|
Name |
Accession |
Description |
Interval |
E-value |
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
184-705 |
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: 652.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 184 ELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQEETFRLEA 263
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 264 AKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSLKDEMDVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQVKLLEEK 343
Cdd:pfam05622 81 ARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLGDLRRQVKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 344 NTMYMQNTVSLEEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKET 423
Cdd:pfam05622 161 NAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRET 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 424 IEELRCVQAQEGQLtTSAGLMPLGSQESSDSLAAEIVTPEIKEKLIRLQHENKMLKLNQEGSDNEKIALLQSLLDDANLR 503
Cdd:pfam05622 241 NEELRCAQLQQAEL-SQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLGQEGSYRERLTELQQLLEDANRR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 504 KNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDaiSVLLKKKLEEHLEKLHEANNEIQRKRAIIEDLEPRYN-NS 582
Cdd:pfam05622 320 KNELETQNRLANQRILELQQQVEELQKALQEQGSKAED--SSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDsNL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 583 SLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGTAPEIQALKNQLQERDRMFHSLEKEYEKTKTQRE 662
Cdd:pfam05622 398 AQKIDELQEALRKKDEDMKAMEERYKKYVEKAKSVIKTLDPKQNPASPPEIQALKNQLLEKDKKIEHLERDFEKSKLQRE 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1729156922 663 MEEKFI-------GMTLHKKAAEDRLASTGS-GQSFLARQRQATNTRRSYP 705
Cdd:pfam05622 478 QEEKLIvtawynmGMALHRKAIEERLAGLSSpGQSFLARQRQATNARRGLS 528
|
|
| HkD_Hook3 |
cd22226 |
Hook domain found in protein Hook 3 (Hook3) and similar proteins; Hook3 is an adaptor protein ... |
8-160 |
4.58e-102 |
|
Hook domain found in protein Hook 3 (Hook3) and similar proteins; Hook3 is an adaptor protein for microtubule-dependent intracellular vesicle and protein trafficking. It is involved in Golgi and endosome transport. It acts as a scaffold for the opposite-polarity microtubule-based motors cytoplasmic dynein-1 and the kinesin KIF1C. It may participate in the turnover of the endocytosed scavenger receptor. Hook3 is a component of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex.
Pssm-ID: 411797 Cd Length: 153 Bit Score: 309.98 E-value: 4.58e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 8 ERAELGESLLTWIQTFNVEAPCQTVEDLTNGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYN 87
Cdd:cd22226 1 DRAELCESLLTWIQTFNVDAPCQTVEDLTSGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1729156922 88 HEILGQQINDFTLPDVNLIGEHSDVAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMSK 160
Cdd:cd22226 81 HEILGQQINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMSK 153
|
|
| HOOK_N |
pfam19047 |
HOOK domain; This domain is found at the N-terminus of HOOK proteins. |
11-161 |
1.94e-94 |
|
HOOK domain; This domain is found at the N-terminus of HOOK proteins.
Pssm-ID: 465958 Cd Length: 151 Bit Score: 290.08 E-value: 1.94e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 11 ELGESLLTWIQTFNVEAPCQTVEDLTNGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEI 90
Cdd:pfam19047 1 ELCDSLLTWLQTFNVPAPCATVEDLTDGVAMAQVLHQIDPSWFTEAWLSRIKEDVGDNWRLKVSNLKKILQSVVDYYQDV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1729156922 91 LGQQINDFTLPDVNLIGEHSDVAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMSKE 161
Cdd:pfam19047 81 LGQQISDFLLPDVNLIGEHSDPAELGRLLQLILGCAVNCEKKQEYIQQIMTLEESVQHVVMTAIQELMSKD 151
|
|
| HkD_Hook |
cd22222 |
Hook domain found in Hook family of microtubule-binding proteins; The Hook family includes ... |
14-159 |
5.41e-90 |
|
Hook domain found in Hook family of microtubule-binding proteins; The Hook family includes Hook1-3. Hook1 is a microtubule-binding protein required for spermatid differentiation. Hook2, also a microtubule-binding protein, contributes to the establishment and maintenance of centrosome function. It may function in the positioning or formation of aggresomes, which are pericentriolar accumulations of misfolded proteins, proteasomes and chaperones. Hook3 is an adaptor protein for microtubule-dependent intracellular vesicle and protein trafficking. It is involved in Golgi and endosome transport. It acts as a scaffold for the opposite-polarity microtubule-based motors cytoplasmic dynein-1 and the kinesin KIF1C. It may participate in the turnover of the endocytosed scavenger receptor. Hook proteins are components of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex. Hook adaptor proteins share an N-terminal conserved globular Hook domain, which folds as a variant of the helical calponin homology (CH) domain, and contacts the helix alpha1 of dynein light intermediate chain 1 (LIC1) in a hydrophobic groove.
Pssm-ID: 411793 Cd Length: 147 Bit Score: 278.36 E-value: 5.41e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 14 ESLLTWIQTFNVEAPCQTVEDLTNGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEILGQ 93
Cdd:cd22222 2 DSLLQWLQTFNLIAPHATAEDLSDGVAIAQVLNQIDPEYFSDSWLSKIKPDVGDNWRLKVSNLKKILKGIVDYYSEVLGQ 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1729156922 94 QINDFTLPDVNLIGEHSDVAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMS 159
Cdd:cd22222 82 QISGFTMPDVNAIAEKEDPKELGRLLQLVLGCAVNCERKEEYIQAIMGLEESVQHVVMEAIQELMS 147
|
|
| HkD_Hook1 |
cd22225 |
Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a ... |
12-161 |
1.33e-80 |
|
Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a microtubule-binding protein required for spermatid differentiation. It is a component of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex.
Pssm-ID: 411796 Cd Length: 150 Bit Score: 254.00 E-value: 1.33e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 12 LGESLLTWIQTFNVEAPCQTVEDLTNGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEIL 91
Cdd:cd22225 1 LCDSLIIWLQTFNTAAPCQTVQDLTSGVAMAQVLHQIDSSWFDESWLSRIKEDVGDNWRIKMSNLKKILQGIVDYYHEFL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 92 GQQINDFTLPDVNLIGEHSDVAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMSKE 161
Cdd:cd22225 81 DQQISEFLLPDLNRIAEHSDPVELGRLLQLILGCAVNCEKKQEHIQNIMTLEESVQHVVMTAIQELMSKE 150
|
|
| HkD_Hook2 |
cd22227 |
Hook domain found in protein Hook 2 (Hook2) and similar proteins; Hook2 is a ... |
11-160 |
1.15e-70 |
|
Hook domain found in protein Hook 2 (Hook2) and similar proteins; Hook2 is a microtubule-binding protein that contributes to the establishment and maintenance of centrosome function. It may function in the positioning or formation of aggresomes, which are pericentriolar accumulations of misfolded proteins, proteasomes and chaperones. Hook2 is a component of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex.
Pssm-ID: 411798 Cd Length: 150 Bit Score: 227.84 E-value: 1.15e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 11 ELGESLLTWIQTFNVEAPCQTVEDLTNGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEI 90
Cdd:cd22227 1 ELCDSLLTWLQTFQVPSPCSSYQDLTSGVAIAQVLNRIDPSWFNEAWLGRIKEDTGDNWRLKVSNLKKILQSLLEYYQDV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 91 LGQQINDFTLPDVNLIGEHSDVAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMSK 160
Cdd:cd22227 81 LGHQVSEDHLPDVNLIGEFSDDTELGKLLQLVLGCAISCEKKQEHIQQIMTLEESVQHVVMEAIQELLTK 150
|
|
| HkD_SF |
cd22211 |
Hook domain-containing proteins superfamily; The Hook domain superfamily includes Hook adaptor ... |
13-159 |
5.91e-54 |
|
Hook domain-containing proteins superfamily; The Hook domain superfamily includes Hook adaptor proteins, Hook-related proteins and nuclear mitotic apparatus protein (NuMA). They share an N-terminal conserved globular Hook domain, which folds as a variant of the helical calponin homology (CH) domain with an extended alpha-helix. The Hook domain is responsible for the binding of microtubule. The Hook family includes microtubule-binding proteins, Hook1-3. Hook1 is required for spermatid differentiation. Hook2 contributes to the establishment and maintenance of centrosome function. Hook3 is an adaptor protein for microtubule-dependent intracellular vesicle and protein trafficking, and is involved in Golgi and endosome transport. Hook proteins are components of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex. The Hook-related protein (HkRP) family includes Daple, Girdin and Gipie. Daple, also called Dvl-associating protein with a high frequency of leucine residues, or coiled-coil domain-containing protein 88C(CCDC88C), or Hook-related protein 2 (HkRP2), is a novel non-receptor nucleotide exchange factor (GEF) required for activation of guanine nucleotide-binding proteins (G-proteins) during non-canonical Wnt signaling. Girdin, also called Akt phosphorylation enhancer (APE), or coiled-coil domain-containing protein 88A (CCDC88A), or G alpha-interacting vesicle-associated protein (GIV), or Girders of actin filament, or Hook-related protein 1 (HkRP1), is a bifunctional modulator of guanine nucleotide-binding proteins (G proteins). Gipie, also called GRP78-interacting protein induced by ER stress, or coiled-coil domain-containing protein 88B(CCDC88B), or brain leucine zipper domain-containing protein, or Hook-related protein 3 (HkRP3), is a novel actin cytoskeleton-binding protein and Akt substrate that regulates cell migratory responses in various biological contexts. NuMA, also called nuclear mitotic apparatus protein 1, or nuclear matrix protein-22 (NMP-22), or SP-H antigen, is a microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignment and the segregation of chromosomes during mitotic cell division.
Pssm-ID: 411792 Cd Length: 145 Bit Score: 182.48 E-value: 5.91e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 13 GESLLTWIQTFNVEAPCQTVEDLTNGVVMAQVLQKIDPAYFDENWLNriKTEVGDNWRLKISNLKKILKGILDYNHEILG 92
Cdd:cd22211 1 EAALLAWINTFPLSSPVESLDDLSDGVVLAEILSQIDPSYFDSEWLE--SRDSSDNWVLKLNNLKKLYRSLSKYYREVLG 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1729156922 93 QQINDFTLPDVNLIGEHSDVAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMS 159
Cdd:cd22211 79 QQLSDLPLPDLSAIARDGDEEEIVKLLELVLGAAVQCENKEEYIARIQQLDESTQAELMLIIQEVLE 145
|
|
| HkD_HkRP |
cd22223 |
Hook domain found in the Hook-related protein (HkRP) family; The HkRP family includes Daple, ... |
15-157 |
3.38e-25 |
|
Hook domain found in the Hook-related protein (HkRP) family; The HkRP family includes Daple, Girdin and Gipie. Daple, also called Dvl-associating protein with a high frequency of leucine residues, or coiled-coil domain-containing protein 88C (CCDC88C), or Hook-related protein 2 (HkRP2), is a novel non-receptor nucleotide exchange factor (GEF) required for activation of guanine nucleotide-binding proteins (G-proteins) during non-canonical Wnt signaling. Girdin, also called Akt phosphorylation enhancer (APE), or coiled-coil domain-containing protein 88A (CCDC88A), or G alpha-interacting vesicle-associated protein (GIV), or Girders of actin filament, or Hook-related protein 1 (HkRP1), is a bifunctional modulator of guanine nucleotide-binding proteins (G proteins). It acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein G(i) alpha subunits. It also acts as a guanine nucleotide dissociation inhibitor for guanine nucleotide-binding protein G(s) subunit alpha GNAS. In addition, Girdin plays an essential role in cell migration. Gipie, also called GRP78-interacting protein induced by ER stress, or coiled-coil domain-containing protein 88B (CCDC88B), or brain leucine zipper domain-containing protein, or Hook-related protein 3 (HkRP3), is a novel actin cytoskeleton-binding protein and Akt substrate that regulates cell migratory responses in various biological contexts. It acts as a positive regulator of T-cell maturation and inflammatory function. As a microtubule-binding protein, Gipie regulates lytic granule clustering and NK cell killing. All family members contain a conserved globular Hook domain which folds as a variant of the helical calponin homology (CH) domain.
Pssm-ID: 411794 Cd Length: 149 Bit Score: 101.90 E-value: 3.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 15 SLLTWIQTFNVEAPCQ-TVEDLTNGVVMAQVLQKIDPAYFDEnwlnRIKTEVGDNWRLKISNLKKILKGILDYNHEILGQ 93
Cdd:cd22223 5 PLVTWAKTFADDGSAElSYTDLVDGVFLNNVMLQIDPRPFSE----VSNRNVDDDVNARIQNLDLLLRNIKSFYQEVLQQ 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1729156922 94 QINdFTLPDVNLIGEHSD----VAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQEL 157
Cdd:cd22223 81 LIV-MKLPDILTIGREPEseqsLEELEKLLLLLLGCAVQCERKEEFIERIKNLDLEVQHALVACIQEV 147
|
|
| HkD_Daple |
cd22228 |
Hook domain found in Daple (Dvl-associating protein with a high frequency of leucine residues) ... |
12-157 |
2.48e-17 |
|
Hook domain found in Daple (Dvl-associating protein with a high frequency of leucine residues) and similar proteins; Protein Daple, also called coiled-coil domain-containing protein 88C (CCDC88C), or Hook-related protein 2 (HkRP2), is a novel non-receptor nucleotide exchange factor (GEF) required for activation of guanine nucleotide-binding proteins (G-proteins) during non-canonical Wnt signaling.
