELAELSArytpnhpdviaLRAQIAALRAQLQQEAQRIlASLEAELEALQAREASL 332
|
170 180
....*....|....*....|..
gi 568954153 407 QKEKDRLRTERDSLKETIEELR 428
Cdd:COG3206 333 QAQLAQLEARLAELPELEAELR 354
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
193-439 |
2.11e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 193 EEIAQRCHELDMQVAALQEEKSSL---LAENQILMERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDDYR 269
Cdd:PRK02224 471 EEDRERVEELEAELEDLEEEVEEVeerLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELE 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 270 IRCEELEKEISELRQQNDE----LTTLADEAQSLKDEIDVL---RHSSDKVSKLEGQVESYKKKLEDLGDLRRQVK-LLE 341
Cdd:PRK02224 551 AEAEEKREAAAEAEEEAEEareeVAELNSKLAELKERIESLeriRTLLAAIADAEDEIERLREKREALAELNDERReRLA 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 342 EKNTMYMQNTVSLEEE-LRKANAARGQLETYKRQVVElqnrlsdeskKADKLDFEYKRLKEKVDGLQ---KEKDRLRTER 417
Cdd:PRK02224 631 EKRERKRELEAEFDEArIEEAREDKERAEEYLEQVEE----------KLDELREERDDLQAEIGAVEnelEELEELRERR 700
|
250 260
....*....|....*....|..
gi 568954153 418 DSLKETIEELRCVQAQEGQLTT 439
Cdd:PRK02224 701 EALENRVEALEALYDEAEELES 722
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
259-670 |
2.95e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 259 FRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEI--DVLRHSSDKVSKLEGQVESYKKKLED----LGD 332
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELeaQIRGNGGDRLEQLEREIERLERELEErerrRAR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 333 LRRQVKLLEekntmyMQNTVSLEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEK-- 410
Cdd:COG4913 364 LEALLAALG------LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKsn 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 411 -----DRLRTE-RDSLKETIEELR--C----VQAQE--------------------------------------GQLTTQ 440
Cdd:COG4913 438 iparlLALRDAlAEALGLDEAELPfvGelieVRPEEerwrgaiervlggfaltllvppehyaaalrwvnrlhlrGRLVYE 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 441 GLMPLGSQE-----SSDSLAAEIVT------PEIREKLIR------------LQHENK------MLKLNQE--------- 482
Cdd:COG4913 518 RVRTGLPDPerprlDPDSLAGKLDFkphpfrAWLEAELGRrfdyvcvdspeeLRRHPRaitragQVKGNGTrhekddrrr 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 483 -DSDN-------EKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKsLQDQGSKAEDAISVLLK-KKLEEH 553
Cdd:COG4913 598 iRSRYvlgfdnrAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQR-LAEYSWDEIDVASAEREiAELEAE 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 554 LEKLHEANNELQKKRAIIEDLEprfnnssLRIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQ 633
Cdd:COG4913 677 LERLDASSDDLAALEEQLEELE-------AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA 749
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 568954153 634 ALKNQLQE------RDRLFHSLEKEYEKTKSQRDMEEKYIVSA 670
Cdd:COG4913 750 LLEERFAAalgdavERELRENLEERIDALRARLNRAEEELERA 792
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
273-574 |
3.25e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.24 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 273 EELEKEISELRQQNDELTTLADEAQSLKDEIDVLRH--SSDKVSKLEGQVESYKKKLEDL-----------GDLRRQVKL 339
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNqkEQDWNKELKSELKNQEKKLEEIqnqisqnnkiiSQLNEQISQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 340 LEEKNTMYMQNTVSLEEELRKANAA-----------RGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQK 408
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEieklkkenqsyKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 409 EKDRLRTERDSLKETIEELRcVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHE-----NKMLKLNQED 483
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLT-NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKElkskeKELKKLNEEK 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 484 SD-NEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEdaisvllKKKLEEHLEKLHEANN 562
Cdd:TIGR04523 506 KElEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKE-------IDEKNKEIEELKQTQK 578
|
330
....*....|..
gi 568954153 563 ELQKKRAIIEDL 574
Cdd:TIGR04523 579 SLKKKQEEKQEL 590
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
334-428 |
3.69e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.69 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 334 RRQVKLLEEKNTMYMQNTVSLEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLK----------EKV 403
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARseerreirkdREI 467
|
90 100
....*....|....*....|....*
gi 568954153 404 DGLQKEKDRLRTERDSLKETIEELR 428
Cdd:COG2433 468 SRLDREIERLERELEEERERIEELK 492
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
174-413 |
4.19e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 174 LDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDPnspAGRRHLQLQTQLEQ 253
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE---LRAELTLLNEEAAN 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 254 LQEETFRLEAAKDDYRIRCEELEKEISELRQQndeLTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLED-LGD 332
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSED---IESLAAEIEELEELIEELESELEALLNERASLEEALALLRSeLEE 898
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 333 LRRQVKLLEEKNTMYMQNTVSLEEELRKANAARGQLETykrQVVELQNRLSDE--------SKKADKLDFEYKRLKEKVD 404
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLELRLEGLEV---RIDNLQERLSEEysltleeaEALENKIEDDEEEARRRLK 975
|
....*....
