|
Name |
Accession |
Description |
Interval |
E-value |
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
179-704 |
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: 629.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 179 FLSEEAEEGDELQQRCLDLERQLMLLSEEKQSLAQENAGLRERMGRPEGEGTPG-LTAKKLLLLQSQLEQLQEENFRLES 257
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGtPGGKKYLLLQKQLEQLQEENFRLET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 258 GREDERLRCAELEREVAELQHRNQALTSLAQEAQALKDEMDELRQSSERAGQLEATLTSCRRRLGELRELRRQVRQLEER 337
Cdd:pfam05622 81 ARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLGDLRRQVKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 338 NAGHAERTRQLEDELRRAGSLRAQLEAQRRQVQELQGQRQEEAMKAEKWLFECRNLEEKYESVTKEKERLLAERDSLREA 417
Cdd:pfam05622 161 NAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRET 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 418 NEELRCAQLQPRGLTQADPSLDPTSTPVDNLAAEILPAELRETLLRLQLENKRL-CRQEAADRERQEELQRHLEDANRAR 496
Cdd:pfam05622 241 NEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLrLGQEGSYRERLTELQQLLEDANRRK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 497 HGLETQHRLNQQQLSELRAQVEDLQKALQEQGGKTEDaiSILLKRKLEEHLQKLHEADLELQRKREYIEELEPPTDSSTA 576
Cdd:pfam05622 321 NELETQNRLANQRILELQQQVEELQKALQEQGSKAED--SSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 577 RRIEELQHNLQKKDADLRAMEERYRRYVDKARMVMQTMEPKQRPAagAPPELHSLRTQLRERDVRIRHLEMDFEKSRSQR 656
Cdd:pfam05622 399 QKIDELQEALRKKDEDMKAMEERYKKYVEKAKSVIKTLDPKQNPA--SPPEIQALKNQLLEKDKKIEHLERDFEKSKLQR 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 154354985 657 EQEEKLLISAWYNMGMALQQRAGEERAP---AHAQSFLAQQRLATNSRRGP 704
Cdd:pfam05622 477 EQEEKLIVTAWYNMGMALHRKAIEERLAglsSPGQSFLARQRQATNARRGL 527
|
|
| HkD_Hook2 |
cd22227 |
Hook domain found in protein Hook 2 (Hook2) and similar proteins; Hook2 is a ... |
7-156 |
2.38e-96 |
|
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: 294.47 E-value: 2.38e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 7 ELCGSLLTWLQTFHVPSPCASPQDLSSGLAVAYVLNQIDPSWFNEAWLQGISEDPGPNWKLKVSNLKMVLRSLVEYSQDV 86
Cdd:cd22227 1 ELCDSLLTWLQTFQVPSPCSSYQDLTSGVAIAQVLNRIDPSWFNEAWLGRIKEDTGDNWRLKVSNLKKILQSLLEYYQDV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 87 LAHPVSEEHLPDVSLIGEFSDPAELGKLLQLVLGCAISCEKKQDHIQRIMTLEESVQHVVMEAIQELMTK 156
Cdd:cd22227 81 LGHQVSEDHLPDVNLIGEFSDDTELGKLLQLVLGCAISCEKKQEHIQQIMTLEESVQHVVMEAIQELLTK 150
|
|
| HOOK_N |
pfam19047 |
HOOK domain; This domain is found at the N-terminus of HOOK proteins. |
7-157 |
2.31e-94 |
|
HOOK domain; This domain is found at the N-terminus of HOOK proteins.
Pssm-ID: 465958 Cd Length: 151 Bit Score: 289.31 E-value: 2.31e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 7 ELCGSLLTWLQTFHVPSPCASPQDLSSGLAVAYVLNQIDPSWFNEAWLQGISEDPGPNWKLKVSNLKMVLRSLVEYSQDV 86
Cdd:pfam19047 1 ELCDSLLTWLQTFNVPAPCATVEDLTDGVAMAQVLHQIDPSWFTEAWLSRIKEDVGDNWRLKVSNLKKILQSVVDYYQDV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 154354985 87 LAHPVSEEHLPDVSLIGEFSDPAELGKLLQLVLGCAISCEKKQDHIQRIMTLEESVQHVVMEAIQELMTKD 157
Cdd:pfam19047 81 LGQQISDFLLPDVNLIGEHSDPAELGRLLQLILGCAVNCEKKQEYIQQIMTLEESVQHVVMTAIQELMSKD 151
|
|
| HkD_Hook |
cd22222 |
Hook domain found in Hook family of microtubule-binding proteins; The Hook family includes ... |
9-155 |
5.30e-82 |
|
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: 256.79 E-value: 5.30e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 9 CGSLLTWLQTFHVPSPCASPQDLSSGLAVAYVLNQIDPSWFNEAWLQGISEDPGPNWKLKVSNLKMVLRSLVEYSQDVLA 88
Cdd:cd22222 1 CDSLLQWLQTFNLIAPHATAEDLSDGVAIAQVLNQIDPEYFSDSWLSKIKPDVGDNWRLKVSNLKKILKGIVDYYSEVLG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 154354985 89 HPVSEEHLPDVSLIGEFSDPAELGKLLQLVLGCAISCEKKQDHIQRIMTLEESVQHVVMEAIQELMT 155
Cdd:cd22222 81 QQISGFTMPDVNAIAEKEDPKELGRLLQLVLGCAVNCERKEEYIQAIMGLEESVQHVVMEAIQELMS 147
|
|
| HkD_Hook1 |
cd22225 |
Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a ... |
8-157 |
1.54e-67 |
|
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: 218.95 E-value: 1.54e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 8 LCGSLLTWLQTFHVPSPCASPQDLSSGLAVAYVLNQIDPSWFNEAWLQGISEDPGPNWKLKVSNLKMVLRSLVEYSQDVL 87
Cdd:cd22225 1 LCDSLIIWLQTFNTAAPCQTVQDLTSGVAMAQVLHQIDSSWFDESWLSRIKEDVGDNWRIKMSNLKKILQGIVDYYHEFL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 88 AHPVSEEHLPDVSLIGEFSDPAELGKLLQLVLGCAISCEKKQDHIQRIMTLEESVQHVVMEAIQELMTKD 157
Cdd:cd22225 81 DQQISEFLLPDLNRIAEHSDPVELGRLLQLILGCAVNCEKKQEHIQNIMTLEESVQHVVMTAIQELMSKE 150
|
|
| HkD_Hook3 |
cd22226 |
Hook domain found in protein Hook 3 (Hook3) and similar proteins; Hook3 is an adaptor protein ... |
4-156 |
3.40e-66 |
|
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: 215.22 E-value: 3.40e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 4 DKAELCGSLLTWLQTFHVPSPCASPQDLSSGLAVAYVLNQIDPSWFNEAWLQGISEDPGPNWKLKVSNLKMVLRSLVEYS 83
Cdd:cd22226 1 DRAELCESLLTWIQTFNVDAPCQTVEDLTSGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 154354985 84 QDVLAHPVSEEHLPDVSLIGEFSDPAELGKLLQLVLGCAISCEKKQDHIQRIMTLEESVQHVVMEAIQELMTK 156
Cdd:cd22226 81 HEILGQQINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMSK 153
|
|
| HkD_SF |
cd22211 |