Pssm-ID: 411799 Cd Length: 153 Bit Score: 79.58 E-value: 2.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 12 LGESLLTWIQTFNV-----EAPCQTVEDLTNGVVMAQVLQKIDPAYFDEnwlnRIKTEVGDNWRLKISNLKKILKGILDY 86
Cdd:cd22228 2 LQSPLVTWVKTFGPlgfgsEDKLSMYMDLVDGVFLNKIMLQIDPRPTNQ----RVNKHVNNDVNLRIQNLTILVRHIKTY 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1729156922 87 NHEILgQQINDFTLPDVNLIGEH----SDVAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQEL 157
Cdd:cd22228 78 YQEVL-QQLIVMNLPNVLMIGKDplsgKSMEEIKKMLLLVLGCAVQCERKEEFIERIKQLDIETQAAIVSHIQEV 151
|
|
| HkD_Girdin |
cd22229 |
Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation ... |
16-157 |
6.92e-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: 66.74 E-value: 6.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 16 LLTWIQTFNVEAPCQTVE-----DLTNGVVMAQVLQKIDPAYFDEnwlnRIKTEVGDNWRLKISNLKKILKGILDYNHEI 90
Cdd:cd22229 9 LVTWVKTFGPLATGNGTPldeyvALVDGVFLNEVMLQINPKSSNQ----RVNKKVNNDASLRIQNLSILVKQIKLYYQET 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1729156922 91 LgQQINDFTLPDVNLIGEH----SDVAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQEL 157
Cdd:cd22229 85 L-QQLIMMSLPNVLVLGRNplseQGTEEMKKLLLLLLGCAVQCERKEEFIERIQTLDFDTKAAVAAHIQEV 154
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
260-636 |
1.11e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.89 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 260 RLEAAKDDY---RIRCEELEKEIAELRQQNEelttLAEEAQSLKDEMDVLrhssdkvaKLESQVESYKKKLEDLGDLRRQ 336
Cdd:COG1196 180 KLEATEENLerlEDILGELERQLEPLERQAE----KAERYRELKEELKEL--------EAELLLLKLRELEAELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 337 VKLLEEKNTMYMQNTVSLEEELRKAHAARSQLEtykRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTE 416
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELE---LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 417 RDSLKETIEELrcvQAQEGQLTTSAglmpLGSQESSDSLAAEIVtpEIKEKLIRLQHENKMLKLNQEGSDNEKIALLQSL 496
Cdd:COG1196 325 LAELEEELEEL---EEELEELEEEL----EEAEEELEEAEAELA--EAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 497 LDDANLRKNELETENRLvNQRLLEVQSQVEELQKSLQEQGSKAEDAisvllKKKLEEHLEKLHEANNEIQRKRAIIEDLE 576
Cdd:COG1196 396 AELAAQLEELEEAEEAL-LERLERLEEELEELEEALAELEEEEEEE-----EEALEEAAEEEAELEEEEEALLELLAELL 469
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 577 PRYNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGTAPEIQAL 636
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL 529
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
260-576 |
7.00e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.32 E-value: 7.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 260 RLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSLKDEMDVLRHSSDK-VAKLESQVESYKKKLEDLGdlrrqvK 338
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdLARLEAEVEQLEERIAQLS------K 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 339 LLEEKNTMYMQNTVSLEEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERD 418
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 419 SLKETIEELrcvQAQEGQLttsaglmplgsQESSDSLAAEIVTPEIKEKLIRLQHEnkmLKLNQEGSDNEKIALLQSLLD 498
Cdd:TIGR02168 835 ATERRLEDL---EEQIEEL-----------SEDIESLAAEIEELEELIEELESELE---ALLNERASLEEALALLRSELE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 499 DANLRKNELETENRLVNQRLLEVQSQVEELQksLQEQGSKAE-----DAISVLLKKKLEEHLEKLHEANNEIQRKRAIIE 573
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQLE--LRLEGLEVRidnlqERLSEEYSLTLEEAEALENKIEDDEEEARRRLK 975
|
...
gi 1729156922 574 DLE 576
Cdd:TIGR02168 976 RLE 978
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
130-667 |
6.45e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.86 E-value: 6.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 130 EQKQEYIQTIMMMEESVQHVVMTAIQELMSKESPVSVGNDAYVDLDRQLKKTTEELNEALATKEEIAqrchELDMQVAAL 209
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIE----ELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 210 QEEKSSLLAENQILMERLNQSDS-IEDPNSPAGR---------RHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEI 279
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKeIEELEEKVKElkelkekaeEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 280 AELRQQNEELTTLAEEAQSLKDEMDVLRHSS---DKVAKLESQVESYKKKLEDL--GDLRRQVKLLEEKNTmymqntvSL 354
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEELEERHelyEEAKAKKEELERLKKRLTGLtpEKLEKELEELEKAKE-------EI 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 355 EEELRKAHAARSQLET----YKRQVVELQ-------------------NRLSEESKKADKLEFEYKLLKEKVDGLQKEKD 411
Cdd:PRK03918 404 EEEISKITARIGELKKeikeLKKAIEELKkakgkcpvcgrelteehrkELLEEYTAELKRIEKELKEIEEKERKLRKELR 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 412 RLRTERD------SLKETIEELRCVQAQegqlttsaglmpLGSQESSDSLAAEIVTPEIKEKLIRLQHENKMLKlnqegS 485
Cdd:PRK03918 484 ELEKVLKkeseliKLKELAEQLKELEEK------------LKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLK-----K 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 486 DNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQ-SQVEELQKSLQE---------QGSKAEDAISVLLKK------ 549
Cdd:PRK03918 547 ELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKElepfyneylELKDAEKELEREEKElkklee 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 550 KLEEHLEKLHEANNEIQRKRAIIEDLEPRYNnsslkiEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLdpkqnqgt 629
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEELEKKYS------EEEYEELREEYLELSRELAGLRAELEELEKRREEI-------- 692
|
570 580 590
....*....|....*....|....*....|....*...
gi 1729156922 630 APEIQALKNQLQERDRMFHSLEKEYEKTKTQREMEEKF 667
Cdd:PRK03918 693 KKTLEKLKEELEEREKAKKELEKLEKALERVEELREKV 730
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
355-662 |
4.46e-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: 4.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 355 EEELRKAHAARSQLETYKRQVVEL---QNRLSEESKKADKlefeYKLLKEKVDGLQK-----EKDRLRTERDSLKETIEE 426
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELerqLKSLERQAEKAER----YKELKAELRELELallvlRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 427 LrcvqaqegqlttsaglmplgsQESSDSLAAEIVTPEIKEKLIRLQHenkmlklnqeGSDNEKIALLQSLLDDANLRKNE 506
Cdd:TIGR02168 251 A---------------------EEELEELTAELQELEEKLEELRLEV----------SELEEEIEELQKELYALANEISR 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 507 LETENRLVNQRLLEVQSQVEELQKSLQEQGSKAED--AISVLLKKKLEEHLEKLHEANNEIQRKRAIIEDLEPRYNNSSL 584
Cdd:TIGR02168 300 LEQQKQILRERLANLERQLEELEAQLEELESKLDElaEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1729156922 585 KIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGTAPEIQALKNQLQERDRMFHSLEKEYEKTKTQRE 662
Cdd:TIGR02168 380 QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE 457
|
|
| HkD_Gipie |
cd22230 |
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar ... |
12-157 |
6.14e-10 |
|
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar proteins; Gipie, also called coiled-coil domain-containing protein 88B (CCDC88B), or brain leucine zipper domain-containing protein, or Hook-related protein 3 (HkRP3), is a novel actin cytoskeleton-binding protein and Akt substrate that regulates cell migratory responses in various biological contexts. It acts as a positive regulator of T-cell maturation and inflammatory function. As a microtubule-binding protein, Gipie regulates lytic granule clustering and NK cell killing.
Pssm-ID: 411801 Cd Length: 170 Bit Score: 58.69 E-value: 6.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 12 LGESLLTWIQTF-------------NVEAPCQTVED-------LTNGVVMAQVLQKIDPAYFDENWLNRikteVGDNWRL 71
Cdd:cd22230 4 MSGALVTWALGFeglvgeeedslgfPEEEEEEGTLDaekrflrLSNGDLLNRVMGIIDPSPRGGPRMRG----DDGPAAH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 72 KISNLKKILKGILDYNHEILgQQINDFTLPDVNLIGEH----SDVAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQ 147
Cdd:cd22230 80 RVQNLHILWGRLRDFYQEEL-QQLILSPPPDLQVMGRDpfteEAVQELEKLLRLLLGAAVQCERRELFIRHIQGLDLDVQ 158
|
170
....*....|
gi 1729156922 148 HVVMTAIQEL 157
Cdd:cd22230 159 AELAEAIQEV 168
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
260-591 |
2.47e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.82 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 260 RLEAAKDDYRIRCEELEKEIAEL----RQQNEELTTLAEEAQSLKDEMDVLRHSSDKVAKLESQVESYKKKLED-LGDLR 334
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREELaeevRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDrLEECR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 335 RQVKLLEEKNTMYMQNTVSLEEELRKAH-----------AARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKV 403
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDLEERAEELReeaaeleseleEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 404 DGLQKEKDRLRTERDSLKETIEELRCVQAqEGQLTTSAGLMPLGSQESSDSLAAEIVTpEIKEKLIRLQHENKMLKLNQE 483
Cdd:PRK02224 415 EELREERDELREREAELEATLRTARERVE-EAEALLEAGKCPECGQPVEGSPHVETIE-EDRERVEELEAELEDLEEEVE 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 484 GSDN--EKIALLQSLLDDANLRKNELETENRLVNQR---LLEVQSQVEELQKSLQEQGSKAEDAISVLLKKKL--EEHLE 556
Cdd:PRK02224 493 EVEErlERAEDLVEAEDRIERLEERREDLEELIAERretIEEKRERAEELRERAAELEAEAEEKREAAAEAEEeaEEARE 572
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1729156922 557 -------KLHEANNEIQRKRAIIEDLEPRYNNSSlKIEELQE 591
Cdd:PRK02224 573 evaelnsKLAELKERIESLERIRTLLAAIADAED-EIERLRE 613
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
173-533 |
3.24e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.47 E-value: 3.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 173 DLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLaENQILMERLnqsdsIEDPNSPAGRRHLQLQTQLE 252
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEK-----REYEGYELLKEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 253 QLQEETFRLEAAKDDYRIRCEELEKEIAELRQQNEELTT-----LAEEAQSLKDEMDVLrhsSDKVAKLESQVESYKKKL 327
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKkikdlGEEEQLRVKEKIGEL---EAEIASLERSIAEKEREL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 328 EDLGDLRRQVKLLEEKNTMYMQNtvsLEEELRKAHAARSQLET----YKRQVVELQNRLSEESKKADKLEFEYKLLKEKV 403
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEE---LEREIEEERKRRDKLTEeyaeLKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 404 DGLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTSAGLMPLGSQESSDSLAAEIVTPEIKEKLIRlqheNKMLKLNQE 483
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA----ADLSKYEQE 470
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1729156922 484 GSD-NEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQ 533
Cdd:TIGR02169 471 LYDlKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
304-606 |
8.03e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.30 E-value: 8.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 304 DVLRHSSDKVAKLESQVES---YKKKLEDLGDLRRQVKLLEekntmymqntvsLEEELRKAHAARSQLETYKRQVVELQN 380
Cdd:TIGR02168 193 DILNELERQLKSLERQAEKaerYKELKAELRELELALLVLR------------LEELREELEELQEELKEAEEELEELTA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 381 RLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEEL--RCVQAQEGQLTTSAGLMPLGSQESSDSLAAE 458
Cdd:TIGR02168 261 ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILreRLANLERQLEELEAQLEELESKLDELAEELA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 459 IVTPEIKEKLIRLQHENKMLKLNQEGSDN--EKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQEQG 536
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEEleSRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQ 420
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 537 SKAEDAISVLLKKKLEEHLEKLHEANNEIQRKRAIIEDLEPRYNNSSLKIEELQEALRKKEEEMKQMEER 606
Cdd:TIGR02168 421 QEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
173-658 |
1.25e-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: 58.53 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 173 DLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSiedpnspagrrhlqlqtQLE 252
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER-----------------QLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 253 QLQEETFRLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSLKDEM--------DVLRHSSDKVAKLESQVESYK 324
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELesrleeleEQLETLRSKVAQLELQIASLN 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 325 KKLEdlgDLRRQVKLLEEKNTMYMQNTVSLEEELRKA--HAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEK 402
Cdd:TIGR02168 400 NEIE---RLEARLERLEDRRERLQQEIEELLKKLEEAelKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 403 VDGLQKEKDRLRTERDSLKETIEEL----RCVQAQEGQLTTSAGLMPLGSQ----ESSDSLAAEIVTPEIKEKLI----- 469
Cdd:TIGR02168 477 LDAAERELAQLQARLDSLERLQENLegfsEGVKALLKNQSGLSGILGVLSElisvDEGYEAAIEAALGGRLQAVVvenln 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 470 ----------------------------RLQHENKMLKLNQEG----------SDNEKIALLQSLL---------DDANL 502
Cdd:TIGR02168 557 aakkaiaflkqnelgrvtflpldsikgtEIQGNDREILKNIEGflgvakdlvkFDPKLRKALSYLLggvlvvddlDNALE 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 503 RKNELETENRLV--------------------NQRLLEVQSQVEELQKSLQEQGSKAEDAISVL--LKKKLEEHLEKLHE 560
Cdd:TIGR02168 637 LAKKLRPGYRIVtldgdlvrpggvitggsaktNSSILERRREIEELEEKIEELEEKIAELEKALaeLRKELEELEEELEQ 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 561 ANNEIQRKRAIIEDLEPRYNNSSLKIEELQEALRKKEEEMKQMEER---YKKYLEKAKSVIRTLDPKQNQGTApEIQALK 637
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEieeLEERLEEAEEELAEAEAEIEELEA-QIEQLK 795
|
570 580
....*....|....*....|.