gi 568954153 405 GLQKEKDRL 413
Cdd:TIGR02168 976 RLENKIKEL 984
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
176-425 |
4.20e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.58 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 176 RQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAE---------------NQILMERLNQSDSIEDPNSPA 240
Cdd:pfam05557 58 RLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADarevisclknelselRRQIQRAELELQSTNSELEEL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 241 GRRHLQLQTQLEQLQEETFRLEAAKD---DYRIRCEELEKEIS-------ELRQQNDELTTLAD---EAQSLKDEIDVLR 307
Cdd:pfam05557 138 QERLDLLKAKASEAEQLRQNLEKQQSslaEAEQRIKELEFEIQsqeqdseIVKNSKSELARIPElekELERLREHNKHLN 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 308 HSSDKVSKLEGQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEE-------ELRKANAARGQLETY--------- 371
Cdd:pfam05557 218 ENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKlaqdtglNLRSPEDLSRRIEQLqqreivlke 297
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568954153 372 ------------KRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIE 425
Cdd:pfam05557 298 enssltssarqlEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILE 363
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
262-665 |
5.12e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 5.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 262 EAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSlKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLGdlrrqvKLLE 341
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE-ARKADELKKAEEKKKADEAKKAEEKKKADEAK------KKAE 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 342 EKNTMymqntvslEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLK 421
Cdd:PTZ00121 1313 EAKKA--------DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAK 1384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 422 ETIEELRcvQAQEGQLTTQGLMPlGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKLNQEDSDNEKIALLQSLLDDA-N 500
Cdd:PTZ00121 1385 KKAEEKK--KADEAKKKAEEDKK-KADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAeE 1461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 501 LRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDAisvllkKKLEEHLEKLHEANNELQKKRAIiedlEPRFNN 580
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEA------KKAAEAKKKADEAKKAEEAKKAD----EAKKAE 1531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 581 SSLRIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQLQERDRLFHSLEKEYEKTKSQR 660
Cdd:PTZ00121 1532 EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEE 1611
|
....*
gi 568954153 661 DMEEK 665
Cdd:PTZ00121 1612 AKKAE 1616
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
274-617 |
8.15e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.04 E-value: 8.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 274 ELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKLLEEKNtmymqNTVS 353
Cdd:pfam02463 663 EVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDK-----INEE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 354 LEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEELRCVQAQ 433
Cdd:pfam02463 738 LKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELL 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 434 EGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKLNQEDSDNEKIALLQSLLDDANLRKNELETENRLV 513
Cdd:pfam02463 818 EEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 514 NQRLLEVQSQVEELQKSLQDQGSKAEDAISVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLRIEELQEALR 593
Cdd:pfam02463 898 EKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNL 977
|
330 340
....*....|....*....|....
gi 568954153 594 KKEEEMKQMEERYKKYLEKAKSVI 617
Cdd:pfam02463 978 MAIEEFEEKEERYNKDELEKERLE 1001
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
368-662 |
8.16e-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: 42.80 E-value: 8.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 368 LETYKRQVVELQNRLSDESKKADKLDFEYKR----LKEKVDGLQKEKDRL----RTE-------RDSLKETIEELRCVQA 432
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNELHEKQKFYLRQsvidLQTKLQEMQMERDAMadirRREsqsqedlRNQLQNTVHELEAAKC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 433 QEGQLTTQGLMPLgSQESSDSLAAEIVTPEIREKLIRLQhENKMLKLNQEdsDNEKIALLQSLLDDANLRKNELETENRL 512
Cdd:pfam15921 160 LKEDMLEDSNTQI-EQLRKMMLSHEGVLQEIRSILVDFE-EASGKKIYEH--DSMSTMHFRSLGSAISKILRELDTEISY 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 513 VNQRLLEVQSQVEELQKSLQDQG----SKAEDAISVLLKKK------LEEHLEKLHEANNELQKKRAIIEDLEPRFNNSS 582
Cdd:pfam15921 236 LKGRIFPVEDQLEALKSESQNKIelllQQHQDRIEQLISEHeveitgLTEKASSARSQANSIQSQLEIIQEQARNQNSMY 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 583 LR--------IEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAP------EIQALKNQLQERDRLFhS 648
Cdd:pfam15921 316 MRqlsdlestVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQEsgnlddQLQKLLADLHKREKEL-S 394
|
330
....*....|....