Hook domain-containing proteins superfamily; The Hook domain superfamily includes Hook adaptor ... |
11-154 |
8.97e-49 |
|
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: 168.22 E-value: 8.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 11 SLLTWLQTFHVPSPCASPQDLSSGLAVAYVLNQIDPSWFNEAWLQgiSEDPGPNWKLKVSNLKMVLRSLVEYSQDVLAHP 90
Cdd:cd22211 3 ALLAWINTFPLSSPVESLDDLSDGVVLAEILSQIDPSYFDSEWLE--SRDSSDNWVLKLNNLKKLYRSLSKYYREVLGQQ 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 154354985 91 VSEEHLPDVSLIGEFSDPAELGKLLQLVLGCAISCEKKQDHIQRIMTLEESVQHVVMEAIQELM 154
Cdd:cd22211 81 LSDLPLPDLSAIARDGDEEEIVKLLELVLGAAVQCENKEEYIARIQQLDESTQAELMLIIQEVL 144
|
|
| HkD_HkRP |
cd22223 |
Hook domain found in the Hook-related protein (HkRP) family; The HkRP family includes Daple, ... |
8-153 |
3.28e-26 |
|
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: 104.98 E-value: 3.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 8 LCGSLLTWLQTFHV-PSPCASPQDLSSGLAVAYVLNQIDPSWFNEAwlqgISEDPGPNWKLKVSNLKMVLRSLVEYSQDV 86
Cdd:cd22223 2 LSSPLVTWAKTFADdGSAELSYTDLVDGVFLNNVMLQIDPRPFSEV----SNRNVDDDVNARIQNLDLLLRNIKSFYQEV 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 154354985 87 LAHPVSEEhLPDVSLIGEFSDP----AELGKLLQLVLGCAISCEKKQDHIQRIMTLEESVQHVVMEAIQEL 153
Cdd:cd22223 78 LQQLIVMK-LPDILTIGREPESeqslEELEKLLLLLLGCAVQCERKEEFIERIKNLDLEVQHALVACIQEV 147
|
|
| HkD_Daple |
cd22228 |
Hook domain found in Daple (Dvl-associating protein with a high frequency of leucine residues) ... |
12-153 |
1.90e-15 |
|
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: 74.19 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 12 LLTWLQTFhvpSPCASPQ--------DLSSGLAVAYVLNQIDPSWFNeawlQGISEDPGPNWKLKVSNLKMVLRSLVEYS 83
Cdd:cd22228 6 LVTWVKTF---GPLGFGSedklsmymDLVDGVFLNKIMLQIDPRPTN----QRVNKHVNNDVNLRIQNLTILVRHIKTYY 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 154354985 84 QDVLAHPVSEeHLPDVSLIGEfsDP------AELGKLLQLVLGCAISCEKKQDHIQRIMTLEESVQHVVMEAIQEL 153
Cdd:cd22228 79 QEVLQQLIVM-NLPNVLMIGK--DPlsgksmEEIKKMLLLVLGCAVQCERKEEFIERIKQLDIETQAAIVSHIQEV 151
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
267-607 |
9.22e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.97 E-value: 9.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 267 AELEREVAELqhRNQAltSLAQEAQALKDEMDELrqsseragQLEATLTSCRRRLGELRELRRQVRQLEERNAGHAERTR 346
Cdd:COG1196 196 GELERQLEPL--ERQA--EKAERYRELKEELKEL--------EAELLLLKLRELEAELEELEAELEELEAELEELEAELA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 347 QLEDELRRagsLRAQLEAQRRQVQELQGQRQEEAMKAEKWLFECRNLEEKYESVTKEKERLLAERDSLREANEELRcAQL 426
Cdd:COG1196 264 ELEAELEE---LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE-EEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 427 QprgltqadpsldptstpVDNLAAEILPAELRETLLRLQLENKRLCRQEAADRERQEELQRHLEDANRARHGLETQHRLN 506
Cdd:COG1196 340 E-----------------ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 507 QQQLSELRAQVEDLQKALQEQggKTEDAISILLKRKLEEHLQKLHEADLELQRKREYIEELEpptDSSTARRIEELQHNL 586
Cdd:COG1196 403 EELEEAEEALLERLERLEEEL--EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL---ELLAELLEEAALLEA 477
|
330 340
....*....|....*....|.
gi 154354985 587 QKKDADLRAMEERYRRYVDKA 607
Cdd:COG1196 478 ALAELLEELAEAAARLLLLLE 498
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
324-663 |
2.86e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.43 E-value: 2.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 324 LRELRRQVRQLEeRNAGHAERTRQLEDEL--RRAGSLRAQLEAQRRQVQELQGQRQEEAMKAEKWLFECRNLEEKYEsvt 401
Cdd:COG1196 195 LGELERQLEPLE-RQAEKAERYRELKEELkeLEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELE--- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 402 KEKERLLAERDSLREANEELRcaqlqprgltqadpsldptstpvdNLAAEIlpAELRETLLRLQLENKRLCRQEAADRER 481
Cdd:COG1196 271 ELRLELEELELELEEAQAEEY------------------------ELLAEL--ARLEQDIARLEERRRELEERLEELEEE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 482 QEELQRHLEDANRARHGLETQHRLNQQQLSELRAQVEDLQKALQEQGGKTEDAISiLLKRKLEEHLQKLHEADLELQRKR 561
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE-ELEELAEELLEALRAAAELAAQLE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 562 EYIEELEpptdsSTARRIEELQHNLQKKDADLRAMEERYRRYVDKARMVMQTMEPKQRPAAGAPPELHSLRTQLRERDVR 641
Cdd:COG1196 404 ELEEAEE-----ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
330 340
....*....|....*....|..
gi 154354985 642 IRHLEMDFEKSRSQREQEEKLL 663
Cdd:COG1196 479 LAELLEELAEAAARLLLLLEAE 500
|
|
| HkD_Girdin |
cd22229 |
Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation ... |
12-153 |
4.41e-13 |
|
Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation enhancer (APE), or coiled-coil domain-containing protein 88A (CCDC88A), or G alpha-interacting vesicle-associated protein (GIV), or Girders of actin filament, or Hook-related protein 1 (HkRP1), is a bifunctional modulator of guanine nucleotide-binding proteins (G proteins). It acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein G(i) alpha subunits. It also acts as a guanine nucleotide dissociation inhibitor for guanine nucleotide-binding protein G(s) subunit alpha GNAS. In addition, Girdin plays an essential role in cell migration.