gi 1729156922 638 NQLQERDRMFHSLEKEYEKTK 658
Cdd:TIGR02168 796 EELKALREALDELRAELTLLN 816
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
262-702 |
2.82e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 262 EAAKDDYRIRCEELEKEiAELRQQNEELTTLAEEAQSLKDEMDvlRHSSDKVAKLESQVESYKKKLEDLGDLRRQVKLLE 341
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKK-AEEAKKADEAKKKAEEAKKKADAAK--KKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 342 EKNtmymqntvslEEELRKAHAARSQLETyKRQVVELQNRLSEESKKADKLEfEYKLLKEKVDGLQKEKDRLRtERDSLK 421
Cdd:PTZ00121 1371 KKK----------EEAKKKADAAKKKAEE-KKKADEAKKKAEEDKKKADELK-KAAAAKKKADEAKKKAEEKK-KADEAK 1437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 422 ETIEELRcvQAQEGQlttsaglmplgsQESSDSLAAEIVTPEIKEKlirlqheNKMLKLNQEGSDNEKIALLQSLLDDAN 501
Cdd:PTZ00121 1438 KKAEEAK--KADEAK------------KKAEEAKKAEEAKKKAEEA-------KKADEAKKKAEEAKKADEAKKKAEEAK 1496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 502 LRKNEL----ETENRLVNQRLLEVQSQVEELQKSlqEQGSKAEDAISVLLKKKLE-----EHLEKLHEANNEIQRKRAii 572
Cdd:PTZ00121 1497 KKADEAkkaaEAKKKADEAKKAEEAKKADEAKKA--EEAKKADEAKKAEEKKKADelkkaEELKKAEEKKKAEEAKKA-- 1572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 573 edlEPRYNNSSLKIEELQEALRKKEEEMKQMEERYKKY----LEKAKSV-IRTLDPKQNQGTAPEIQALKNQLQERDRMF 647
Cdd:PTZ00121 1573 ---EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMkaeeAKKAEEAkIKAEELKKAEEEKKKVEQLKKKEAEEKKKA 1649
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1729156922 648 HSLEKEYEKTKTQREmEEKFIGMTLHKKAAEDRLASTGSGQSFLARQRQATNTRR 702
Cdd:PTZ00121 1650 EELKKAEEENKIKAA-EEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK 1703
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
174-426 |
4.19e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 4.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 174 LDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDPNSpagRRHLQLQTQLEQ 253
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE---ERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 254 LQEETFRLEAAKDDYRIRCEELEKEIAELRQQNEEL---------TTLAEEAQSLKDEMDVLRHSSDKVAKLESQVESYK 324
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAeaelaeaeeALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 325 KKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVD 404
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
250 260
....*....|....*....|..
gi 1729156922 405 GLQKEKDRLRTERDSLKETIEE 426
Cdd:COG1196 481 ELLEELAEAAARLLLLLEAEAD 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
259-547 |
6.70e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 6.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 259 FRLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSLKDEMDV-LRHSSDKVAKLESQVESYKKKLEDLG----DL 333
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQqKQILRERLANLERQLEELEAQLEELEskldEL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 334 RRQVKLLEEKNTMYMQNTVSLEEELRKAHA----ARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKE 409
Cdd:TIGR02168 336 AEELAELEEKLEELKEELESLEAELEELEAeleeLESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDR 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 410 KDRLRTERDSLKETIEELRCVQAQEGQLTTSAGLMPLGSQESSDSLAAEIVTPEIKEKLIRLQHENkmlklNQEGSDNEK 489
Cdd:TIGR02168 416 RERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE-----RELAQLQAR 490
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1729156922 490 IALLQSLLddanlrkNELETENRLVNQrLLEVQSQVEELQKSLQEQ---GSKAEDAISVLL 547
Cdd:TIGR02168 491 LDSLERLQ-------ENLEGFSEGVKA-LLKNQSGLSGILGVLSELisvDEGYEAAIEAAL 543
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
174-472 |
7.92e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.23 E-value: 7.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 174 LDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDsiedpnspagRRHLQLQTQLEQ 253
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK----------ERLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 254 LQEETFRLEAAKDDYRIRCEELEKEIAELRQQNEEL--TTLAEEAQSLKDEMDVLRhssDKVAKLESQVESYKKKLEDLg 331
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLeaRLSHSRIPEIQAELSKLE---EEVSRIEARLREIEQKLNRL- 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 332 DLRRQvkLLEEKntmyMQNTVSLEEELRKAHAARSQ-LETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEK 410
Cdd:TIGR02169 825 TLEKE--YLEKE----IQELQEQRIDLKEQIKSIEKeIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL 898
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 411 DRLRTERDSLKETIEELRC--------VQAQEGQLTTSAGLMPLGSQESSDSLAAEIVTPEIKEKLIRLQ 472
Cdd:TIGR02169 899 RELERKIEELEAQIEKKRKrlselkakLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIR 968
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
213-666 |
8.30e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 8.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 213 KSSLLA-ENQILMERLNQSdsIEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDDYR---IRCEELEKEIAELRQQNEE 288
Cdd:COG4717 36 KSTLLAfIRAMLLERLEKE--ADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAelqEELEELEEELEELEAELEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 289 LTT---LAEEAQSLKDEMDVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEELRkaHAAR 365
Cdd:COG4717 114 LREeleKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLS--LATE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 366 SQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKdrlrtERDSLKETIEELR---------CVQAQEGQ 436
Cdd:COG4717 192 EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL-----EAAALEERLKEARlllliaaalLALLGLGG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 437 LTTSAGLMPLGSQESSDSLAAEIVTPEIKEKLIRLQHENKMLKLN-QEGSDNEKIALLQSLLDDANLRKNELETENRLVN 515
Cdd:COG4717 267 SLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPaLEELEEEELEELLAALGLPPDLSPEELLELLDRI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 516 QRLLEVQSQVEELQKSLQEQGskAEDAISVLLKK---KLEEHLEKLHEANNEIQRKRAIIEDLEPRYNNSSLKIEELQEA 592
Cdd:COG4717 347 EELQELLREAEELEEELQLEE--LEQEIAALLAEagvEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEA 424
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1729156922 593 LrkkeeemkqMEERYKKYLEKAKSVIRTLDPKQNQGTApEIQALKNQLQ--ERDRMFHSLEKEYEKTKTQREMEEK 666
Cdd:COG4717 425 L---------DEEELEEELEELEEELEELEEELEELRE-ELAELEAELEqlEEDGELAELLQELEELKAELRELAE 490
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
173-427 |
2.07e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.69 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 173 DLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAE-------------NQILMERLNQSDSIEDPNSP 239
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlshsripeiqaelSKLEEEVSRIEARLREIEQK 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 240 AGRRHLQLQTQLEQLQEETFRLEAAKDdyriRCEELEKEIAELRQQNEELTTLAEEAQ-SLKDEMDVLRHSSDKVAKLES 318
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQRIDLKE----QIKSIEKEIENLNGKKEELEEELEELEaALRDLESRLGDLKKERDELEA 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 319 QVESYKKKLEDLG----DLRRQVKLLEEKNTMYMQNTVSLEEELRK---AHAARSQLETYKRQVVELQNRLSEESKKADK 391
Cdd:TIGR02169 897 QLRELERKIEELEaqieKKRKRLSELKAKLEALEEELSEIEDPKGEdeeIPEEELSLEDVQAELQRVEEEIRALEPVNML 976
|
250 260 270
....*....|....*....|....*....|....*.
gi 1729156922 392 LEFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEEL 427
Cdd:TIGR02169 977 AIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
283-617 |
2.57e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 283 RQQNEELTTLAEEAQSLKDEMDVLRhssDKVAKLESQVESYKKKLED----LGDLRRQVKLLEEKNTMYMQNTVSLEEEL 358
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQ---SELRRIENRLDELSQELSDasrkIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 359 ----RKAHAARSQLETYKRQVVELQNRLSEESKKADKLEfeYKLLKEKVDGLQKEKDRLRTERDSLKETIEELrcvqaqE 434
Cdd:TIGR02169 747 ssleQEIENVKSELKELEARIEELEEDLHKLEEALNDLE--ARLSHSRIPEIQAELSKLEEEVSRIEARLREI------E 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 435 GQLTTSAGLMPLGSQESSdslaaeivtpEIKEKLIRLQHENKMLKLNQEgSDNEKIALLQSLLDDANLRKNELETENRLV 514
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQ----------ELQEQRIDLKEQIKSIEKEIE-NLNGKKEELEEELEELEAALRDLESRLGDL 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 515 NQRLLEVQSQVEELQKSLQEQGSKAEDAISVL--LKKKLEEHLEKLHEANN--------------------EIQRKRAII 572
Cdd:TIGR02169 888 KKERDELEAQLRELERKIEELEAQIEKKRKRLseLKAKLEALEEELSEIEDpkgedeeipeeelsledvqaELQRVEEEI 967
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1729156922 573 EDLEP-------RYNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSV 617
Cdd:TIGR02169 968 RALEPvnmlaiqEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
271-681 |
2.65e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 271 RCEELEKEIAELRQQNEELTTLAEE---AQSLKDEMDVLRHSSD--KVAKLESQVESYKKKLEDLGDLRRQVKLLEEKNT 345
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKAAAAkkkADEAKKKAEEKKKADEakKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 346 MymQNTVSLEEELRKAHAARSQLETYKRQVVELQNRlSEESKKADKLEFEYKllKEKVDGLQKEKDRLRTERDSLKETI- 424
Cdd:PTZ00121 1472 A--DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA-AEAKKKADEAKKAEE--AKKADEAKKAEEAKKADEAKKAEEKk 1546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 425 --EELRcvQAQEGQLTTSAGLMPLGSQESSDSLAAEIVTPEIK-------EKLIRLQHENKMLKLNQEGSDNEKIALLQS 495
Cdd:PTZ00121 1547 kaDELK--KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKkaeeariEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 496 LLDDANLRKNELEtenrlVNQRLLEVQSQVEELQKSLQEQGSKAEDaisvlLKKKLEEHLEKLHEANNEIQRKRAIIEDL 575
Cdd:PTZ00121 1625 LKKAEEEKKKVEQ-----LKKKEAEEKKKAEELKKAEEENKIKAAE-----EAKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 576 EpRYNNSSLKIEELqealRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQgTAPEIQALKNQLQERDRMFHSLEKEYE 655
Cdd:PTZ00121 1695 K-KEAEEAKKAEEL----KKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE-DKKKAEEAKKDEEEKKKIAHLKKEEEK 1768
|
410 420
....*....|....*....|....*.