gi 568954153 649 LEKEYEKTKSQRDM 662
Cdd:pfam15921 395 LEKEQNKRLWDRDT 408
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
190-428 |
9.92e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.61 E-value: 9.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 190 SAKEEIAQRCHELD-MQVAALQEEKSS-----LLAENQILMERLNQSDSIEDPNSpagrrhlqlQTQLEQLQEETFRLEA 263
Cdd:PRK05771 16 SYKDEVLEALHELGvVHIEDLKEELSNerlrkLRSLLTKLSEALDKLRSYLPKLN---------PLREEKKKVSVKSLEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 264 AKDDYRIRCEELEKEISELrqqNDELTTLADEAQSLKDEIDVLrhssdkvsklegqvesykKKLEDLG-DLRRqvkLLEE 342
Cdd:PRK05771 87 LIKDVEEELEKIEKEIKEL---EEEISELENEIKELEQEIERL------------------EPWGNFDlDLSL---LLGF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 343 KNTMYMQNTVSLE-EELRKANAARGQLETYKRQ-------VVELQNRLSDESKKADKLDF------EYKRLKEKVDGLQK 408
Cdd:PRK05771 143 KYVSVFVGTVPEDkLEELKLESDVENVEYISTDkgyvyvvVVVLKELSDEVEEELKKLGFerleleEEGTPSELIREIKE 222
|
250 260
....*....|....*....|
gi 568954153 409 EKDRLRTERDSLKETIEELR 428
Cdd:PRK05771 223 ELEEIEKERESLLEELKELA 242
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
273-667 |
1.04e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 273 EELEKEI----SELRQQNDELTTLADeaqSLKDEIDVLRHSSDKVSKLEGQVESYKKKLED----LGDLRRQVKLLEEKN 344
Cdd:TIGR04523 36 KQLEKKLktikNELKNKEKELKNLDK---NLNKDEEKINNSNNKIKILEQQIKDLNDKLKKnkdkINKLNSDLSKINSEI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 345 TMYMQNTVSLEEELRKAnaaRGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKETI 424
Cdd:TIGR04523 113 KNDKEQKNKLEVELNKL---EKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 425 EELRcvqAQEGQLTTQGLMPLGSQESSDSLAAEIVtpeirekliRLQHENKMLKlNQEDSDNEKIALLQSLLDDANLRKN 504
Cdd:TIGR04523 190 DKIK---NKLLKLELLLSNLKKKIQKNKSLESQIS---------ELKKQNNQLK-DNIEKKQQEINEKTTEISNTQTQLN 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 505 ELETENRLVNQRLLEVQSQVEE---LQKSLQDQGSKAEDAISVLLKKKLEEHLEKLHEannELQKKRAIIEDLEPRFNNS 581
Cdd:TIGR04523 257 QLKDEQNKIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISDLNNQKEQDWNKELKS---ELKNQEKKLEEIQNQISQN 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 582 SLRIEELQEA---LRKKEEEMKQMEERYKKYLEKAKSVIRTLDpKQNQGAAPEIQALKNQLQERDRLF------------ 646
Cdd:TIGR04523 334 NKIISQLNEQisqLKKELTNSESENSEKQRELEEKQNEIEKLK-KENQSYKQEIKNLESQINDLESKIqnqeklnqqkde 412
|
410 420 430
....*....|....*....|....*....|
gi 568954153 647 ---------HSLEKEYEKTKSQRDMEEKYI 667
Cdd:TIGR04523 413 qikklqqekELLEKEIERLKETIIKNNSEI 442
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
173-579 |
1.13e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 173 DLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQ---------------SDSIEDPN 237
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEkqneieklkkenqsyKQEIKNLE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 238 SPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSD----KV 313
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTREsletQL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 314 SKLEGQVESYKKKLED-----------LGDLRRQVKLLEEKNTMYMQNTVSLEEELRKANAARGQLEtykrqvvelqNRL 382
Cdd:TIGR04523 471 KVLSRSINKIKQNLEQkqkelkskekeLKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKE----------SKI 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 383 SDESKKADKLDFEYKR--LKEKVDGLQKEKDRLRTERDSLKETIEELrcvqaqegqlttqglmplgsQESSDSLAAEI-- 458
Cdd:TIGR04523 541 SDLEDELNKDDFELKKenLEKEIDEKNKEIEELKQTQKSLKKKQEEK--------------------QELIDQKEKEKkd 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 459 VTPEIREKLIRLQHENKMLKLNQEDsdNEKialLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKA 538
Cdd:TIGR04523 601 LIKEIEEKEKKISSLEKELEKAKKE--NEK---LSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKI 675