Pssm-ID: 411800 Cd Length: 156 Bit Score: 67.51 E-value: 4.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 12 LLTWLQTFHVPSPCASPQ-----DLSSGLAVAYVLNQIDPSWFNEAWLQGISEDPgpnwKLKVSNLKMVLRSLVEYSQDV 86
Cdd:cd22229 9 LVTWVKTFGPLATGNGTPldeyvALVDGVFLNEVMLQINPKSSNQRVNKKVNNDA----SLRIQNLSILVKQIKLYYQET 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 154354985 87 LAHPVSEEhLPDVSLIGE--FSDPA--ELGKLLQLVLGCAISCEKKQDHIQRIMTLEESVQHVVMEAIQEL 153
Cdd:cd22229 85 LQQLIMMS-LPNVLVLGRnpLSEQGteEMKKLLLLLLGCAVQCERKEEFIERIQTLDFDTKAAVAAHIQEV 154
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
254-568 |
6.15e-13 |
|
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: 72.40 E-value: 6.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 254 RLESGREDERLRCAELEREVAELQHRNQALTSLAQEAQALKDEMDelRQSSERAGQLEATLTSCRRRLGELRELRRQVRQ 333
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS--RQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 334 LEERNAGHAERTRQLEDELRRAGSLRAQLEAQ-----------RRQVQELQGQRQEEAMKAEKWLFECRNLEEKYESVTK 402
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQieqlkeelkalREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 403 EKERLLAERDSLREANEELRCAQLQprgltqadpsldptstpvdnlaAEILPAELRETLLRLQLENKRLCRQEAADRERQ 482
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEIEE----------------------LEELIEELESELEALLNERASLEEALALLRSEL 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 483 EELQRHLEDANRARHGLETQHRLNQQQLSELRAQVEDLQKALQEQggktEDAISILLKRKLEEHLQKLHEADLELQRKRE 562
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL----QERLSEEYSLTLEEAEALENKIEDDEEEARR 972
|
....*.
gi 154354985 563 YIEELE 568
Cdd:TIGR02168 973 RLKRLE 978
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
175-714 |
4.79e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 4.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 175 RRYYFLSEEAE--EGDELQQRCLDLERQLMLLSEEKQSLAQENAGLRERMgrpegegtpgltAKKLLLLQSQLEQLQEEN 252
Cdd:COG1196 213 ERYRELKEELKelEAELLLLKLRELEAELEELEAELEELEAELEELEAEL------------AELEAELEELRLELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 253 FRLESGREDERLRCAELEREVAELQHRNQALTSLAQEAQALKDEMDELRqssERAGQLEATLTSCRRRLGELRELRRQVR 332
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE---EELEELEEELEELEEELEEAEEELEEAE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 333 -QLEERNAGHAERTRQLEDELRRAGSLRAQLEAQRRQVQELQGQRQEEAMKAEKWLFECRNLEEKYESVTKEKERLLAER 411
Cdd:COG1196 358 aELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 412 DSLREANEELRCAQLQprgltqadpsldptstpVDNLAAEILPAELRETLLRLQLENKRLCRQEAADRERQEELQRHLED 491
Cdd:COG1196 438 EEEEEALEEAAEEEAE-----------------LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 492 ANRARHGLETQHRLNQQQLSELRAQVEDLQKALQEQGGKTEDAISILLKRKLEEHLQKLHEADLELQRKREYIEELEPPT 571
Cdd:COG1196 501 ADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLD 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 572 DSSTARRIEELQHNLQKKDA-DLRAMEERY---RRYVDKARMVMQTMEPKQRPAAGAppELHSLRTQLRERDVRIRHLEM 647
Cdd:COG1196 581 KIRARAALAAALARGAIGAAvDLVASDLREadaRYYVLGDTLLGRTLVAARLEAALR--RAVTLAGRLREVTLEGEGGSA 658
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 154354985 648 DFEKSRSQREQEEKLLISAWYNMGMALQQRAGEERAPAHAQSFLAQQRLATNSRRGPLGRLASLNLR 714
Cdd:COG1196 659 GGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEA 725
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
180-500 |
6.56e-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: 6.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 180 LSEEAEEGDELQQRCLDLERQLMLLSEEKQSLAQENAGLRERMGRPEGEGTPgLTAKKLLllqsqleqlqeenfrLESGR 259
Cdd:TIGR02168 707 LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE-LEAEIEE---------------LEERL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 260 EDERLRCAELEREVAELQHR-NQALTSLAQEAQALKDEMDELRQSSERAGQLEATLTSCRRRlgeLRELRRQVRQLEERN 338
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQiEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR---IAATERRLEDLEEQI 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 339 AGHAERTRQLEDELRRAGSLRAQLEAQRRQVQELQGQRQEEAMKAEKwlfECRNLEEKYESVTKEKERLLAERDSLREAN 418
Cdd:TIGR02168 848 EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS---ELEELSEELRELESKRSELRRELEELREKL 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 419 E--ELRCAQLQPRGLTQADPSLDPTSTPVDNLAA-----EILPAELRETLLRLQLENKRLCR------QEAAD-RERQEE 484
Cdd:TIGR02168 925 AqlELRLEGLEVRIDNLQERLSEEYSLTLEEAEAlenkiEDDEEEARRRLKRLENKIKELGPvnlaaiEEYEElKERYDF 1004
|
330
....*....|....*.