gi 1729156922 656 KTKTQREMEEKFIGMTLHKKAAEDRL 681
Cdd:PTZ00121 1769 KAEEIRKEKEAVIEEELDEEDEKRRM 1794
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
173-642 |
3.11e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 173 DLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDpnsPAGRRHLQLQTQLE 252
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA---EAEEELEELAEELL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 253 QLQEETFRLEAAKDDYRIRCEELEKEIAELRQQNEEL-TTLAEEAQSLKDEMDVLRHSSDKVAKLESQVESYKKKLEDLG 331
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELeEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 332 DLRRQVKLLEEKNTMYMQNTVSLEEELRKAHAARSQLE--TYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKE 409
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLegVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 410 KDRLRTERDsLKETIEELRcvQAQEGQLTTSAGLMPLGSQESSDSLAAEIVTPEIKEKLIRLQHENkmLKLNQEGSDNEK 489
Cdd:COG1196 550 NIVVEDDEV-AAAAIEYLK--AAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREAD--ARYYVLGDTLLG 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 490 IALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDAISVLLKKKLEEHLEKLHEANNEIQRKR 569
Cdd:COG1196 625 RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEE 704
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1729156922 570 AIIEDLEPRYNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGTAP-EIQALKNQLQE 642
Cdd:COG1196 705 EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELErELERLEREIEA 778
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
318-541 |
6.78e-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: 6.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 318 SQVESYKKKLEDLGDLRRQVKLLEEKntmymqntvsLEEELRKAHAARSQLETYKRQVVELQNRLSEeskkadkLEFEYK 397
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKE----------LAALKKEEKALLKQLAALERRIAALARRIRA-------LEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 398 LLKEKVDGLQKEKDRLRTERDSLKETIEELRCVQAQEGQlttSAGLMPLGSQESSDSLAA-----EIVTPEIKEKLIRLQ 472
Cdd:COG4942 80 ALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGR---QPPLALLLSPEDFLDAVRrlqylKYLAPARREQAEELR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1729156922 473 HENKMLKLNQEGSDNEKiALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAED 541
Cdd:COG4942 157 ADLAELAALRAELEAER-AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
260-681 |
9.44e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 9.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 260 RLEAAKDDYRIRCEELEKEIAE-------LRQQNEELTTLAEEAQSLkdeMDVLRHSSDKVAKLESQVESYKKKLEDLGD 332
Cdd:PRK03918 166 NLGEVIKEIKRRIERLEKFIKRtenieelIKEKEKELEEVLREINEI---SSELPELREELEKLEKEVKELEELKEEIEE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 333 LRRQVKLLEEKNTMYMQNTVSLEEELRKAHAARSQLETYKRQVVELQnrlsEESKKADKLEFEYKLLKEKVDGLQKEKDR 412
Cdd:PRK03918 243 LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK----EKAEEYIKLSEFYEEYLDELREIEKRLSR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 413 LRTERDSLKETIEELRCVQAQEGQLTTSaglmplgSQESSDSLAAEIVTPEIKEKLIRLQHENKMLKLNQEGSDNEKIAl 492
Cdd:PRK03918 319 LEEEINGIEERIKELEEKEERLEELKKK-------LKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLE- 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 493 lqSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQEQgSKAEDAISVLLKKKLEEHLEKLheanneIQRKRAII 572
Cdd:PRK03918 391 --KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEEL-KKAKGKCPVCGRELTEEHRKEL------LEEYTAEL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 573 EDLEPRYNNSSLKIEELQEALRkkeeemkqmeeRYKKYLEKAKSVIRTLDpkqnqgTAPEIQALKNQLQErdrmfHSLEK 652
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELR-----------ELEKVLKKESELIKLKE------LAEQLKELEEKLKK-----YNLEE 519
|
410 420
....*....|....*....|....*....
gi 1729156922 653 EYEKTKTQREMEEKFIGMTLHKKAAEDRL 681
Cdd:PRK03918 520 LEKKAEEYEKLKEKLIKLKGEIKSLKKEL 548
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
260-703 |
1.19e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 260 RLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSLKDEMDVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQVKL 339
Cdd:PTZ00121 1225 KAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKA 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 340 LEEKNTmymqntvslEEELRKAHAARSQLETYKRQVVELQNRlSEESKKAD--------KLEFEYKLLKEKVDGLQKEKD 411
Cdd:PTZ00121 1305 DEAKKK---------AEEAKKADEAKKKAEEAKKKADAAKKK-AEEAKKAAeaakaeaeAAADEAEAAEEKAEAAEKKKE 1374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 412 RLRTERDSLKETIEELRcvQAQEgqLTTSAGLMPLGSQESSDSLAAEIVTPEIKEKLIRLQHENKMLKLNQEGSDNEKIA 491
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEKK--KADE--AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAK 1450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 492 LLQSLLDDA-NLRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDAISVLLKKKLEEHLEKLHEANNEIQRKRA 570
Cdd:PTZ00121 1451 KKAEEAKKAeEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKA 1530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 571 iiedLEPRYNNSSLKIEELQEAlrkkEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGTAPEIQALKNQLQERDRMFHSL 650
Cdd:PTZ00121 1531 ----EEAKKADEAKKAEEKKKA----DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYE 1602
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1729156922 651 EKEYEKTKTQREMEEKFIGMTLHKKAAEDRLASTGSGQSFLARQRQATNTRRS 703
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA 1655
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
260-662 |
1.39e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 260 RLEAAKDdyriRCEELEKEIAELRQQNEELTTLAEE---AQSLKDEMDVLRHSSDKVAKLESQvesyKKKLEDLGDLRRQ 336
Cdd:PTZ00121 1358 EAEAAEE----KAEAAEKKKEEAKKKADAAKKKAEEkkkADEAKKKAEEDKKKADELKKAAAA----KKKADEAKKKAEE 1429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 337 VKLLEEKNTMymqntvslEEELRKAHAARSQLETYKRqvVELQNRLSEESKKADKLEFEYKLlKEKVDGLQKEKDRLRTE 416
Cdd:PTZ00121 1430 KKKADEAKKK--------AEEAKKADEAKKKAEEAKK--AEEAKKKAEEAKKADEAKKKAEE-AKKADEAKKKAEEAKKK 1498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 417 RDSLKETIEELRcvQAQEGQLTTSAGLMPLGSQESSDSLAAEIVTPEIKEKLIRLQHENKMLKLNQEGSDNEKiallQSL 496
Cdd:PTZ00121 1499 ADEAKKAAEAKK--KADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEA----KKA 1572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 497 LDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDA-ISVLLKKKLEEHLEKLHEANNEIQRKRAIIEDL 575
Cdd:PTZ00121 1573 EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAkIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEEL 1652
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 576 EPRYNNSSLKIEELQ----------EALRKKEEEMKQMEERYKKYLEKAKSVIRTldPKQNQGTAPEIQALKNQLQERDR 645
Cdd:PTZ00121 1653 KKAEEENKIKAAEEAkkaeedkkkaEEAKKAEEDEKKAAEALKKEAEEAKKAEEL--KKKEAEEKKKAEELKKAEEENKI 1730
|
410
....*....|....*..
gi 1729156922 646 MFHSLEKEYEKTKTQRE 662
Cdd:PTZ00121 1731 KAEEAKKEAEEDKKKAE 1747
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
304-594 |
1.42e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 304 DVLRHSSDKVAKLESQVESYKkkleDLGDLRRQVK--LLEEKNTM--------YMQNTVSLEEELRKAHAARSQLEtykr 373
Cdd:COG4913 184 RRLGIGSEKALRLLHKTQSFK----PIGDLDDFVReyMLEEPDTFeaadalveHFDDLERAHEALEDAREQIELLE---- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 374 QVVELQNRLSEESKKADKLEF------------EYKLLKEKVDGLQKEKDRLRTERDSLKETIEELRcvqaqegqlttsa 441
Cdd:COG4913 256 PIRELAERYAAARERLAELEYlraalrlwfaqrRLELLEAELEELRAELARLEAELERLEARLDALR------------- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 442 glmplgsqessdslaaeivtpeikEKLIRLQHEnkmlklnQEGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEV 521
Cdd:COG4913 323 ------------------------EELDELEAQ-------IRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAL 371
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1729156922 522 QSQVEELQKSLQEQGSKAEDAISVL------LKKKLEEHLEKLHEANNEIQRKRAIIEDLEPRYNNSSLKIEELQEALR 594
Cdd:COG4913 372 GLPLPASAEEFAALRAEAAALLEALeeeleaLEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
179-431 |
1.42e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 179 KKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDsiEDPNSPAGRRHLQLQTQLEQLQEET 258
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE--EKKKAEEAKKAEEDKNMALRKAEEA 1586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 259 FRLEAAKDDYRIRCEELEKEI-AELRQQNEELTTLAEEAQSLKDEMDVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQV 337
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEEKKMkAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 338 KLLEEKNTMYMQNTVSLEEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTER 417
Cdd:PTZ00121 1667 AKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA 1746
|
250
....*....|....
gi 1729156922 418 DSLKETIEELRCVQ 431
Cdd:PTZ00121 1747 EEAKKDEEEKKKIA 1760
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
130-655 |
2.04e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 51.27 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 130 EQKQEYIQTIMMMEESVQHVVMT--AIQELMSKEspvsvgNDAYVDLDRQLKKTTEELNEALATKEEIaqrcheLDMQVA 207
Cdd:pfam15921 103 KQKFYLRQSVIDLQTKLQEMQMErdAMADIRRRE------SQSQEDLRNQLQNTVHELEAAKCLKEDM------LEDSNT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 208 ALQEEKSSLLAENQILMERLNQSDSIEDPNSPAGRRHlqlqtqlEQLQEETFRLEAAKDDYRIRceELEKEIAELRQQ-- 285
Cdd:pfam15921 171 QIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEH-------DSMSTMHFRSLGSAISKILR--ELDTEISYLKGRif 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 286 --NEELTTLAEEAQSlKDEMdVLRHSSDKVAKLESQVEsykkkLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEelrkaha 363
Cdd:pfam15921 242 pvEDQLEALKSESQN-KIEL-LLQQHQDRIEQLISEHE-----VEITGLTEKASSARSQANSIQSQLEIIQEQ------- 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 364 ARSQLETYKRQVVELQNRLSEESKkadKLEFEYKLLKEKVDGLQK-------EKDRLRTERDSLketieelrcvqaqegq 436
Cdd:pfam15921 308 ARNQNSMYMRQLSDLESTVSQLRS---ELREAKRMYEDKIEELEKqlvlansELTEARTERDQF---------------- 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 437 lttsaglmplgSQES---SDSLAAEIVTPEIKEKLIRLQHENKMLKLNQEGSDNEKIALLQSLLDDANLRKNELETenrL 513
Cdd:pfam15921 369 -----------SQESgnlDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEA---L 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 514 VNQRLLEVQSQVEELQKSLQEQGSKAEDAISvlLKKKLEEHLEKLHEANNEIQRKRAIIEDLEPRYNNSSLKIEELQEAL 593
Cdd:pfam15921 435 LKAMKSECQGQMERQMAAIQGKNESLEKVSS--LTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAI 512
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1729156922 594 RKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGTapEIQALKNQLQERDRMFHSLEKEYE 655
Cdd:pfam15921 513 EATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQT--ECEALKLQMAEKDKVIEILRQQIE 572
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
359-666 |
2.08e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 359 RKAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEyKLLKEKVDGLQKEKDRLR-TERDSLKETIE-ELRCVQAQEGQ 436
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE-REKAERYQALLKEKREYEgYELLKEKEALErQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 437 LTTS-AGLMPLGSQESSDSLAAEIVTPEIKEKLIRLQhENKMLKLNQE-GSDNEKIALLQSLLDDANLRKNELETENRLV 514
Cdd:TIGR02169 249 LEEElEKLTEEISELEKRLEEIEQLLEELNKKIKDLG-EEEQLRVKEKiGELEAEIASLERSIAEKERELEDAEERLAKL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 515 NQRLLEVQSQVEELQKSLQEQGSKAEDAISVL---------LKKKLEEHLEKLHEANNEIQRKRAIIEDLEPRYNNSSLK 585
Cdd:TIGR02169 328 EAEIDKLLAEIEELEREIEEERKRRDKLTEEYaelkeeledLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 586 IEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNqgtapEIQALKNQLQERDRMFHSLEKEYEKTK-TQREME 664
Cdd:TIGR02169 408 LDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL-----EIKKQEWKLEQLAADLSKYEQELYDLKeEYDRVE 482
|
..
gi 1729156922 665 EK 666
Cdd:TIGR02169 483 KE 484
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
260-428 |
3.41e-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: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 260 RLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAE-------------EAQSLKDEMDVLRHSSDKVAKLESQVESYKKK 326
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeidvasaerEIAELEAELERLDASSDDLAALEEQLEELEAE 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 327 LEDL----GDLRRQVKLLEEKNTmymqntvSLEEELRKAHAARSQLETYKRQVV--ELQNRLSEESKKAdklefeykLLK 400
Cdd:COG4913 701 LEELeeelDELKGEIGRLEKELE-------QAEEELDELQDRLEAAEDLARLELraLLEERFAAALGDA--------VER 765
|
170 180
....*....|....*....|....*...
gi 1729156922 401 EKVDGLQKEKDRLRTERDSLKETIEELR 428
Cdd:COG4913 766 ELRENLEERIDALRARLNRAEEELERAM 793
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
273-427 |
3.77e-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: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 273 EELEKEIAELRqqnEELTTLAEEAQSLKDEMDVLRhssdKVAKLESQVESYKKKLEDLGDLRRQVklleekntmymqntV 352
Cdd:COG4913 613 AALEAELAELE---EELAEAEERLEALEAELDALQ----ERREALQRLAEYSWDEIDVASAEREI--------------A 671
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1729156922 353 SLEEELRKAHAARSQLETYKRQVVELQNRLseeskkaDKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEEL 427
Cdd:COG4913 672 ELEAELERLDASSDDLAALEEQLEELEAEL-------EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
260-426 |
5.09e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 5.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 260 RLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSLKDEMDV-LRHSSDKVAKLESQVESYKKKLEDLGDLRRQVK 338
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKeIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 339 LLEEKNTMYMQNTVsLEEELRKAHAarsQLETYKRQVVELQNRLSEESKKADKLEFEyklLKEKVDGLQKEKDRLRTERD 418
Cdd:COG1579 94 LQKEIESLKRRISD-LEDEILELME---RIEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAERE 166
|
....*...