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568954153 539 EDAISVLLK----------------------KKLEEHLEKLHEANNELQKKRAIIEDLEPRFN 579
Cdd:TIGR04523 676 DDIIELMKDwlkelslhykkyitrmirikdlPKLEEKYKEIEKELKKLDEFSKELENIIKNFN 738
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
260-531 |
1.14e-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: 42.52 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 260 RLEAAKDDYRIRCEELEKEISELRQQ-NDELTTLADEAQSLKDEIDVLrhSSDKVSKLEGQVESYKKKLEDLGDLRRQVK 338
Cdd:pfam12128 280 ERQETSAELNQLLRTLDDQWKEKRDElNGELSAADAAVAKDRSELEAL--EDQHGAFLDADIETAAADQEQLPSWQSELE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 339 LLEEKNTMYMQNTVSLEEELRKANAARGQletykrqvvelqnrlsdeskkadkldfeykRLKEKVDGLQKEKDRLRTERD 418
Cdd:pfam12128 358 NLEERLKALTGKHQDVTAKYNRRRSKIKE------------------------------QNNRDIAGIKDKLAKIREARD 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 419 SLKETIEELrcVQAQEGQLTTQ---GLMPLGSQESSDSLAAE-----IVTPEIREKLIrLQHENKMLKLNQEDSDNEK-- 488
Cdd:pfam12128 408 RQLAVAEDD--LQALESELREQleaGKLEFNEEEYRLKSRLGelklrLNQATATPELL-LQLENFDERIERAREEQEAan 484
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 568954153 489 --IALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSL 531
Cdd:pfam12128 485 aeVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQL 529
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
488-665 |
1.94e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 488 KIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDaisvlLKKKLEEHLEKLHEANNELQKK 567
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE-----LELELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 568 RAIIEDLEPRFNNSSLRIEELQEALRKKEEEMKQMEERykkyLEKAKSVIRTLDPKQNQGAApEIQALKNQLQERDRLFH 647
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEE----LEELEEELEEAEEELEEAEA-ELAEAEEALLEAEAELA 375
|
170
....*....|....*...
gi 568954153 648 SLEKEYEKTKSQRDMEEK 665
Cdd:COG1196 376 EAEEELEELAEELLEALR 393
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
311-423 |
2.01e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 311 DKVSKLEGQVESYKKKLEDLGDLRRQvklLEEKNTMYMQNTVSLEEELRKANAARGQLETYKRQV-------VELQNRLS 383
Cdd:PHA02562 299 DRITKIKDKLKELQHSLEKLDTAIDE---LEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAkkvkaaiEELQAEFV 375
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 568954153 384 DESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKET 423
Cdd:PHA02562 376 DNAEELAKLQDELDKIVKTKSELVKEKYHRGIVTDLLKDS 415
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
271-674 |
2.11e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 271 RCEELEKEISELRQQNDELTTLADE---AQSLKDEIDVLRHSSDKVSKLE--GQVESYKKKLEDLGDLRRQVKLLEEKNT 345
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKAAAAkkkADEAKKKAEEKKKADEAKKKAEeaKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 346 MymQNTVSLEEELRKANAARGQLETYKRQVVELQN-----------RLSDESKKADKLdfEYKRLKEKVDGLQKEKDRLR 414
Cdd:PTZ00121 1472 A--DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKaaeakkkadeaKKAEEAKKADEA--KKAEEAKKADEAKKAEEKKK 1547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 415 TERDSLKETIEELRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKLNQEDSDNEKIALLQS 494
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK 1627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 495 LLDD----ANLRKNELETENRLVNQRLLEVQSQV--EELQKSLQDQGSKAEDAisvllkKKLEEHLEKLHEANNELQKKR 568
Cdd:PTZ00121 1628 AEEEkkkvEQLKKKEAEEKKKAEELKKAEEENKIkaAEEAKKAEEDKKKAEEA------KKAEEDEKKAAEALKKEAEEA 1701
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 569 AIIEDLEPRFNNSSLRIEELQ----------EALRKKEEEMKQMEERYKKYLEKAKSVIRTldPKQNQGAAPEIQALKNQ 638
Cdd:PTZ00121 1702 KKAEELKKKEAEEKKKAEELKkaeeenkikaEEAKKEAEEDKKKAEEAKKDEEEKKKIAHL--KKEEEKKAEEIRKEKEA 1779
|
410 420 430
....*....|....*....|....*....|....*.