gi 154354985 485 LQRHLEDANRARHGLE 500
Cdd:TIGR02168 1005 LTAQKEDLTEAKETLE 1020
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
267-542 |
1.17e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.54 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 267 AELEREVAELQHRNQALTSLAQEAQALKDE-MDELRQSSERAGQLEATLTSCRRRLGEL-RELRRQVRQLEERNAGHAER 344
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEElRLEVSELEEEIEELQKELYALANEISRLeQQKQILRERLANLERQLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 345 TRQLEDELRRAGSLRAQLEAQRRQVQELQGQRQEEAMKAEKWLFECRNLEEKYESVTKEKERLLAERDSLREANEELRcA 424
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN-N 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 425 QLQ--PRGLTQADPSLDPTSTPVDNLAAEILPAELRETLLRLQLENKRLCRQEaadrERQEELQRHLEDANRARHGLETQ 502
Cdd:TIGR02168 401 EIErlEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQ----EELERLEEALEELREELEEAEQA 476
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 154354985 503 HRLNQQQLSELRAQVEDLQKALQEQGGKTEDAISILLKRK 542
Cdd:TIGR02168 477 LDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQS 516
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
268-568 |
7.25e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.77 E-value: 7.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 268 ELEREVAELQhrnqaLTSLAQEAQALKDEMDELRQSSERAGQLEATLTS-CRRRLGELRELRRQVRQLEERnagHAERTR 346
Cdd:TIGR02168 217 ELKAELRELE-----LALLVLRLEELREELEELQEELKEAEEELEELTAeLQELEEKLEELRLEVSELEEE---IEELQK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 347 QLEDELRRAGSLRAQLEAQRRQVQELQGQRQEEAMKAEKWLFECRNLEEKYESVTKEKERLLAERDSLREANEELRcAQL 426
Cdd:TIGR02168 289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE-AEL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 427 QprgltqadpsldptstpvdnlAAEILPAELRETLLRLQLENKRLCRQEAADRERQEELQRHLEDANRARHGLETQHRLN 506
Cdd:TIGR02168 368 E---------------------ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEL 426
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 154354985 507 QQQLS-----ELRAQVEDLQKALQEQGGKTEDAISIL--LKRKLEEHLQKLHEADLELQRKREYIEELE 568
Cdd:TIGR02168 427 LKKLEeaelkELQAELEELEEELEELQEELERLEEALeeLREELEEAEQALDAAERELAQLQARLDSLE 495
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
256-660 |
8.65e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.47 E-value: 8.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 256 ESGREDERLRCAELEREVAELQHRNQALTSLAQEAQAlKDEMDELRQSSERAGQLEATLTSCRRRLGELRElrrqvrqle 335
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE-ARKADELKKAEEKKKADEAKKAEEKKKADEAKK--------- 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 336 ernagHAERTRQLEDELRRAGSLRAQLEAQRRQVQELQGQRQEEAMKAEKWLFECRNLEEKYESVTKEKERLLAERDSLR 415
Cdd:PTZ00121 1310 -----KAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAK 1384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 416 EANEELRCAQLQPRGLTQADPSLDptstPVDNLAAEILPAElretLLRLQLENKRLC---RQEAADRERQEELQRHLEDA 492
Cdd:PTZ00121 1385 KKAEEKKKADEAKKKAEEDKKKAD----ELKKAAAAKKKAD----EAKKKAEEKKKAdeaKKKAEEAKKADEAKKKAEEA 1456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 493 NRA----RHGLETQHRLNQQQLSELRAQVEDLQKALQEQGGKTEDAisillkRKLEEHLQKLHEAdlelqRKREYIEELE 568
Cdd:PTZ00121 1457 KKAeeakKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEA------KKAAEAKKKADEA-----KKAEEAKKAD 1525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 569 PPTDSSTARRIEELQHNLQKKDADLRAMEERYRRYVDKARMVMQTMEPKQRPAAGAPPELHSLRTQLRERDVRIRHLEMD 648
Cdd:PTZ00121 1526 EAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK 1605
|
410
....*....|..
gi 154354985 649 FEKSRSQREQEE 660
Cdd:PTZ00121 1606 KMKAEEAKKAEE 1617
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
254-598 |
2.12e-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: 61.24 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 254 RLESGREDERLRCAELEREVAELQHRNQALTSLAQEAQALKDEMDELRQSSERAGQLEATLTscrrrlGELRELRRQVRQ 333
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK------ERLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 334 LEernaghaertRQLEDELRRAGSLRAQLEAQRRQVQELqgQRQEEAMKAEKWLFECRNLEEKYESVTKEKERLLAerdS 413
Cdd:TIGR02169 749 LE----------QEIENVKSELKELEARIEELEEDLHKL--EEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEA---R 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 414 LREANEELRCAQLqprgltqadpsldptstpvDNLAAEILPAELRETLLRLQLENKRLCRQEAADRERQEELQRHLEDAN 493
Cdd:TIGR02169 814 LREIEQKLNRLTL-------------------EKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE 874
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 494 RARHGLETQHRLNQQQLSELRAQVEDLQKALQEQGGKTEDAISIL--LKRKLEEHLQKLHEADLELQRKREYIEELEPpt 571
Cdd:TIGR02169 875 AALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLseLKAKLEALEEELSEIEDPKGEDEEIPEEELS-- 952
|
330 340
....*....|....*....|....*..
gi 154354985 572 dsstarrIEELQHNLQKKDADLRAMEE 598
Cdd:TIGR02169 953 -------LEDVQAELQRVEEEIRALEP 972
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
317-637 |
2.70e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.84 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 317 CRRRlgELRELRRQVRQLEERNAghaertrqledelrragSLRAQLEAQRRQVQELQGQRQEEAMKAEKWLFECRNLEEK 396
Cdd:TIGR02168 674 ERRR--EIEELEEKIEELEEKIA-----------------ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 397 YESVTKEKERLLAERDSLREANEELRC-AQLQPRGLTQADPSLDPTSTPVDNLAAEILPAE-----LRETLLRLQLENKR 470
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAeIEELEERLEEAEEELAEAEAEIEELEAQIEQLKeelkaLREALDELRAELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 471 LCRQEAADRERQEELQRHLEDANRARHGLETQHRLNQQQLSELRAQVEDLQKALQEQggktEDAISILLKRKlEEHLQKL 550
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL----ESELEALLNER-ASLEEAL 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 551 HEADLELQRKREYIEELEpptdsSTARRIEELQHNLQKKDADLRAMEERYR------------RYVDKARMVMQTMEPKQ 618
Cdd:TIGR02168 890 ALLRSELEELSEELRELE-----SKRSELRRELEELREKLAQLELRLEGLEvridnlqerlseEYSLTLEEAEALENKIE 964
|
330
....*....|....*....
gi 154354985 619 RPAAGAPPELHSLRTQLRE 637
Cdd:TIGR02168 965 DDEEEARRRLKRLENKIKE 983
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
181-608 |
6.82e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 6.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 181 SEEAEEGDELQQRCLDLERqlmllSEEKQSLAQENAGLRERMGRPEGEGTPGLTAKKLLLLQSQLEqlqeenfrlESGRE 260
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEKKK-----ADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAD---------EAKKK 1439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 261 DERLRCAELEREVAELQHRNQALTSLAQEAQAlKDEMDELRQSSERAGQLEATLTSCRRRLGELRELRRQVRQLEErnAG 340
Cdd:PTZ00121 1440 AEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK-ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADE--AK 1516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 341 HAERTRQlEDELRRAGSLRAQLEAQRRQvqelQGQRQEEAMKAEkwlfECRNLEE--KYESVTKEKERllaERDSLREAn 418
Cdd:PTZ00121 1517 KAEEAKK-ADEAKKAEEAKKADEAKKAE----EKKKADELKKAE----ELKKAEEkkKAEEAKKAEED---KNMALRKA- 1583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 419 EELRCAQlQPRGLTQADPSLDPTSTPVDNLAAEILPAELRETLLRLQLENKR---LCRQEAADRERQEELQRHLEDANRA 495
Cdd:PTZ00121 1584 EEAKKAE-EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKveqLKKKEAEEKKKAEELKKAEEENKIK 1662
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 496 RHGLETQHRLNQQQLSELRAQVEDLQKALQEQGGKTEDAISI-LLKRKLEEHLQKLHEADLELQRKREYIEELEPPTDSS 574
Cdd:PTZ00121 1663 AAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAeELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED 1742
|
410 420 430
....*....|....*....|....*....|....*.