gi 1729156922 419 SLKETIEE 426
Cdd:COG1579 167 ELAAKIPP 174
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
273-588 |
6.60e-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: 6.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 273 EELEKEIAELRQQNEELTTLAEEAQSLKDEMDV----LRHSSDKVAKLESQVESYKKKLEDLGDLRRQVKLLEEKNTMYM 348
Cdd:pfam02463 202 LKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLneerIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEK 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 349 QNTVSLEEELRKAHA-ARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEEL 427
Cdd:pfam02463 282 KLQEEELKLLAKEEEeLKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEEL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 428 RCVQAQEgqlttsaglmplgSQESSDSLAAEIVTPEIKEKLIRLQHENKMLKLNQEGSDNEKIALLQSLLDDANLRKNEL 507
Cdd:pfam02463 362 EKLQEKL-------------EQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 508 ETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDAISVLLKKKLEEHLEKLHEANNEIQRKRAIIEDLEPRYNNSSLKIE 587
Cdd:pfam02463 429 LEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSG 508
|
.
gi 1729156922 588 E 588
Cdd:pfam02463 509 L 509
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
350-684 |
7.79e-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: 49.68 E-value: 7.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 350 NTVSLEEELRKAhaaRSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEELRC 429
Cdd:TIGR02169 668 FSRSEPAELQRL---RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 430 ------------------VQAQEGQLTTSAGLMPLGSQESSDSLAAEIVtPEIKEKLIRLQHENKML---------KLNQ 482
Cdd:TIGR02169 745 dlssleqeienvkselkeLEARIEELEEDLHKLEEALNDLEARLSHSRI-PEIQAELSKLEEEVSRIearlreieqKLNR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 483 EGSDNE----KIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDaisvlLKKKLEEHLEKL 558
Cdd:TIGR02169 824 LTLEKEylekEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD-----LKKERDELEAQL 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 559 HEANNEIQRKRAIIEDLEPRYNNSSLKIEELQEALrkkeeemkqmeerykKYLEKAKSviRTLDPKQNQGTAPEIQALKN 638
Cdd:TIGR02169 899 RELERKIEELEAQIEKKRKRLSELKAKLEALEEEL---------------SEIEDPKG--EDEEIPEEELSLEDVQAELQ 961
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1729156922 639 QLQERDRMFHSL----EKEYEKT-KTQREMEEKFIGMTLHKKAAEDRLAST 684
Cdd:TIGR02169 962 RVEEEIRALEPVnmlaIQEYEEVlKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
191-442 |
8.75e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 8.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 191 TKEEIAQRCHELDMQVAALQEEKSSL---LAENQILMERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDD 267
Cdd:PRK02224 469 TIEEDRERVEELEAELEDLEEEVEEVeerLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAE 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 268 YRIRCEELEKEIAELRQQNEE----LTTLAEEAQSLKDEMDVL---RHSSDKVAKLESQVESYKKKLEDLGDLRRQVK-L 339
Cdd:PRK02224 549 LEAEAEEKREAAAEAEEEAEEareeVAELNSKLAELKERIESLeriRTLLAAIADAEDEIERLREKREALAELNDERReR 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 340 LEEKNTMYMQNTVSLEEE-LRKAHAARSQLETYKRQVVElqnRLSEESKKADKLEFEYKLLKEKVDGLqkekDRLRTERD 418
Cdd:PRK02224 629 LAEKRERKRELEAEFDEArIEEAREDKERAEEYLEQVEE---KLDELREERDDLQAEIGAVENELEEL----EELRERRE 701
|
250 260
....*....|....*....|....
gi 1729156922 419 SLKETIEELRCVQAQEGQLTTSAG 442
Cdd:PRK02224 702 ALENRVEALEALYDEAEELESMYG 725
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
360-544 |
1.10e-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: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 360 KAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEEL------RCVQAQ 433
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERreelgeRARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 434 EGQLTTSAGLMPLGSQESSD----SLAAEIVTPEIKEKLIRLQHENKMLKlNQEGSDNEKIALLQSLLDDANLRKNELET 509
Cdd:COG3883 97 RSGGSVSYLDVLLGSESFSDfldrLSALSKIADADADLLEELKADKAELE-AKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 1729156922 510 ---ENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDAIS 544
Cdd:COG3883 176 qqaEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
173-427 |
1.15e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.90 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 173 DLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAE----NQILMERLNQSDSIEDPNSPAGRRHLQLQ 248
Cdd:TIGR02168 723 ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERleeaEEELAEAEAEIEELEAQIEQLKEELKALR 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 249 TQLEQLQEETFRLEAAKDDYRIRCEELEKEIAELRQQNEElttLAEEAQSLKDEMDVLRHSsdkVAKLESQVESYKKKLE 328
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLED---LEEQIEELSEDIESLAAE---IEELEELIEELESELE 876
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 329 DLGDLRRQVK-LLEEKNTMYMQNTVSLEEELRKAHAARSQLETYKRQVVELQNRLSE--------ESKKADKLEFEYKLL 399
Cdd:TIGR02168 877 ALLNERASLEeALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGlevridnlQERLSEEYSLTLEEA 956
|
250 260
....*....|....*....|....*...
gi 1729156922 400 KEKVDGLQKEKDRLRTERDSLKETIEEL 427
Cdd:TIGR02168 957 EALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
273-663 |
1.28e-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: 48.96 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 273 EELEKEIAELRQQNEELTTLAEEAQSLKDE-------MDVLRHSSD----KVAKLESQVESYKKKLEdlGDLRRQVKLLE 341
Cdd:pfam15921 377 DQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDdrnmEVQRLEALLKAMKSECQ--GQMERQMAAIQ 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 342 EKN------TMYMQNTVSLEEELRKA----HAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKD 411
Cdd:pfam15921 455 GKNeslekvSSLTAQLESTKEMLRKVveelTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQ 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 412 RLRTERDSLKETieelrcvqaqegqlttsaglmplgsQESSDSLAAEIVTPEIKEKLIRLQHENKMLKLNQEGSDNEKI- 490
Cdd:pfam15921 535 HLKNEGDHLRNV-------------------------QTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMq 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 491 ---ALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQ---KSLQEQGSKAEDAISVlLKKKLEEHLEKLHEANNE 564
Cdd:pfam15921 590 vekAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLElekVKLVNAGSERLRAVKD-IKQERDQLLNEVKTSRNE 668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 565 IQRKRAIIEDLEPRYNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKS----VIRTLDPKQNQGTAP--EIQALKN 638
Cdd:pfam15921 669 LNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGsdghAMKVAMGMQKQITAKrgQIDALQS 748
|
410 420 430
....*....|....*....|....*....|
gi 1729156922 639 QLQERDRMFHSLEKEY-----EKTKTQREM 663
Cdd:pfam15921 749 KIQFLEEAMTNANKEKhflkeEKNKLSQEL 778
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
260-697 |
2.74e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 47.91 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 260 RLEAAKDDYRIRCEELEKEIAELRQQ-NEELTTLAEEAQSLKDEMDVLrhSSDKVAKLESQVESYKKKLEDLGDLRRQVK 338
Cdd:pfam12128 280 ERQETSAELNQLLRTLDDQWKEKRDElNGELSAADAAVAKDRSELEAL--EDQHGAFLDADIETAAADQEQLPSWQSELE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 339 LLEEKntmymqntvsleeelrkaHAArsqLETYKRQVVELQNRLseESKKADKLEFEYKLLKEKVDGLQKEKDRLRT-ER 417
Cdd:pfam12128 358 NLEER------------------LKA---LTGKHQDVTAKYNRR--RSKIKEQNNRDIAGIKDKLAKIREARDRQLAvAE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 418 DSLKETIEELRC-VQAQEGQLTTSAGLMPLGSQESSDSLAAEIVTPEIKEKLIRLQHENKMLKLNQEGSdNEKIALLQSL 496
Cdd:pfam12128 415 DDLQALESELREqLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAA-NAEVERLQSE 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 497 LDDANLRKNELETENRLVNQRLLEVQSQVEELQkslqEQGSKAEDAISVLLKKKL---EEHLEK-----------LHEAN 562
Cdd:pfam12128 494 LRQARKRRDQASEALRQASRRLEERQSALDELE----LQLFPQAGTLLHFLRKEApdwEQSIGKvispellhrtdLDPEV 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 563 NEIQRKR-----AIIEDLEPRYNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGTAPEIQALK 637
Cdd:pfam12128 570 WDGSVGGelnlyGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALK 649
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 638 NQLQERDRMFHslEKEYEKTKTQREMEEkfigmtlHKKAAEDRLASTGSGQSFLARQRQA 697
Cdd:pfam12128 650 NARLDLRRLFD--EKQSEKDKKNKALAE-------RKDSANERLNSLEAQLKQLDKKHQA 700
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
298-581 |
3.05e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 47.23 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 298 SLKDEMD-VLR--HSSDKVaklesQVESYKKKLEDLgdlrrQVKLLEEKNTMYMQNTVSLEEELRKAHAARSQLETYKrq 374
Cdd:PRK05771 13 TLKSYKDeVLEalHELGVV-----HIEDLKEELSNE-----RLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVS-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 375 VVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLK--ETIE-ELRCVQAQEGqLTTSAGLMPLGSQES 451
Cdd:PRK05771 81 VKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwGNFDlDLSLLLGFKY-VSVFVGTVPEDKLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 452 SDSLAAEIVTPEIKEKlirlqHENKMLKLNQEGSDNEKIAllqSLLDDANLRKNELETENRL------VNQRLLEVQSQV 525
Cdd:PRK05771 160 LKLESDVENVEYISTD-----KGYVYVVVVVLKELSDEVE---EELKKLGFERLELEEEGTPselireIKEELEEIEKER 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 526 EELQKSLQEQGSKAEDAISVL------LKKKLE--------------------EHLEKLHEANNEIQRKRAIIEDLEPRY 579
Cdd:PRK05771 232 ESLLEELKELAKKYLEELLALyeyleiELERAEalskflktdktfaiegwvpeDRVKKLKELIDKATGGSAYVEFVEPDE 311
|
..
gi 1729156922 580 NN 581
Cdd:PRK05771 312 EE 313
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
144-686 |
4.21e-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: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 144 ESVQHVVMTAIQELMSKESPVSVGNDAYVDLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQIL 223
Cdd:TIGR02168 284 EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 224 -MERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAkddyRIRCEELEKEIAELRQQNEELTTLAEEAQSLKDE 302
Cdd:TIGR02168 364 eAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL----EARLERLEDRRERLQQEIEELLKKLEEAELKELQ 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 303 M----------DVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQVKLLEEKNTMymqnTVSLEEELRKAHAARSQLETYK 372
Cdd:TIGR02168 440 AeleeleeeleELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS----LERLQENLEGFSEGVKALLKNQ 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 373 RQVVELQNRLSeeskkaDKLEFEYKLLKEKVDGLQKEKDRLRTER-DSLKETIEELRcvQAQEGQLT------------T 439
Cdd:TIGR02168 516 SGLSGILGVLS------ELISVDEGYEAAIEAALGGRLQAVVVENlNAAKKAIAFLK--QNELGRVTflpldsikgteiQ 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 440 SAGLMPLGSQESSDSLAAEIVTPEIK----------------------EKLIRLQHENKMLKLNQE---------GSDNE 488
Cdd:TIGR02168 588 GNDREILKNIEGFLGVAKDLVKFDPKlrkalsyllggvlvvddldnalELAKKLRPGYRIVTLDGDlvrpggvitGGSAK 667
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 489 KIALLQSllddanlRKNELETenrlVNQRLLEVQSQVEELQKSLQEQGSKAEDAISVL--LKKKLEEHLEKLHEANNEIQ 566
Cdd:TIGR02168 668 TNSSILE-------RRREIEE----LEEKIEELEEKIAELEKALAELRKELEELEEELeqLRKELEELSRQISALRKDLA 736
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 567 RKRAIIEDLEPRYNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGTAPE--IQALKNQLQERD 644
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALReaLDELRAELTLLN 816
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1729156922 645 RMFHSLEKEYEKTKTQREMEEKFIGMTL--HKKAAEDRLASTGS 686
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEeqIEELSEDIESLAAE 860
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
261-428 |
6.18e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 6.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 261 LEAAKDDYRIRCEELEKEIAELRQQNEeLTTLAEEAQSLKDEMDVLRhssDKVAKLESQVESYKKKLEDLgdlRRQVKLL 340
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNG-LVDLSEEAKLLLQQLSELE---SQLAEARAELAEAEARLAAL---RAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 341 EEKNTMYMQNTV--SLEEELRKAHAARSQLET-----------YKRQVVELQNRLSEESKKA-DKLEFEYKLLKEKVDGL 406
Cdd:COG3206 253 PDALPELLQSPViqQLRAQLAELEAELAELSArytpnhpdviaLRAQIAALRAQLQQEAQRIlASLEAELEALQAREASL 332
|
170 180
....*....|....*....|..