gi 568954153 639 LQERDrlfhsLEKEYEKTKSQRDMEEKYIVSAWYNM 674
Cdd:PTZ00121 1780 VIEEE-----LDEEDEKRRMEVDKKIKDIFDNFANI 1810
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
261-593 |
2.12e-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: 41.75 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 261 LEAAKDDYRIRCEELEKEISELRQQNDELTT-LADEAQSLKDEIDVLR-----HSSDKVSKLEGQVESYKKKLEDLGDLR 334
Cdd:pfam12128 609 AEEALQSAREKQAAAEEQLVQANGELEKASReETFARTALKNARLDLRrlfdeKQSEKDKKNKALAERKDSANERLNSLE 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 335 RQVKLLEEKNTMYmqntvsLEEELRKANAARGQLETYKRQVVELQNRLSDESKKAdkLDFEYKRLKEKVDGLQKEKDR-- 412
Cdd:pfam12128 689 AQLKQLDKKHQAW------LEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAA--IAARRSGAKAELKALETWYKRdl 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 413 ------------LRTERDSLKETIEELrcvqAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHEnkmLKLN 480
Cdd:pfam12128 761 aslgvdpdviakLKREIRTLERKIERI----AVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQ---LARL 833
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 481 QEDS--DNEKIALLQSLLDDANLRKNELETENRLVNQRL--LEVQSQVEELQKSLQDQGSKAEDAISVL------LKKKL 550
Cdd:pfam12128 834 IADTklRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLatLKEDANSEQAQGSIGERLAQLEDLKLKRdylsesVKKYV 913
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568954153 551 E---------------EHLEKLHEANNELQKKRAIIED-------LEPRFNnssLRIEELQEALR 593
Cdd:pfam12128 914 EhfknviadhsgsglaETWESLREEDHYQNDKGIRLLDyrklvpyLEQWFD---VRVPQSIMVLR 975
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
169-428 |
2.30e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 169 DAYVDLDRQLKKTTEELnEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENqilmerlnqsdsiedpnspAGRRHLQLQ 248
Cdd:COG4913 235 DDLERAHEALEDAREQI-ELLEPIRELAERYAAARERLAELEYLRAALRLWF-------------------AQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 249 TQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTlaDEAQSLKDEIDVLRhssDKVSKLEGQVESYKKKLE 328
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGG--DRLEQLEREIERLE---RELEERERRRARLEALLA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 329 DLGdlrrqvklleekntmyMQNTVSLEEELRKANAARGQLETYKRQVVELQNRLsdeskkaDKLDFEYKRLKEKVDGLQK 408
Cdd:COG4913 370 ALG----------------LPLPASAEEFAALRAEAAALLEALEEELEALEEAL-------AEAEAALRDLRRELRELEA 426
|
250 260
....*....|....*....|
gi 568954153 409 EKDRLRTERDSLKETIEELR 428
Cdd:COG4913 427 EIASLERRKSNIPARLLALR 446
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
270-428 |
2.43e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 270 IRCEELEKEISELRQ--QNDELTTLADEAQSLKDEIDVLRhssDKVSKLEGQVESYKKKLEDLgdlRRQVKLLEEKNTMy 347
Cdd:COG2433 373 IRGLSIEEALEELIEkeLPEEEPEAEREKEHEERELTEEE---EEIRRLEEQVERLEAEVEEL---EAELEEKDERIER- 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 348 mqntvsLEEELRKAnaargqletykrqvvelqnrlSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEEL 427
Cdd:COG2433 446 ------LERELSEA---------------------RSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLERL 498
|
.
gi 568954153 428 R 428
Cdd:COG2433 499 K 499
|
|
| Taf7 |
COG5414 |
TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation ... |
387-575 |
2.70e-03 |
|
TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation complex [Transcription];
Pssm-ID: 227701 Cd Length: 392 Bit Score: 40.84 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 387 KKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEE------LRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVT 460
Cdd:COG5414 207 KKVDDLLEKDMKAESVSVVLKDEKELARQERVSSWENFKEepgeplSRPALKKEKQGAEEEGEEGMSEEDLDVGAAEIEN 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 461 PEIREKLIRLQHENKMlklNQEDSDNEKiallQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAED 540
Cdd:COG5414 287 KEVSEGDKEQQQEEVE---NAEAHKEEV----QSDRPDEIGEEKEEDDENEENERHTELLADELNELEKGIEEKRRQMES 359
|
170 180 190
....*....|....*....|....*....|....*
gi 568954153 541 AISVLLKKKLEEHLEKLHEannELQKKRAIIEDLE 575
Cdd:COG5414 360 ATNPILQKRFESQLNVLLK---ELELKRKQLEMEE 391
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
169-428 |
2.78e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 169 DAYVDLDRQLKKTTEELNEALSAKEEIAQrchELDMQVAALQEEKSSLLAENQILM-ERLNQSDSIEDPNSPAGRRHLQL 247
Cdd:TIGR04523 380 QSYKQEIKNLESQINDLESKIQNQEKLNQ---QKDEQIKKLQQEKELLEKEIERLKeTIIKNNSEIKDLTNQDSVKELII 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 248 QTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKL 327
Cdd:TIGR04523 457 KNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEK 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 328 ED-LGDLRRQVK---------LLEEKNTMYMQNTVSLEEELRKANAARGQLET----YKRQVVELQNRLSDESKKADKLD 393
Cdd:TIGR04523 537 ESkISDLEDELNkddfelkkeNLEKEIDEKNKEIEELKQTQKSLKKKQEEKQElidqKEKEKKDLIKEIEEKEKKISSLE 616