gi 154354985 575 TaRRIEELQ--HNLQKKDADLRAMEERYRRYVDKAR 608
Cdd:PTZ00121 1743 K-KKAEEAKkdEEEKKKIAHLKKEEEKKAEEIRKEK 1777
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
180-598 |
7.62e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 7.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 180 LSEEAEEGDELQQRCLDLERQLMLLSEEKQSLAQENAGLRERMGRPEGEGTPGLTAKKLLLLQSQLEQLQEENFRLESGR 259
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 260 EDERLRcAELEREVAELQHRNQALTSLAQEAQALKDEMDELRQSSERAGQLEATLTSCRRRLGELRELRRQVRQLEERNA 339
Cdd:COG1196 405 LEEAEE-ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 340 GHAERTRQLEDELRRAGSLRAQLEAQRRQVQELQGQRQEEAMKAE--KWLFECRNLEEKYES------VTKEKERLLAER 411
Cdd:COG1196 484 EELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVliGVEAAYEAALEAALAaalqniVVEDDEVAAAAI 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 412 DSLREAN----EELRCAQLQPRGLTQADPSLDPTSTPVDNLAAEILPAELR----------ETLLRLQLENKRLCRQEAA 477
Cdd:COG1196 564 EYLKAAKagraTFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARyyvlgdtllgRTLVAARLEAALRRAVTLA 643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 478 DRERQEELQRHLEDANRARHGLETQHRLNQQQLSELRAQVEDLQKALQEQGGKTEDAISILLKRKLEEHLQKLHEADLEL 557
Cdd:COG1196 644 GRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEE 723
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 154354985 558 QRKREYIEEL------------------------EPPTDSSTARRIEELQHNLQKKDA-DLRAMEE 598
Cdd:COG1196 724 EALEEQLEAEreelleelleeeelleeealeelpEPPDLEELERELERLEREIEALGPvNLLAIEE 789
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
287-638 |
8.88e-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: 58.93 E-value: 8.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 287 AQEAQALKDEMDELRQSsERAGQLEATLTSCRRRLGELRELRRQVRQLEErnaghaertrQLEDELRRAGSLRAQLEAQR 366
Cdd:TIGR02169 210 AERYQALLKEKREYEGY-ELLKEKEALERQKEAIERQLASLEEELEKLTE----------EISELEKRLEEIEQLLEELN 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 367 RQVQELQGQRQeeamkaekwlfecRNLEEKYESVTKEKERLlaeRDSLREANEELRcaqlqprgltQADPSLDPTSTPVD 446
Cdd:TIGR02169 279 KKIKDLGEEEQ-------------LRVKEKIGELEAEIASL---ERSIAEKERELE----------DAEERLAKLEAEID 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 447 NLAAEIlpAELRETLLRLQLENKRLCRQEAADRERQEELQRHLEDanrarhgLETQHRLNQQQLSELRAQVEDLQKALQE 526
Cdd:TIGR02169 333 KLLAEI--EELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE-------VDKEFAETRDELKDYREKLEKLKREINE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 527 QggKTEDAISILLKRKLEEHLQKLHEadlELQRKREYIEELEPPTDSStARRIEELQHNLQKKDADLRAMEERYRRYVDK 606
Cdd:TIGR02169 404 L--KRELDRLQEELQRLSEELADLNA---AIAGIEAKINELEEEKEDK-ALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
330 340 350
....*....|....*....|....*....|..
gi 154354985 607 ARMVMQTMEPKQRPAAGAPPELHSLRTQLRER 638
Cdd:TIGR02169 478 YDRVEKELSKLQRELAEAEAQARASEERVRGG 509
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
180-695 |
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 154354985 180 LSEEAEEGDELQQRCLDLERQLMLLSEEKQSLAQENAGLRERMGRPEGEGTPGLTAKKLLLLQSQLEQLQEenFRLESGR 259
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV--AQLELQI 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 260 EDERLRCAELEREVAELQHRNQALTS--LAQEAQALKDEMDELRQSSERAGQLEATLTSCRRRLGE-LRELRRQVRQLEE 336
Cdd:TIGR02168 396 ASLNNEIERLEARLERLEDRRERLQQeiEELLKKLEEAELKELQAELEELEEELEELQEELERLEEaLEELREELEEAEQ 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 337 RnaghaerTRQLEDELRRAGSLRAQLEAQRRQVQELQGQRQEEAMKAEKW------LFECRNLEEKYES----------- 399
Cdd:TIGR02168 476 A-------LDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLsgilgvLSELISVDEGYEAaieaalggrlq 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 400 --VTKEKERLLAERDSLREAN-------------------------EELRCAQLQPRGLTQADPSLDPTSTP-------V 445
Cdd:TIGR02168 549 avVVENLNAAKKAIAFLKQNElgrvtflpldsikgteiqgndreilKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvV 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 446 DNL--AAEILP----------------------------------------AELRETLLRLQLENKRLCRQEAADRERQE 483
Cdd:TIGR02168 629 DDLdnALELAKklrpgyrivtldgdlvrpggvitggsaktnssilerrreiEELEEKIEELEEKIAELEKALAELRKELE 708
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 484 ELQRHLEDANRARHGLETQHRLNQQQLSELRAQVEDLQKALQEQGGKTEDaisilLKRKLEEHLQKLHEADLELQRKREY 563
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE-----LEAEIEELEERLEEAEEELAEAEAE 783
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 564 IEELEPptdsstarRIEELQHNLQKKDADLRAMEERYRRYVDKARMVMQTMEPKQRPAAGAPPELHSLRTQLRERDVRIR 643
Cdd:TIGR02168 784 IEELEA--------QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 154354985 644 HLEMDFEKSRSQREQEEKLLISawynmgmALQQRAGEERAPAHAQSFLAQQR 695
Cdd:TIGR02168 856 SLAAEIEELEELIEELESELEA-------LLNERASLEEALALLRSELEELS 900
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
256-661 |
1.80e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.13 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 256 ESGREDERLRCAELEREVAELQHRNQALTSLAQ----EAQALKDEMDELrqsSERAGQLEATLTSCRRRLGELRE----L 327
Cdd:PRK02224 271 EREREELAEEVRDLRERLEELEEERDDLLAEAGlddaDAEAVEARREEL---EDRDEELRDRLEECRVAAQAHNEeaesL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 328 RRQVRQLEERNAGHAERTRQLEDELRRAgslRAQLEAQRRQVQELQGQRQEEAMKAEKWLFECRNLEEKYESVTKEKERL 407
Cdd:PRK02224 348 REDADDLEERAEELREEAAELESELEEA---REAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDEL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 408 LAERDSLR----------EANEELRCAQLQPRGLTQADPSLDPTSTPVDNLAAEILPAELRETLLRLQLENKRLCRQEAA 477
Cdd:PRK02224 425 REREAELEatlrtarervEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 478 dRERQEELQRHLEDANRARHGLETQH-RLNQQ--QLSELRAQVEDLQKALQEQGGKTEDAISillkrKLEEHLQKLHEAD 554
Cdd:PRK02224 505 -VEAEDRIERLEERREDLEELIAERReTIEEKreRAEELRERAAELEAEAEEKREAAAEAEE-----EAEEAREEVAELN 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 555 LELQRKREYIEELEpptdsstarRIEELQHNLQKKDADLRAMEERyrryvdkaRMVMQTMEpKQRpaagappelhslRTQ 634
Cdd:PRK02224 579 SKLAELKERIESLE---------RIRTLLAAIADAEDEIERLREK--------REALAELN-DER------------RER 628
|
410 420
....*....|....*....|....*..