gi 1729156922 407 QKEKDRLRTERDSLKETIEELR 428
Cdd:COG3206 333 QAQLAQLEARLAELPELEAELR 354
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
174-427 |
7.38e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 7.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 174 LDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQS----DSIEDPNSPAGRRHLQLQT 249
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLrerlESLERRIAATERRLEDLEE 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 250 QLEQLQEETFRLEAAKDDYRIRCEELEKEIAELrqqNEELTTLAEEAQSLKDEMDVLrhsSDKVAKLESQVESYKKKLED 329
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEAL---LNERASLEEALALLRSELEEL---SEELRELESKRSELRRELEE 919
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 330 LGDLRRQVKLLEEKNTMYMQNT---------VSLEEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLK 400
Cdd:TIGR02168 920 LREKLAQLELRLEGLEVRIDNLqerlseeysLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELK 999
|
250 260
....*....|....*....|....*..
gi 1729156922 401 EKVDGLQKEKDRLRTERDSLKETIEEL 427
Cdd:TIGR02168 1000 ERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
263-428 |
8.00e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.16 E-value: 8.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 263 AAKDDYRIRCEELEKEIAELRQQNEELTT-LAEEAQSLKDEMDVLRHSSDKVAKLESQVESYKK--KLEDLGDL----RR 335
Cdd:PHA02562 213 ENIARKQNKYDELVEEAKTIKAEIEELTDeLLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKviKMYEKGGVcptcTQ 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 336 QVKLLEEKNTMYMQNTVSLEEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRT 415
Cdd:PHA02562 293 QISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQA 372
|
170
....*....|...
gi 1729156922 416 ERDSLKETIEELR 428
Cdd:PHA02562 373 EFVDNAEELAKLQ 385
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
334-428 |
8.80e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.00 E-value: 8.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 334 RRQVKLLEEKNTMYMQNTVSLEEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLK----------EKV 403
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARseerreirkdREI 467
|
90 100
....*....|....*....|....*
gi 1729156922 404 DGLQKEKDRLRTERDSLKETIEELR 428
Cdd:COG2433 468 SRLDREIERLERELEEERERIEELK 492
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
364-644 |
8.88e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 8.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 364 ARSQLETYKRQVVELQNRLSEeskkadklefeyklLKEKVDGLQKEKDRLRTERDSLkETIEELRcvqaqegqlttsagl 443
Cdd:COG4913 608 NRAKLAALEAELAELEEELAE--------------AEERLEALEAELDALQERREAL-QRLAEYS--------------- 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 444 mplgsqessdslAAEIVTPEIKEKLIRLQHENKMLKlnqegSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQS 523
Cdd:COG4913 658 ------------WDEIDVASAEREIAELEAELERLD-----ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEK 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 524 QV---EELQKSLQEQGSKAEDAISVLLKKKLEEHLEKLHEANNEiqrkRAIIEDLEPRYNNSSLKIEELQEALRKKEeem 600
Cdd:COG4913 721 ELeqaEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVE----RELRENLEERIDALRARLNRAEEELERAM--- 793
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1729156922 601 kqmeeryKKYLEKAKSVIRTLDPkqNQGTAPEIQALKNQLQERD 644
Cdd:COG4913 794 -------RAFNREWPAETADLDA--DLESLPEYLALLDRLEEDG 828
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
154-425 |
1.19e-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: 45.50 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 154 IQELMSKESPVSVGNDAYVDLDRQLKKTTEELNEALATKE-----------EIAQRCHELDMQVAALQEEKSSLLAENQI 222
Cdd:pfam05557 57 IRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKEsqladarevisCLKNELSELRRQIQRAELELQSTNSELEE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 223 LMERLNQSDS----IEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRI---------RCEELEKEIAELRQQNEEL 289
Cdd:pfam05557 137 LQERLDLLKAkaseAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIvknskselaRIPELEKELERLREHNKHL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 290 TT-------LAEEAQSLKDEMDVLRHSSDKVA-------KLESQVESYKKKLEDLG-------DLRRQVKLLEEKNTMYM 348
Cdd:pfam05557 217 NEnienkllLKEEVEDLKRKLEREEKYREEAAtlelekeKLEQELQSWVKLAQDTGlnlrspeDLSRRIEQLQQREIVLK 296
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1729156922 349 QNTVSLEEELRKAHAARSQLETYKRQVVelqnrlseesKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKETIE 425
Cdd:pfam05557 297 EENSSLTSSARQLEKARRELEQELAQYL----------KKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILE 363
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
259-666 |
1.54e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 259 FRLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSLKDEM--DVLRHSSDKVAKLESQVEsykkkledlgDLRRQ 336
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELeaQIRGNGGDRLEQLEREIE----------RLERE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 337 VKLLEEKNTMYMQNTVSLEEELRkahAARSQLETYKRQVVELQNRLSEESKKADKLEFEyklLKEKVDGLQKEKDRLRTE 416
Cdd:COG4913 354 LEERERRRARLEALLAALGLPLP---ASAEEFAALRAEAAALLEALEEELEALEEALAE---AEAALRDLRRELRELEAE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 417 RDSLK-------ETIEELRCVQAQEGQLTTS-----AGLM---------------------------------------- 444
Cdd:COG4913 428 IASLErrksnipARLLALRDALAEALGLDEAelpfvGELIevrpeeerwrgaiervlggfaltllvppehyaaalrwvnr 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 445 ------------------PLGSQESSDSLAAEIVT------PEIKEKLIR------------LQHENK------MLKLNQ 482
Cdd:COG4913 508 lhlrgrlvyervrtglpdPERPRLDPDSLAGKLDFkphpfrAWLEAELGRrfdyvcvdspeeLRRHPRaitragQVKGNG 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 483 E----------------GSDN-EKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKsLQEQGSKAEDAISV 545
Cdd:COG4913 588 TrhekddrrrirsryvlGFDNrAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQR-LAEYSWDEIDVASA 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 546 LLK-KKLEEHLEKLHEANNEIQRKRAIIEDLEprynnssLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPK 624
Cdd:COG4913 667 EREiAELEAELERLDASSDDLAALEEQLEELE-------AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1729156922 625 QNQGTAPEIQALKNQLQE------RDRMFHSLEKEYEKTKTQREMEEK 666
Cdd:COG4913 740 EDLARLELRALLEERFAAalgdavERELRENLEERIDALRARLNRAEE 787
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
260-410 |
1.68e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 44.24 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 260 RLEAAKDDYRIRC-------EELEKEIAELRQQNEEL----TTLAEEAQSLKDEMDVLRHSSDKVAKLESQVESYKKklE 328
Cdd:smart00787 127 RLEAKKMWYEWRMklleglkEGLDENLEGLKEDYKLLmkelELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDP--T 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 329 DLGDLRRQVKLLEEKNTMYMQNTVSLEEELR----KAHAARSQLETYKRQVVELQNRLsEESKKADklEFEYKLLKEKVD 404
Cdd:smart00787 205 ELDRAKEKLKKLLQEIMIKVKKLEELEEELQelesKIEDLTNKKSELNTEIAEAEKKL-EQCRGFT--FKEIEKLKEQLK 281
|
....*.
gi 1729156922 405 GLQKEK 410
Cdd:smart00787 282 LLQSLT 287
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
278-720 |
2.30e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 278 EIAELRQQNEELTTLAEEAQSLKDEMDVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEE 357
Cdd:PRK01156 296 YINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 358 LRKAHAARSQLEtykRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEEL-RCVQAQEGQ 436
Cdd:PRK01156 376 KKKIEEYSKNIE---RMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELsRNMEMLNGQ 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 437 LTTSAGLMPLGSQESSDslaaeiVTPEIKEKLIRLqhENKMLKLNQEGSD-NEKIALLQSLLDDANLRK-NELETENRLV 514
Cdd:PRK01156 453 SVCPVCGTTLGEEKSNH------IINHYNEKKSRL--EEKIREIEIEVKDiDEKIVDLKKRKEYLESEEiNKSINEYNKI 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 515 NQRLLEVQSQVEELQKsLQEQGSKAEDAISVLLKKKLEEHLEKLHEANNEIQRKRAI-IEDLEPRYNNSSLKIEELQEAL 593
Cdd:PRK01156 525 ESARADLEDIKIKINE-LKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVISLIdIETNRSRSNEIKKQLNDLESRL 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 594 RKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNqgtapEIQALKNQLQERDRMFHSLEKEY----EKTKTQREMEEKFIG 669
Cdd:PRK01156 604 QEIEIGFPDDKSYIDKSIREIENEANNLNNKYN-----EIQENKILIEKLRGKIDNYKKQIaeidSIIPDLKEITSRIND 678
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1729156922 670 MTLHKKAAEDRLASTGSGQsflARQRQATNTRRSYPGHVQPATASPRKILE 720
Cdd:PRK01156 679 IEDNLKKSRKALDDAKANR---ARLESTIEILRTRINELSDRINDINETLE 726
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
173-597 |
3.23e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 173 DLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDPnspAGRRHLQLQTQLE 252
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE---EEEALEEAAEEEA 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 253 QLQEETFRLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSLKDEMDVLRHSSDKVAKLESQVESYKKKLEDLGD 332
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 333 LRRQVKLLEEKNTMYMQNTVslEEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDR 412
Cdd:COG1196 533 EAAYEAALEAALAAALQNIV--VEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLRE 610
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 413 LRTERDSLKETIEELRCVQAQ-----------EGQLTTSAGLMPLGSQESSDSLAAEIvtpeiKEKLIRLQHENKMLKLN 481
Cdd:COG1196 611 ADARYYVLGDTLLGRTLVAARleaalrravtlAGRLREVTLEGEGGSAGGSLTGGSRR-----ELLAALLEAEAELEELA 685
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 482 QEGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDAISVLLKKKLEEHLEKLHEA 561
Cdd:COG1196 686 ERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEEL 765
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1729156922 562 NNEIQRKRAIIEDLEP--------------RYNNSSLKIEELQEALRKKE 597
Cdd:COG1196 766 ERELERLEREIEALGPvnllaieeyeeleeRYDFLSEQREDLEEARETLE 815
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
384-662 |
3.56e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 384 EESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTSAglmplgsQESSDSLAAEIVTPE 463
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL-------RKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 464 ikEKLIRLQHENKMLklnqegsdNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDai 543
Cdd:TIGR02168 747 --ERIAQLSKELTEL--------EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL-- 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 544 svlLKKKLEEHLEKLHEANNEIQRKRAIIEDLEPRYNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDP 623
Cdd:TIGR02168 815 ---LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1729156922 624 ---------KQNQGTAPEIQALKNQLQERDRMFHSLEKEYEKTKTQRE 662
Cdd:TIGR02168 892 lrseleelsEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
183-594 |
3.74e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 183 EELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDPNSPAGRRHlqlqtqleqlqeetfRLE 262
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELE---------------ALE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 263 AAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSLKDEMDVL--RHSSDKVAKLESQVESYKKKLEDLGDLRRQVKLL 340
Cdd:COG4717 139 AELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELleQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 341 EEKNTMYMQNTVSLEEELRKAHAARsQLETYKRQ------VVELQNRLSEESKKADK-------------LEFEYKLLKE 401
Cdd:COG4717 219 QEELEELEEELEQLENELEAAALEE-RLKEARLLlliaaaLLALLGLGGSLLSLILTiagvlflvlgllaLLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 402 KVDGLQKEKDRLRTERDSLKET-IEELRCVQAQEGQLTTSAGLMPLGSQESSDSLAAEIVTPEIKEKLIRLQHENKMLkL 480
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEeLEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL-L 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 481 NQEGSDNEKIalLQSLLDDANlRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDAisvLLKKKLEEHLEKLHE 560
Cdd:COG4717 377 AEAGVEDEEE--LRAALEQAE-EYQELKEELEELEEQLEELLGELEELLEALDEEELEEELE---ELEEELEELEEELEE 450
|
410 420 430
....*....|....*....|....*....|....*.
gi 1729156922 561 ANNEIQRKRAIIEDLEP--RYNNSSLKIEELQEALR 594
Cdd:COG4717 451 LREELAELEAELEQLEEdgELAELLQELEELKAELR 486
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
182-443 |
4.21e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 182 TEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQsdsiedpnspagrrhlqlqtqleqlqeetfrL 261
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA-------------------------------L 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 262 EAAKDDYRIRCEELEKEIAELRQQNEELTT-LAEEAQSLKDEMDVL-RHSSDKVAKLESQVESYKKKLEDLGDLRRQVKL 339
Cdd:COG4942 68 ARRIRALEQELAALEAELAELEKEIAELRAeLEAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 340 LEEKNTMYMQNTVSLEEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKLEfeyKLLKEKVDGLQKEKDRLRTERDS 419
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLL---ARLEKELAELAAELAELQQEAEE 224
|
250 260
....*....|....*....|....