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 568954153 394 -------FEYKRLKEKVDGLQKEKDRLRTERDSLKETIEELR 428
Cdd:TIGR04523 617 kelekakKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIR 658
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
501-665 |
3.34e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.81 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 501 LRKNELETENRLVN-----QRLLEVQSQVEELQKSLQDQGSKAEDAISV----------LLKKKLEEHLEKLHEANNELQ 565
Cdd:TIGR02168 170 YKERRKETERKLERtrenlDRLEDILNELERQLKSLERQAEKAERYKELkaelrelelaLLVLRLEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 566 KKRAIIEDLEPRFNNSSLRIEELQEALRKKEEEMKQMEERY----------KKYLEKAKSVIRTLDPKQNQGAApEIQAL 635
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELyalaneisrlEQQKQILRERLANLERQLEELEA-QLEEL 328
|
170 180 190
....*....|....*....|....*....|
gi 568954153 636 KNQLQERDRLFHSLEKEYEKTKSQRDMEEK 665
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEA 358
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
266-376 |
3.34e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.84 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 266 DDYRIRCEELEKEISELRQQNDELTtlADEAQSLKDEIDVLRhssDKVSKLEGQVESYKKKLEDLGDLRRQvklLEEKNt 345
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEQDEAS--FERLAELRDELAELE---EELEALKARWEAEKELIEEIQELKEE---LEQRY- 484
|
90 100 110
....*....|....*....|....*....|.
gi 568954153 346 mymQNTVSLEEELRKANAARGQLETYKRQVV 376
Cdd:COG0542 485 ---GKIPELEKELAELEEELAELAPLLREEV 512
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
393-593 |
4.11e-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: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 393 DFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEEL-RCVQAQEGQLTTqglmplgSQESSDSLAAEIVtpEIREKLIRLQ 471
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELnEEYNELQAELEA-------LQAEIDKLQAEIA--EAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 472 HE-NKMLKLNQEDSDNEKI--ALLQS-----LLDDANLRKNELETENRLVNQrLLEVQSQVEELQKSLQDQGSKAEDais 543
Cdd:COG3883 86 EElGERARALYRSGGSVSYldVLLGSesfsdFLDRLSALSKIADADADLLEE-LKADKAELEAKKAELEAKLAELEA--- 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568954153 544 vlLKKKLEEHLEklhEANNELQKKRAIIEDLEPRFNNSSLRIEELQEALR 593
Cdd:COG3883 162 --LKAELEAAKA---ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
360-639 |
4.17e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 360 KANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEELrcvQAQEGQLtt 439
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL---EKEIAEL-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 440 qglmplgsqessdslaaeivtpeiREKLIRLQHE-NKMLKLNQEDSDNEKIALL--QSLLDDANLRKNELETENRLVNQR 516
Cdd:COG4942 96 ------------------------RAELEAQKEElAELLRALYRLGRQPPLALLlsPEDFLDAVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 517 LLEVQSQVEELQKslqdqgskaedaisvlLKKKLEEHLEKLHEANNELQKKRAIIEDLEprfNNSSLRIEELQEALRKKE 596
Cdd:COG4942 152 AEELRADLAELAA----------------LRAELEAERAELEALLAELEEERAALEALK---AERQKLLARLEKELAELA 212
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 568954153 597 EEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQL 639
Cdd:COG4942 213 AELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
182-441 |
4.17e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 182 TEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQsdsiedpnspagrrhlqlqtqleqlqeetfrL 261
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA-------------------------------L 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 262 EAAKDDYRIRCEELEKEISELRQQNDELTT-LADEAQSLKDEIDVL-RHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKL 339
Cdd:COG4942 68 ARRIRALEQELAALEAELAELEKEIAELRAeLEAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 340 LEEKNTMYMQNTVSLEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLdfeYKRLKEKVDGLQKEKDRLRTERDS 419
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL---LARLEKELAELAAELAELQQEAEE 224
|
250 260
....*....|....*....|..
gi 568954153 420 LKETIEELRCVQAQEGQLTTQG 441
Cdd:COG4942 225 LEALIARLEAEAAAAAERTPAA 246
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
260-437 |
5.31e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.10 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 260 RLEAAKDdyrIRcEELEKEISELRQQNDELTTLADEAQSLKDEidvLRHSSDKV----SKLEGQVESYKKKLEDLgdlRR 335
Cdd:pfam15921 644 RLRAVKD---IK-QERDQLLNEVKTSRNELNSLSEDYEVLKRN---FRNKSEEMetttNKLKMQLKSAQSELEQT---RN 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 336 QVKLLEEKNTMYMQNTVSLEEELrkaNAARGQLETYKRQVVELQNRLSDESKkadkldfEYKRLKEKVDGLQKEKDRLRT 415
Cdd:pfam15921 714 TLKSMEGSDGHAMKVAMGMQKQI---TAKRGQIDALQSKIQFLEEAMTNANK-------EKHFLKEEKNKLSQELSTVAT 783
|
170 180
....*....|....*....|..