gi 154354985 635 LRERDVRIRHLEMDFEKSRSQREQEEK 661
Cdd:PRK02224 629 LAEKRERKRELEAEFDEARIEEAREDK 655
|
|
| HkD_Gipie |
cd22230 |
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar ... |
8-153 |
5.34e-08 |
|
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar proteins; Gipie, also called coiled-coil domain-containing protein 88B (CCDC88B), or brain leucine zipper domain-containing protein, or Hook-related protein 3 (HkRP3), is a novel actin cytoskeleton-binding protein and Akt substrate that regulates cell migratory responses in various biological contexts. It acts as a positive regulator of T-cell maturation and inflammatory function. As a microtubule-binding protein, Gipie regulates lytic granule clustering and NK cell killing.
Pssm-ID: 411801 Cd Length: 170 Bit Score: 52.91 E-value: 5.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 8 LCGSLLTWLQTF------------------HVPSPCASPQ--DLSSGLAVAYVLNQIDPSWFNEAWLQGISEDPgpnwKL 67
Cdd:cd22230 4 MSGALVTWALGFeglvgeeedslgfpeeeeEEGTLDAEKRflRLSNGDLLNRVMGIIDPSPRGGPRMRGDDGPA----AH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 68 KVSNLKMVLRSLVEYSQDVLaHPVSEEHLPDVSLIGEfsDP------AELGKLLQLVLGCAISCEKKQDHIQRIMTLEES 141
Cdd:cd22230 80 RVQNLHILWGRLRDFYQEEL-QQLILSPPPDLQVMGR--DPfteeavQELEKLLRLLLGAAVQCERRELFIRHIQGLDLD 156
|
170
....*....|..
gi 154354985 142 VQHVVMEAIQEL 153
Cdd:cd22230 157 VQAELAEAIQEV 168
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
267-422 |
5.53e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 5.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 267 AELEREVAELQHRNQALTSLAQEAQALKDEMDELRQSSERA-----------------GQLEATLTSCRRRLGELRELRR 329
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLaeyswdeidvasaereiAELEAELERLDASSDDLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 330 QVRQLEERnagHAERTRQLEDELRRAGSLRAQLEAQRRQVQELQGQRQEEAMKAEKWLFECrnLEEKYESVTKEK----- 404
Cdd:COG4913 693 QLEELEAE---LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL--LEERFAAALGDAverel 767
|
170
....*....|....*....
gi 154354985 405 -ERLLAERDSLREANEELR 422
Cdd:COG4913 768 rENLEERIDALRARLNRAE 786
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
271-662 |
1.04e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 271 REVAELQHRNQALTSLAQEAQALKDEMDELRQSSERAGQLEATLTSCRRRLG---ELRELRRQVRQLEERNAGHAERTRQ 347
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEkllQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 348 LEDELRRAGSLRAQLEAQRRQVQELQGQRQEE---------------AMKAEKWLFECRNLEEKYESVTKEKERLLAERD 412
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELleqlslateeelqdlAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 413 SLR------EANEELRCAQLQPR------GLTQADPSLDPTSTPVDNLAAEIL-PAELRETLLRLQLENKRLCRQEAADR 479
Cdd:COG4717 231 QLEneleaaALEERLKEARLLLLiaaallALLGLGGSLLSLILTIAGVLFLVLgLLALLFLLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 480 ERQEELQRHLEDANRARHGLETqhRLNQQQLSELRAQVEDLQKALQEQGGKTEDAISILLKRKLEEHLQKLHEADLE--- 556
Cdd:COG4717 311 PALEELEEEELEELLAALGLPP--DLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEelr 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 557 --LQRKREYIEELEpptdsstarRIEELQHNLQKKDADLRAMEERYRRYVDKARmvMQTMEPKQRPAAGappELHSLRTQ 634
Cdd:COG4717 389 aaLEQAEEYQELKE---------ELEELEEQLEELLGELEELLEALDEEELEEE--LEELEEELEELEE---ELEELREE 454
|
410 420
....*....|....*....|....*...