gi 1729156922 420 LKETIEELRCVQAQEGQLTTSAGL 443
Cdd:COG4942 225 LEALIARLEAEAAAAAERTPAAGF 248
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
260-606 |
5.09e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.81 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 260 RLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSLKDEMDVLR---HSSDKVAKLESQVESYKKKLEDLGDLR-- 334
Cdd:pfam02463 146 IIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEelkLQELKLKEQAKKALEYYQLKEKLELEEey 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 335 ----RQVKLLEEKNTMYMQNTVSLEEELRKAhAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEK 410
Cdd:pfam02463 226 llylDYLKLNEERIDLLQELLRDEQEEIESS-KQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 411 DRLRTERDSLKETIEELRCVQAQEGQlttsaglmplgSQESSDSLAAEIVTPEIKEKLIRLQHENKMLKLNQEGSDNEKI 490
Cdd:pfam02463 305 LERRKVDDEEKLKESEKEKKKAEKEL-----------KKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 491 ALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDAISVLLKKKLEEHLEKLHEANNEIQRKRA 570
Cdd:pfam02463 374 ELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEEL 453
|
330 340 350
....*....|....*....|....*....|....*.
gi 1729156922 571 IIEDLEPRYNNSSLKIEELQEALRKKEEEMKQMEER 606
Cdd:pfam02463 454 EKQELKLLKDELELKKSEDLLKETQLVKLQEQLELL 489
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
502-666 |
6.45e-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: 43.51 E-value: 6.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 502 LRKNELETENRLVN-----QRLLEVQSQVEELQKSLQEQGSKAEDAISV----------LLKKKLEEHLEKLHEANNEIQ 566
Cdd:TIGR02168 170 YKERRKETERKLERtrenlDRLEDILNELERQLKSLERQAEKAERYKELkaelrelelaLLVLRLEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 567 RKRAIIEDLEPRYNNSSLKIEELQEALRKKEEEMKQMEERY----------KKYLEKAKSVIRTLDPKQNQGTApEIQAL 636
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELyalaneisrlEQQKQILRERLANLERQLEELEA-QLEEL 328
|
170 180 190
....*....|....*....|....*....|
gi 1729156922 637 KNQLQERDRMFHSLEKEYEKTKTQREMEEK 666
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEA 358
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
284-593 |
8.14e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.97 E-value: 8.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 284 QQNEELTTLAEEAQ----SLKDEMDVLRHSSDKVAKLESQ----VESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSLE 355
Cdd:PLN02939 111 IDNEQQTNSKDGEQlsdfQLEDLVGMIQNAEKNILLLNQArlqaLEDLEKILTEKEALQGKINILEMRLSETDARIKLAA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 356 EELRKAHAARSQLETYKRqvvELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEELRCVQAQEG 435
Cdd:PLN02939 191 QEKIHVEILEEQLEKLRN---ELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFKLEKERS 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 436 QLTTSaglmpLGSQESSDSLAAEIVTpeikeKLIRLQHENKMlklnqegsdnEKIALLQSLLDDAnlrKNELEtENRLVN 515
Cdd:PLN02939 268 LLDAS-----LRELESKFIVAQEDVS-----KLSPLQYDCWW----------EKVENLQDLLDRA---TNQVE-KAALVL 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 516 QRLLEVQSQVEELQKSLQEQG-SKAEDAISVLLKKK---LEEHLEKL-HEANNEIQRKRAIIEDLEPryNNSSLKIEELQ 590
Cdd:PLN02939 324 DQNQDLRDKVDKLEASLKEANvSKFSSYKVELLQQKlklLEERLQASdHEIHSYIQLYQESIKEFQD--TLSKLKEESKK 401
|
...
gi 1729156922 591 EAL 593
Cdd:PLN02939 402 RSL 404
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
262-411 |
1.24e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.42 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 262 EAAKDDYRIRCEELEK--EIAELRQQNEELTTLAEEAQSLKDEMDVLRHSSDKVakLESQVESYKKKLEdlgDLRRQVKL 339
Cdd:pfam17380 443 ERAREMERVRLEEQERqqQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKI--LEKELEERKQAMI---EEERKRKL 517
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1729156922 340 LeEKNTMYMQNTVSLEEELRKAHAA-RSQLETYKRQVVELQNRL-SEESKKADKLEFEYKLLKEKVDGLQKEKD 411
Cdd:pfam17380 518 L-EKEMEERQKAIYEEERRREAEEErRKQQEMEERRRIQEQMRKaTEERSRLEAMEREREMMRQIVESEKARAE 590
|
|
| DUF2046 |
pfam09755 |
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ... |
261-404 |
1.41e-03 |
|
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues of a family of proteins of unknown function possibly containing a coiled-coil domain.
Pssm-ID: 401633 [Multi-domain] Cd Length: 304 Bit Score: 41.35 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 261 LEAAKDDYRIRCEELEKEIAELRQ----------QNEEL--TTLAEEAQSLKDEMDVLRHSSDKvaKLESQVESYKKKLE 328
Cdd:pfam09755 40 LKMELETYKLRCKALQEENRALRQasvniqakaeQEEEFisNTLLKKIQALKKEKETLAMNYEQ--EEEFLTNDLSRKLT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 329 DLGDLRRQVKLLEEKNTMYMQNTVSLEEELRKA--HAARSQLETYKRQVVELQNRLSEES--------KKADKLEFEYKL 398
Cdd:pfam09755 118 QLRQEKVELEQTLEQEQEYQVNKLMRKIEKLEAetLNKQTNLEQLRREKVELENTLEQEQealvnrlwKRMDKLEAEKRL 197
|
....*.
gi 1729156922 399 LKEKVD 404
Cdd:pfam09755 198 LQEKLD 203
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
360-662 |
1.83e-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: 42.03 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 360 KAHAARSqLETYKRQVVELQNRLSEESKKADKLEFEYKL----LKEKVDGLQKEKDRL----RTE-------RDSLKETI 424
Cdd:pfam15921 73 KEHIERV-LEEYSHQVKDLQRRLNESNELHEKQKFYLRQsvidLQTKLQEMQMERDAMadirRREsqsqedlRNQLQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 425 EELRCVQA-QEGQLTTSAGLMplgSQESSDSLAAEIVTPEIKEKLIRLQhENKMLKLNQEgsDNEKIALLQSLLDDANLR 503
Cdd:pfam15921 152 HELEAAKClKEDMLEDSNTQI---EQLRKMMLSHEGVLQEIRSILVDFE-EASGKKIYEH--DSMSTMHFRSLGSAISKI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 504 KNELETENRLVNQRLLEVQSQVEELQKSLQEQG----SKAEDAISVLLKKK------LEEHLEKLHEANNEIQRKRAIIE 573
Cdd:pfam15921 226 LRELDTEISYLKGRIFPVEDQLEALKSESQNKIelllQQHQDRIEQLISEHeveitgLTEKASSARSQANSIQSQLEIIQ 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 574 DLEPRYNNSSLK--------IEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQgTAPEIQALKNQLQERDR 645
Cdd:pfam15921 306 EQARNQNSMYMRqlsdlestVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQ-FSQESGNLDDQLQKLLA 384
|
330
....*....|....*..
gi 1729156922 646 MFHSLEKEYEKTKTQRE 662
Cdd:pfam15921 385 DLHKREKELSLEKEQNK 401
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
174-409 |
2.04e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.81 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 174 LDRQLKKTTEELNEALATKEEIAqrcHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDpnspagrrhlqlqtqleq 253
Cdd:PLN02939 199 LEEQLEKLRNELLIRGATEGLCV---HSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEE------------------ 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 254 lqeETFRLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAqsLKDEMDVLRHSSDKVAKlesQVESYKKKLEDLGDL 333
Cdd:PLN02939 258 ---RVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLQYDC--WWEKVENLQDLLDRATN---QVEKAALVLDQNQDL 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 334 RRQVKLLEE--------KNTMY----MQNTV-SLEEELRKAHAA-RSQLETYKRQVVELQ---NRLSEESKKadklefey 396
Cdd:PLN02939 330 RDKVDKLEAslkeanvsKFSSYkvelLQQKLkLLEERLQASDHEiHSYIQLYQESIKEFQdtlSKLKEESKK-------- 401
|
250
....*....|...
gi 1729156922 397 KLLKEKVDGLQKE 409
Cdd:PLN02939 402 RSLEHPADDMPSE 414
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
351-594 |
2.13e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 351 TVSLEEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTE----RDSLKETIEE 426
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKvkelKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 427 LRCVQAQEGQLTTSAGLMPLGSqESSDSLAAEIvtpeikEKLIRlQHENKMLKLNQEGSDNEKIALLQSLLDDAnLRKNE 506
Cdd:COG1340 87 LNELREELDELRKELAELNKAG-GSIDKLRKEI------ERLEW-RQQTEVLSPEEEKELVEKIKELEKELEKA-KKALE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 507 LETENRLVNQRLLEVQSQVEELQKSLQEQGSKAE--DAISVLLKKKLEEHLEKLHEANNEIQRKRAIIEDLEPRYNNSSL 584
Cdd:COG1340 158 KNEKLKELRAELKELRKEAEEIHKKIKELAEEAQelHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQK 237
|
250
....*....|
gi 1729156922 585 KIEELQEALR 594
Cdd:COG1340 238 ELRELRKELK 247
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
275-427 |
2.28e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 275 LEKEIAELRQQNEELTTLAEEAQS--LKDEMDVLRHSSDKVAKLESQVEsykkkledlgDLRRQVKLLEEKNTMymqntv 352
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEEreLTEEEEEIRRLEEQVERLEAEVE----------ELEAELEEKDERIER------ 445
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1729156922 353 sLEEELRKahaARSQletykrqvvelQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEEL 427
Cdd:COG2433 446 -LERELSE---ARSE-----------ERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLE 505
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
260-542 |
2.55e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 260 RLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSLKDEMDVLRHSSDK-VAKLESQVESYKKKLED-----LGDL 333
Cdd:pfam01576 409 KLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKdVSSLESQLQDTQELLQEetrqkLNLS 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 334 RRQVKLLEEKNTMYMQntvsLEEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKLEFEYKLLKEKVDG-------- 405
Cdd:pfam01576 489 TRLRQLEDERNSLQEQ----LEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEAltqqleek 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 406 -------------LQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTSAGLMPLGSQESSDSLAAEIVTPEIK------- 465
Cdd:pfam01576 565 aaaydklektknrLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRalslara 644
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 466 -----EKLIRLQHENKMLKLNQEGsdnekialLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQEqgskAE 540
Cdd:pfam01576 645 leealEAKEELERTNKQLRAEMED--------LVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQA----TE 712
|
..
gi 1729156922 541 DA 542
Cdd:pfam01576 713 DA 714
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
266-376 |
3.16e-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: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 266 DDYRIRCEELEKEIAELRQQNEELTtlAEEAQSLKDEMDVLRhssDKVAKLESQVESYKKKLEDLGDLRRQvklLEEKNt 345
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEQDEAS--FERLAELRDELAELE---EELEALKARWEAEKELIEEIQELKEE---LEQRY- 484
|
90 100 110
....*....|....*....|....*....|.
gi 1729156922 346 mymQNTVSLEEELRKAHAARSQLETYKRQVV 376
Cdd:COG0542 485 ---GKIPELEKELAELEEELAELAPLLREEV 512
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
176-656 |
3.40e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.83 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 176 RQLKKTTEELNEALATKEEIAQRCHELDMQVAAL-QEEKSSLLAENQILMER-------LNQSDSIEDPNSPAGR--RHL 245
Cdd:COG5022 878 ELAERQLQELKIDVKSISSLKLVNLELESEIIELkKSLSSDLIENLEFKTELiarlkklLNNIDLEEGPSIEYVKlpELN 957
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 246 QLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAEEAQSL---KDEMDVLRHSSDKVAKLESQVES 322
Cdd:COG5022 958 KLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALqesTKQLKELPVEVAELQSASKIISS 1037
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 323 YKKKLEDLGDLRRQVKLLEEKNT----------MYMQNTVSLEEELRKAHAARSQLETYKRQVVELQNR-LSEESKKADK 391
Cdd:COG5022 1038 ESTELSILKPLQKLKGLLLLENNqlqarykalkLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRnLVKPANVLQF 1117
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 392 LEFE---YKLLKEKVDGLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTSAGLMPLGSQESSDSLAA---------EI 459
Cdd:COG5022 1118 IVAQmikLNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRLYQSAlydeksklsSS 1197
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 460 VTPEIKEKLIRLQHE--------NKMLKLNQEGSDnekIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKS 531
Cdd:COG5022 1198 EVNDLKNELIALFSKifsgwprgDKLKKLISEGWV---PTEYSTSLKGFNNLNKKFDTPASMSNEKLLSLLNSIDNLLSS 1274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 532 LQEQGSKAEDAISVLLKKKLEEHLEKLHEANNEIQRKRAIIEDLeprynNSSLKIEELQEALRKKEEEMKQMEERYKKYL 611
Cdd:COG5022 1275 YKLEEEVLPATINSLLQYINVGLFNALRTKASSLRWKSATEVNY-----NSEELDDWCREFEISDVDEELEELIQAVKVL 1349
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1729156922 612 EKAKSVI----RTLDPKQNQGTApEIQALKNQLQERDRMfHSLEKEYEK 656
Cdd:COG5022 1350 QLLKDDLnkldELLDACYSLNPA-EIQNLKSRYDPADKE-NNLPKEILK 1396
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
275-668 |
3.43e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 275 LEKEIAELRQQNEELTTLAEEAQSLKDEMDVLRHSSDKVAKLESQVESYKKKLEDL--------GDLRRQVKLLEEKNTM 346
Cdd:TIGR04523 98 INKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKEleklnnkyNDLKKQKEELENELNL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 347 YMQNTVSLEEELRKAHAARSQLETykrqvveLQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEE 426
Cdd:TIGR04523 178 LEKEKLNIQKNIDKIKNKLLKLEL-------LLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISN 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 427 lrcvqAQEGQLTTSAGLMPLGSQESSDSLAAEIVTPEIKEKLIRLQH-ENKMLKLNQEgSDNEKIALLQSLLDDANLRKN 505
Cdd:TIGR04523 251 -----TQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQlKSEISDLNNQ-KEQDWNKELKSELKNQEKKLE 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 506 ELETENRLVNQRLLEVQSQVEELQKSLQEQGSKAEDaisvlLKKKLEEHLEKLHEANNEIQRKRAIIEDLEPRYNNSSLK 585
Cdd:TIGR04523 325 EIQNQISQNNKIISQLNEQISQLKKELTNSESENSE-----KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 586 IEELQEALRKKEEEMKQMEERYKKyLEKAKSVIRTLDPKQNQgtapEIQALKNQLqerdrmfHSLEKEYEKTKTQREMEE 665
Cdd:TIGR04523 400 IQNQEKLNQQKDEQIKKLQQEKEL-LEKEIERLKETIIKNNS----EIKDLTNQD-------SVKELIIKNLDNTRESLE 467
|
...