gi 568954153 416 ERDSLKETIEELRcvqAQEGQL 437
Cdd:pfam15921 784 EKNKMAGELEVLR---SQERRL 802
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
260-574 |
6.14e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.16 E-value: 6.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 260 RLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDK-VSKLEGQV--------ESYKKKLEDL 330
Cdd:pfam01576 409 KLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKdVSSLESQLqdtqellqEETRQKLNLS 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 331 GDLRrqvKLLEEKNTMYMQntvsLEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQK-- 408
Cdd:pfam01576 489 TRLR---QLEDERNSLQEQ----LEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQql 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 409 -----EKDRLRTERDSLKETIEELRCVQAQEGQLTT---------------QGLMPLGSQESSDSLAAEIVTPEIR---- 464
Cdd:pfam01576 562 eekaaAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSnlekkqkkfdqmlaeEKAISARYAEERDRAEAEAREKETRalsl 641
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 465 --------EKLIRLQHENKMLKLNQEDsdnekialLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQdqgs 536
Cdd:pfam01576 642 araleealEAKEELERTNKQLRAEMED--------LVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQ---- 709
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 568954153 537 KAEDAISVL------LKKKLEEHLEKLHEANNElqKKRAIIEDL 574
Cdd:pfam01576 710 ATEDAKLRLevnmqaLKAQFERDLQARDEQGEE--KRRQLVKQV 751
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
129-655 |
7.85e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.57 E-value: 7.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 129 CEQKQEYIQAIMMMEESVQHVVMTAIQELMSKESPVSAGHDAYVDLDRQLKKTTEELNEALSAKEEIAQRcHELDMQVAA 208
Cdd:TIGR00618 305 IEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQ-HTLTQHIHT 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 209 LQEEKSSLLAENQILMERLNQSDSIEDPNSPagrRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDE 288
Cdd:TIGR00618 384 LQQQKTTLTQKLQSLCKELDILQREQATIDT---RTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIH 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 289 LTTLAdeaQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVK-------------LLEEKNTMYMQNTVSLE 355
Cdd:TIGR00618 461 LQESA---QSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCgscihpnparqdiDNPGPLTRRMQRGEQTY 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 356 EELRKANA-ARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEELRC----- 429
Cdd:TIGR00618 538 AQLETSEEdVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACeqhal 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 430 -VQAQEGQLTTQGLMPLGSQESSDSLA--------AEIVTPEIREKLIRLqhenKMLKLNQEDSDNEKIALLQSLLDDAN 500
Cdd:TIGR00618 618 lRKLQPEQDLQDVRLHLQQCSQELALKltalhalqLTLTQERVREHALSI----RVLPKELLASRQLALQKMQSEKEQLT 693
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 501 LRKNELETEN---RLVNQRLLEVQSQVEELQKSLQDQGSK---AEDAISVLLKKKLEEHLEKLHEANNELQKKRAIIEDL 574
Cdd:TIGR00618 694 YWKEMLAQCQtllRELETHIEEYDREFNEIENASSSLGSDlaaREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAA 773
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 575 EPRFNNSSLRIEELQEALRKKEEEMKQMEERYKKYLEKAKS--VIRTLDPKQNQGaapEIQALKNQLQERDRLFHSLEKE 652
Cdd:TIGR00618 774 LQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSdeDILNLQCETLVQ---EEEQFLSRLEEKSATLGEITHQ 850
|
...