gi 154354985 635 LRERDVRIRHLEMDFEKSRSQREQEEKL 662
Cdd:COG4717 455 LAELEAELEQLEEDGELAELLQELEELK 482
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
180-661 |
1.82e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 180 LSEEAEEGDELQQRCLDLERqlmllseEKQSLAQENAGLRERMGrpegegtpgltakkllllqsqleqlqeenfRLESGR 259
Cdd:PRK03918 226 LEKEVKELEELKEEIEELEK-------ELESLEGSKRKLEEKIR------------------------------ELEERI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 260 EDERLRCAELEREVAELQHrnqaLTSLAQEAQALKDEM----DELRQSSERAGQLEATLTSCRRRLGELRELRRQVRQLE 335
Cdd:PRK03918 269 EELKKEIEELEEKVKELKE----LKEKAEEYIKLSEFYeeylDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 336 ERNAGHAERTRQLEDELRRAGSLRAQLEAQRRQVQELQGQRQEEAMKaekwlfECRNLEEKYESVTKEKERLLAERDSLR 415
Cdd:PRK03918 345 KKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEK------ELEELEKAKEEIEEEISKITARIGELK 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 416 EANEELRCAQLQprgLTQADPSLDPTSTPVDNLAAEILPAELRETLLRLQLENKRLCRQEAADRERQEELQRHLEDANR- 494
Cdd:PRK03918 419 KEIKELKKAIEE---LKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEl 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 495 ------ARHGLETQHRLNQQQLSELRAQVEDLQKaLQEQGGKTEDAISILLKR--KLEEHLQKLHEADLELQRKREYIEE 566
Cdd:PRK03918 496 iklkelAEQLKELEEKLKKYNLEELEKKAEEYEK-LKEKLIKLKGEIKSLKKEleKLEELKKKLAELEKKLDELEEELAE 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 567 LEPPTDSSTARRIEELqhnlqkkDADLRAMEERYRRYVdKARMVMQTMEPKQRpaagappELHSLRTQLRERDVRIRHLE 646
Cdd:PRK03918 575 LLKELEELGFESVEEL-------EERLKELEPFYNEYL-ELKDAEKELEREEK-------ELKKLEEELDKAFEELAETE 639
|
490
....*....|....*
gi 154354985 647 MDFEKSRSQREQEEK 661
Cdd:PRK03918 640 KRLEELRKELEELEK 654
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
188-421 |
2.83e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 188 DELQQRCLDLERQLMLLSEEKQSLAQENAGLRERMGRPEGEgtPGLTAKKLLLLQSQLEQLQEENFRLESGREDERLRCA 267
Cdd:TIGR02168 792 EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR--IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 268 ELEREVAELQH-RNQALTSLAQEAQALKDEMDELRQSSERAGQLEATLTSCRRRLGELR----ELRRQVRQLEERNAGHA 342
Cdd:TIGR02168 870 ELESELEALLNeRASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLElrleGLEVRIDNLQERLSEEY 949
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 343 ERTrqLEDELRRAGSLRAQLEAQRRQVQELQGQRQE------EAMKaekwlfECRNLEEKYESVTKEKERLLAERDSLRE 416
Cdd:TIGR02168 950 SLT--LEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlAAIE------EYEELKERYDFLTAQKEDLTEAKETLEE 1021
|
....*
gi 154354985 417 ANEEL 421
Cdd:TIGR02168 1022 AIEEI 1026
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
181-519 |
2.97e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 181 SEEAEEGDELQQRCLDLERqlmllSEEKQSLAQENAGLRERMGRPEGEGTPGLTAKKLLLLQSQLEQLqeenfRLESGRE 260
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKK-----ADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK-----KAEEAKK 1535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 261 DERLRCAELEREVAELQ-----HRNQALTSLAQEAQALKDEMDELRQSSERAGQLEATLTSCRRRLGELRELRRQVRQLE 335
Cdd:PTZ00121 1536 ADEAKKAEEKKKADELKkaeelKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 336 ERNAGHAERTRQLEDELRRAGSLRAQLEAQRRQVQELQGQRQEEAMKAEKWLFECRNLEEKYESVTK-EKERLLAERDSL 414
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKaEEDEKKAAEALK 1695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 415 REANEELRCAQLQPRGltqadpsldptstpvdnlAAEILPAE-LRETLLRLQLENKRLCRQEAADRERQEELQRHLEDAN 493
Cdd:PTZ00121 1696 KEAEEAKKAEELKKKE------------------AEEKKKAEeLKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK 1757
|
330 340
....*....|....*....|....*.
gi 154354985 494 RARHGLETQHRLNQQQLSELRAQVED 519
Cdd:PTZ00121 1758 KIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
268-602 |
3.50e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 268 ELEREVAELQHRNQALTSLAQEAQALKDEMDELRQSSERAGQLEATLtscrRRLGELRELRRQVRQLEERNAGHAERTRQ 347
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL----EKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 348 LEDELRRAGSLRAQLEAQRRQVQELQGQRQEE---------------AMKAEKWLFECRNLEEKYESVTKEKERLLAERD 412
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELleqlslateeelqdlAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 413 SLR------EANEELRCAQLQPR------GLTQADPSLDPTSTPVDNLAAEIL-PAELRETLLRLQLENKRLCRQEAADR 479
Cdd:COG4717 231 QLEneleaaALEERLKEARLLLLiaaallALLGLGGSLLSLILTIAGVLFLVLgLLALLFLLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 480 ERQEELQRHLEDANRARHGLET--------------------QHRLNQQQLSELRAQVEDLQKAL-QEQGGKTEDAISIL 538
Cdd:COG4717 311 PALEELEEEELEELLAALGLPPdlspeellelldrieelqelLREAEELEEELQLEELEQEIAALlAEAGVEDEEELRAA 390
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 154354985 539 LK--RKLEEHLQKLHEADLELQRKR-EYIEELEPPTDSSTARRIEELQHNLQKKDADLRAMEERYRR 602
Cdd:COG4717 391 LEqaEEYQELKEELEELEEQLEELLgELEELLEALDEEELEEELEELEEELEELEEELEELREELAE 457
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
405-608 |
7.14e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 7.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 405 ERLLAERDSLREANEELRCAQLQPRGLTqadpsldptstPVDNLAAEIlpAELRETLLRLQLENKRLCRQEAadRERQEE 484
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLE-----------PIRELAERY--AAARERLAELEYLRAALRLWFA--QRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 485 LQRHLEDANRARHGLETQHRLNQQQLSELRAQVEDLQKALQEQGGKTEDAisilLKRKLEEHLQKLHEADLELQRKREYI 564
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ----LEREIERLERELEERERRRARLEALL 368
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 154354985 565 EELEPPTDSStARRIEELQHNLQKKDADLRAMEERYRRYVDKAR 608
Cdd:COG4913 369 AALGLPLPAS-AEEFAALRAEAAALLEALEEELEALEEALAEAE 411
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
259-568 |
1.08e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 259 REDERLRCAELEREVAELQHRN--QALTSLAQEAQALKDEMDELRQSSERA----GQLEATLTSCRRRLGELRELRRQVR 332
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKDlhERLNGLESELAELDEEIERYEEQREQAretrDEADEVLEEHEERREELETLEAEIE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 333 QLEERNAGhAERTRQledelrragSLRAQLEAQRRQVQELQGQRQEEAMKAEKWLFECRNLEEKYESVTKEKERLlaeRD 412