gi 1729156922 666 KFI 668
Cdd:TIGR04523 468 TQL 470
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
169-421 |
3.47e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 169 DAYVDLDRQLKKTTEELnEALATKEEIAQRCHELDMQVAALQEEKSSLLAENqilmerlnqsdsiedpnspAGRRHLQLQ 248
Cdd:COG4913 235 DDLERAHEALEDAREQI-ELLEPIRELAERYAAARERLAELEYLRAALRLWF-------------------AQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 249 TQLEQLQEETFRLEAAKDDYRIRCEELEKEIAELRQQneelttlaeeaqslkdemdVLRHSSDKVAKLESQVEsykkkle 328
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQ-------------------IRGNGGDRLEQLEREIE------- 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 329 dlgDLRRQVKLLEEKNTMYMQNTVSLEEELRkahAARSQLETYKRQVVELQNRLSEESKKADKLEFEyklLKEKVDGLQK 408
Cdd:COG4913 349 ---RLERELEERERRRARLEALLAALGLPLP---ASAEEFAALRAEAAALLEALEEELEALEEALAE---AEAALRDLRR 419
|
250
....*....|...
gi 1729156922 409 EKDRLRTERDSLK 421
Cdd:COG4913 420 ELRELEAEIASLE 432
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
441-660 |
3.84e-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: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 441 AGLMPLGSQESSDSLAAEIvtPEIKEKLIRLQHENKMLKlNQEGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLE 520
Cdd:COG4942 11 LALAAAAQADAAAEAEAEL--EQLQQEIAELEKELAALK-KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 521 VQSQVEELQKSLQEQGSKAEDAISVLLKKKLEEHLEKLHEANN--EIQRKRAIIEDLEPRYNNSSLKIEELQEALRKKEE 598
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDflDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1729156922 599 EMKQMEERYKKYLEKAKSvirtldpkqnqgtapEIQALKNQLQERDRMFHSLEKEYEKTKTQ 660
Cdd:COG4942 168 ELEAERAELEALLAELEE---------------ERAALEALKAERQKLLARLEKELAELAAE 214
|
|
| Taf7 |
COG5414 |
TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation ... |
387-576 |
4.34e-03 |
|
TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation complex [Transcription];
Pssm-ID: 227701 Cd Length: 392 Bit Score: 40.07 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 387 KKADKLEFEYklLKEKVDGLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTSAGLMPLGS---QESSDSLAAEIVTPE 463
Cdd:COG5414 195 KKSSKIEIEE--VEKKVDDLLEKDMKAESVSVVLKDEKELARQERVSSWENFKEEPGEPLSRpalKKEKQGAEEEGEEGM 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 464 IKEKLIRLQHENKMLKLNQE---------GSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQE 534
Cdd:COG5414 273 SEEDLDVGAAEIENKEVSEGdkeqqqeevENAEAHKEEVQSDRPDEIGEEKEEDDENEENERHTELLADELNELEKGIEE 352
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1729156922 535 QGSKAEDAISVLLKKKLEEHLEKLHEannEIQRKRAIIEDLE 576
Cdd:COG5414 353 KRRQMESATNPILQKRFESQLNVLLK---ELELKRKQLEMEE 391
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
175-411 |
4.83e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 175 DRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSiedpnspagrrhlqlqtqleql 254
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA---------------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 255 qeetfRLEAAKDDYRIRCEELEKEIAELRQQNEELTTLAE--EAQSLKDEMDvlrhssdKVAKLESQVESYKKKLEDLGD 332
Cdd:COG3883 73 -----EIAEAEAEIEERREELGERARALYRSGGSVSYLDVllGSESFSDFLD-------RLSALSKIADADADLLEELKA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1729156922 333 LRRQVKLLEEKntmymqntvsLEEELRKAHAARSQLETYKRqvvELQNRLSEESKKADKLEFEYKLLKEKVDGLQKEKD 411
Cdd:COG3883 141 DKAELEAKKAE----------LEAKLAELEALKAELEAAKA---ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
260-482 |
5.38e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.49 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 260 RLEAAKDdyrIRcEELEKEIAELRQQNEELTTLAEEAQSLKDEmdvLRHSSDKVA----KLESQVESYKKKLEDLgdlRR 335
Cdd:pfam15921 644 RLRAVKD---IK-QERDQLLNEVKTSRNELNSLSEDYEVLKRN---FRNKSEEMEtttnKLKMQLKSAQSELEQT---RN 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 336 QVKLLEEKNTMYMQNTVSLEEELRkahAARSQLETYKRQVVELQNRLSEESKkadklefEYKLLKEKVDGLQKEKDRLRT 415
Cdd:pfam15921 714 TLKSMEGSDGHAMKVAMGMQKQIT---AKRGQIDALQSKIQFLEEAMTNANK-------EKHFLKEEKNKLSQELSTVAT 783
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1729156922 416 ERDSLKETIEELRcvqAQEGQLTTSAGLMPLGSQESSDSLAaeivtpEIKEKLIRLQHENKMLKLNQ 482
Cdd:pfam15921 784 EKNKMAGELEVLR---SQERRLKEKVANMEVALDKASLQFA------ECQDIIQRQEQESVRLKLQH 841
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
273-458 |
5.50e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 273 EELEKEIAELRQQNEELTTLAEEAQSLKDEMDVLRHSSDKV-AKLESQVESYKKKLEDLGDLRRQVK-----------LL 340
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLqAEIAEAEAEIEERREELGERARALYrsggsvsyldvLL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 341 EEKNT------MYMQNTVSL--EEELRKAHAARSQLETYKRQVVELQNRLSEeskKADKLEFEYKLLKEKVDGLQKEKDR 412
Cdd:COG3883 110 GSESFsdfldrLSALSKIADadADLLEELKADKAELEAKKAELEAKLAELEA---LKAELEAAKAELEAQQAEQEALLAQ 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1729156922 413 LRTERDSLKETIEELRCVQAQEGQLTTSAGLMPLGSQESSDSLAAE 458
Cdd:COG3883 187 LSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
458-591 |
6.73e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.91 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 458 EIVTP-EIKEKLIRLQHENKMLKLN--QEGSDNEKIALLQSLLDDANLRKNELET---ENRLVNQRLLEVQSQ-VEELQK 530
Cdd:PRK05771 10 LIVTLkSYKDEVLEALHELGVVHIEdlKEELSNERLRKLRSLLTKLSEALDKLRSylpKLNPLREEKKKVSVKsLEELIK 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1729156922 531 SLQEQGSKAEDAISVLLkkkleehlEKLHEANNEIQRKRAIIEDLEPrYNNSSLKIEELQE 591
Cdd:PRK05771 90 DVEEELEKIEKEIKELE--------EEISELENEIKELEQEIERLEP-WGNFDLDLSLLLG 141
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
275-681 |
7.52e-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: 40.03 E-value: 7.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 275 LEKEIAELRQQNEELTTLAEEAQSLKDEMDvlrHSSDKVAKLESQVESYKKKLEDLGDLRRQVKLLEekntmymqntvSL 354
Cdd:TIGR00606 579 LHSKSKEINQTRDRLAKLNKELASLEQNKN---HINNELESKEEQLSSYEDKLFDVCGSQDEESDLE-----------RL 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 355 EEELRKAHAARSQLETYKRQVVELQNRLSEESKKADKL-EFEYKLLKEKVDGLQKEKDRLRTERDSLKETIEELRcvqAQ 433
Cdd:TIGR00606 645 KEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELK---KK 721
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 434 EGQLTTSAGLMPlGSQESSDSLAAEIvtPEIKEKLIRLQHENKMLKLNQEgsDNEKiaLLQSLLDDANLRKnELETENRL 513
Cdd:TIGR00606 722 EKRRDEMLGLAP-GRQSIIDLKEKEI--PELRNKLQKVNRDIQRLKNDIE--EQET--LLGTIMPEEESAK-VCLTDVTI 793
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 514 VNQrlleVQSQVEELQKSLQEQGSKAE----DAISVLLKKKLEEHLEKLHEANNEIQRKRAIIEDLEPRYNNSSLKIEEL 589
Cdd:TIGR00606 794 MER----FQMELKDVERKIAQQAAKLQgsdlDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNEL 869
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 590 QE---ALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQgTAPEIQALKNQLQERDRMFHSLEKEYEKTKTQ-REMEE 665
Cdd:TIGR00606 870 KSeklQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQ-DSPLETFLEKDQQEKEELISSKETSNKKAQDKvNDIKE 948
|
410
....*....|....*.
gi 1729156922 666 KFIGMTLHKKAAEDRL 681
Cdd:TIGR00606 949 KVKNIHGYMKDIENKI 964
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
176-393 |
8.41e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 8.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 176 RQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNqsdsiedpnspagrrhlqlqtqleqlq 255
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID--------------------------- 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 256 eetfrLEAAKDdyriRCEELEKEIAELRQQNEELTTLAEEAQSLKDEMDVLRhssDKVAKLESQVESYKKKLEDLGDLRR 335
Cdd:COG4913 663 -----VASAER----EIAELEAELERLDASSDDLAALEEQLEELEAELEELE---EELDELKGEIGRLEKELEQAEEELD 730
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1729156922 336 QVKLLEEKNTMYMQNTVSLEEELRKAHAARSQLETYKRQvvELQNRLSEESKKADKLE 393
Cdd:COG4913 731 ELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRE--NLEERIDALRARLNRAE 786
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
260-665 |
8.78e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 39.70 E-value: 8.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 260 RLEAAKDDYRIRCEELEKEIAELRQQN----------EELTTLAEEAQSLKDEMDVLRHSSDKVAKLESQVESYKKKLE- 328
Cdd:pfam05483 371 RLEKNEDQLKIITMELQKKSSELEEMTkfknnkevelEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREk 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 329 DLGDLRRQVKLLEEKNTMYMQNTVSLEEELRKAHAARSQLETYKRQVVELQNRLSEEskkADKLEFEYKLLKEKVDGLQK 408
Cdd:pfam05483 451 EIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQE---ASDMTLELKKHQEDIINCKK 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 409 EKDRLRTERDSLKET----IEELRCVQAQEGQLTTSAGLMPLGSQESSDSLAAEIVTPEIKEKL-------IRLQHENK- 476
Cdd:pfam05483 528 QEERMLKQIENLEEKemnlRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKIlenkcnnLKKQIENKn 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 477 --MLKLNQEGSDNEKIALLQS-LLDDANLRKNELETENRLVNQRLLEVqsqVEELQKSLQEQGSKAEDAISVLLKKK--L 551
Cdd:pfam05483 608 knIEELHQENKALKKKGSAENkQLNAYEIKVNKLELELASAKQKFEEI---IDNYQKEIEDKKISEEKLLEEVEKAKaiA 684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729156922 552 EEHLEKLHEANNEIQRKRAIIEDLEPRYNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTldpkqnqgtap 631
Cdd:pfam05483 685 DEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKA----------- 753
|
410 420 430
....*....|....*....|....*....|....
gi 1729156922 632 EIQALKNQLQerdrmfhsLEKEyEKTKTQREMEE 665
Cdd:pfam05483 754 ELLSLKKQLE--------IEKE-EKEKLKMEAKE 778
|
|
| |