gi 568954153 653 YEK 655
Cdd:TIGR00618 851 LLK 853
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
173-599 |
7.92e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 7.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 173 DLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQilMERLNQsDSIEDPNSPAGRRHLQLQTQLE 252
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG--LDDADA-EAVEARREELEDRDEELRDRLE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 253 QLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQS-----------LKDEIDVLRHSSDKVSKLEGQVE 321
Cdd:PRK02224 332 ECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREavedrreeieeLEEEIEELRERFGDAPVDLGNAE 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 322 SYKKKL-EDLGDLRRQVKLLEEKntmymqnTVSLEEELRKANAAR--------GQ----------LETYKRQVVELQNRL 382
Cdd:PRK02224 412 DFLEELrEERDELREREAELEAT-------LRTARERVEEAEALLeagkcpecGQpvegsphvetIEEDRERVEELEAEL 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 383 SDESKKADKLDFEYKRLKEKVDgLQKEKDRLRTERDSLKETIEELRC-VQAQEGQLTT-----QGLMPLGSQESSDSLAA 456
Cdd:PRK02224 485 EDLEEEVEEVEERLERAEDLVE-AEDRIERLEERREDLEELIAERREtIEEKRERAEElreraAELEAEAEEKREAAAEA 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 457 EIVTPEIREKLIRLqhENKMLKLNQEDSDNEKIALLQSLLDDA-------NLRKNELETENRLVNQRLLEVQSQVEELQK 529
Cdd:PRK02224 564 EEEAEEAREEVAEL--NSKLAELKERIESLERIRTLLAAIADAedeierlREKREALAELNDERRERLAEKRERKRELEA 641
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 530 SLQDqgSKAEDAISVllKKKLEEHLEKLHEANNELQKKRaiiedleprfnnsslriEELQEALRKKEEEM 599
Cdd:PRK02224 642 EFDE--ARIEEARED--KERAEEYLEQVEEKLDELREER-----------------DDLQAEIGAVENEL 690
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
462-659 |
8.01e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.36 E-value: 8.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 462 EIREKLIRLQHENKMLKlNQEDSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDA 541
Cdd:COG4942 31 QLQQEIAELEKELAALK-KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 542 ISVLLKKKLEEHLEKLHEANNELQKKR--AIIEDLEPRFNNsslRIEELQEALRKKEEEmkqmeeryKKYLEKAKSVIRT 619
Cdd:COG4942 110 LRALYRLGRQPPLALLLSPEDFLDAVRrlQYLKYLAPARRE---QAEELRADLAELAAL--------RAELEAERAELEA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568954153 620 LDPKQNQgaapEIQALKNQLQERDRLFHSLEKEYEKTKSQ 659
Cdd:COG4942 179 LLAELEE----ERAALEALKAERQKLLARLEKELAELAAE 214
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
273-666 |
8.72e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 39.64 E-value: 8.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 273 EELEKEISELRQQNDELTTLADEAQSLKD----EIDVLRHSSDKVSKLEGQVESykkkledlgDLRRQVKLLEekntmym 348
Cdd:TIGR00606 712 KSTESELKKKEKRRDEMLGLAPGRQSIIDlkekEIPELRNKLQKVNRDIQRLKN---------DIEEQETLLG------- 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 349 qnTVSLEEELRKA-NAARGQLETYKRQVVELQNRLSDESKKADKLDFE--YKRLKEKVDGLQKEKDRLRTERDSLKETIE 425
Cdd:TIGR00606 776 --TIMPEEESAKVcLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDrtVQQVNQEKQEKQHELDTVVSKIELNRKLIQ 853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 426 ElrcvQAQEGQLTTQGLMPLGSQESSDSLAAEiVTPEIREKLIRLQHENKMLKLNQEDSDNEKIALLQSLLDDANlRKNE 505
Cdd:TIGR00606 854 D----QQEQIQHLKSKTNELKSEKLQIGTNLQ-RRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQ-EKEE 927
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 506 L----ETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDAISVLLKKKlEEHLEKLHEANNELQKKRAIIED----LEPR 577
Cdd:TIGR00606 928 LisskETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQK-ETELNTVNAQLEECEKHQEKINEdmrlMRQD 1006
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 578 FNNSSLRIEELQEAL--RKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQlqerDRLFHSLEKEYEK 655
Cdd:TIGR00606 1007 IDTQKIQERWLQDNLtlRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRN----HVLALGRQKGYEK 1082
|
410 420
....*....|....*....|.
gi 568954153 656 ----------TKSQRDMEEKY 666
Cdd:TIGR00606 1083 eikhfkkelrEPQFRDAEEKY 1103
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
265-665 |
9.49e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 39.64 E-value: 9.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 265 KDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKledlgdlRRQVKLLEEKN 344
Cdd:TIGR00606 590 RDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKS-------SKQRAMLAGAT 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 345 TMYMQNTVSLEEELRKANAARGQLETYKRQVVE----LQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSL 420
Cdd:TIGR00606 663 AVYSQFITQLTDENQSCCPVCQRVFQTEAELQEfisdLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLK 742
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 421 KETIEELRcvqaQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKLNQEDSDNE-KIALLQSLLD-- 497
Cdd:TIGR00606 743 EKEIPELR----NKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVErKIAQQAAKLQgs 818
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 498 DANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQgskaEDAISVLLKKKLEEHLEKLHEANNeLQKKRAIIEDLEPR 577
Cdd:TIGR00606 819 DLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQ----QEQIQHLKSKTNELKSEKLQIGTN-LQRRQQFEEQLVEL 893
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954153 578 fnnsSLRIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDpKQNQGAAPEIQALKNQLQERDRLFHSLEKEYEKTK 657
Cdd:TIGR00606 894 ----STEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKE-TSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGK 968
|
....*...
gi 568954153 658 SQRDMEEK 665
Cdd:TIGR00606 969 DDYLKQKE 976
|
|
| |