Cdd:PRK02224 262 DLRETIAE-TERERE---------ELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEEL---RD 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 413 SLREANEELRCAQLQPRGLTQADPSLDPTSTPVDNLAAEiLPAELRETllRLQLENKRlcRQEAADRERQEELQRHLEDA 492
Cdd:PRK02224 329 RLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAE-LESELEEA--REAVEDRR--EEIEELEEEIEELRERFGDA 403
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 154354985 493 NRARHGLETQHRLNQQQLSELRAQVEDLQKALQEQGGKTEDAISILLKRKLEEHLQKLHEADL--ELQRKREYIEELE 568
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHveTIEEDRERVEELE 481
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
180-615 |
1.16e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 180 LSEEAEEGDELQQRCLDLERQLMLLSEEKQSLAQENAGLRERMGRpegegtpgltAKKLLLLQSQLEQLQEENFRLESgr 259
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK----------LEKLLQLLPLYQELEALEAELAE-- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 260 EDERLRcaELEREVAELQHRNQALTSLAQEAQALKDEMDELRQ--SSERAGQLEATLTSCRRRLGELRELRRQVRQLEER 337
Cdd:COG4717 144 LPERLE--ELEERLEELRELEEELEELEAELAELQEELEELLEqlSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 338 NAGHAERTRQLEDELRRAGSLRAQLEAQRRQ-----VQELQGQRQEEAMKAEKW----------LFECRNLEEKYESVTK 402
Cdd:COG4717 222 LEELEEELEQLENELEAAALEERLKEARLLLliaaaLLALLGLGGSLLSLILTIagvlflvlglLALLFLLLAREKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 403 EKERLLAERDSLREANEELRCAQLQPRGltqadpsLDPTSTPVDNLAAEILPAELRETLLRLQLENKRLCRQEAADRERQ 482
Cdd:COG4717 302 KEAEELQALPALEELEEEELEELLAALG-------LPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 483 EELQRHLEDANRARHGLEtqhrlNQQQLSELRAQVEDLQKALQEQGGKTEDAISILLKRKLEEHLQKLHEADLELQRKRE 562
Cdd:COG4717 375 LLAEAGVEDEEELRAALE-----QAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELE 449
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 154354985 563 Y-----------IEELEpptdssTARRIEELQHNLQKKDADLRAMEERYRRYVDKARMVMQTME 615
Cdd:COG4717 450 ElreelaeleaeLEQLE------EDGELAELLQELEELKAELRELAEEWAALKLALELLEEARE 507
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
173-568 |
1.69e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.51 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 173 QSRRYYFLSEEAEEGDELQQRCLDLERQLMLLSEEKQSLAQENAGLRERMGRPEGE----GTPGLTAKKLLLLQSQLEQL 248
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPArqdiDNPGPLTRRMQRGEQTYAQL 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 249 QEENFRLESGREDERLRCAELEREVAELQHRNQALTSLAQEaqaLKDEMDELRQSSERAGQLEATLTSCRRRLGElrELR 328
Cdd:TIGR00618 541 ETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNR---SKEDIPNLQNITVRLQDLTEKLSEAEDMLAC--EQH 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 329 RQVRQLEERNAGH--AERTRQLEDELRRAGSLRAQLE---AQRRQVQELQGQRQEEAMKAEKWLFECRNLEEKYESVTKE 403
Cdd:TIGR00618 616 ALLRKLQPEQDLQdvRLHLQQCSQELALKLTALHALQltlTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYW 695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 404 KERLLAERDSLREANEELRCAQLQPRGLTQADPSLDPTSTPVDNLAAEILP---AELRETLLRLQLENKRLCRQEAADRE 480
Cdd:TIGR00618 696 KEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKelmHQARTVLKARTEAHFNNNEEVTAALQ 775
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 481 RQEELQ---RHLEDANRARHGLETQHRLNQQQLSELRAQVEDLQKALQEQGGKTEDAisilLKRKLEEHLQKLHEADLEL 557
Cdd:TIGR00618 776 TGAELShlaAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQ----FLSRLEEKSATLGEITHQL 851
|
410
....*....|.
gi 154354985 558 QRKREYIEELE 568
Cdd:TIGR00618 852 LKYEECSKQLA 862
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
180-427 |
3.23e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.84 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 180 LSEEAEEGDELQQRCLDLERQLMLLSEEKQslaqenAGLRERMGRPEGEGTpgLTAKKLLLLQSQLEQLQEENFRLESGR 259
Cdd:TIGR02169 260 ISELEKRLEEIEQLLEELNKKIKDLGEEEQ------LRVKEKIGELEAEIA--SLERSIAEKERELEDAEERLAKLEAEI 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 260 EDERLRCAELEREVAELQHRNQALTSlaqEAQALKDEMDELRQsseRAGQLEATLTSCRRRLGELRE----LRRQVRQLE 335
Cdd:TIGR02169 332 DKLLAEIEELEREIEEERKRRDKLTE---EYAELKEELEDLRA---ELEEVDKEFAETRDELKDYREklekLKREINELK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 336 ERNAGHAERTRQLEDELRRagsLRAQLEAQRRQVQELQGQRQEEAMKAEKwlfECRNLEEKYESVTKEKERLLAERDSLR 415
Cdd:TIGR02169 406 RELDRLQEELQRLSEELAD---LNAAIAGIEAKINELEEEKEDKALEIKK---QEWKLEQLAADLSKYEQELYDLKEEYD 479
|
250
....*....|..
gi 154354985 416 EANEELRCAQLQ 427
Cdd:TIGR02169 480 RVEKELSKLQRE 491
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
288-440 |
4.04e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 50.34 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 288 QEAQALKDEMDELRQSSERAGQLEATLTSCRRRLGELRELRRQVRQLEERNAGHAERTRQLEDELRRAGSLRAQLEAQ-- 365
Cdd:COG3096 495 QTARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQaa 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 366 ---------RRQVQELQGQRQEEAMKAEKWL----------------FECRNLEEKYESVTKEKER-LLAERDSLREANE 419
Cdd:COG3096 575 eaveqrselRQQLEQLRARIKELAARAPAWLaaqdalerlreqsgeaLADSQEVTAAMQQLLEREReATVERDELAARKQ 654
|
170 180
....*....|....*....|.
gi 154354985 420 ELrcaQLQPRGLTQADPSLDP 440
Cdd:COG3096 655 AL---ESQIERLSQPGGAEDP 672
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
332-571 |
4.85e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 4.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 332 RQLEERNAGHAERTRQLEDELRRagsLRAQLEAQRRQVQELQGQRQEEAMKAEKwlfecRNLEEKYESVTKEKERLLAER 411
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPE---LRKELEEAEAALEEFRQKNGLVDLSEEA-----KLLLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 412 DSLREANEELRcAQLQPRGLTQADPSLDPTstpVDNLAAEILPAELRETLLRLQLEN-----KRLCRQ-EAADRERQEEL 485
Cdd:COG3206 236 AEAEARLAALR-AQLGSGPDALPELLQSPV---IQQLRAQLAELEAELAELSARYTPnhpdvIALRAQiAALRAQLQQEA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 486 QRHLEDANRARHGLETQHRLNQQQLSELRAQVEDLQKALQEQGGKTEDAISilLKRKLEEHLQKLHEADLELQRKREYIE 565
Cdd:COG3206 312 QRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEV--ARELYESLLQRLEEARLAEALTVGNVR 389
|
....*.
gi 154354985 566 ELEPPT 571
Cdd:COG3206 390 VIDPAV 395
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
260-610 |
1.01e-05 |
|
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: 48.95 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 260 EDERLRCAELErEVAELQHRNqaLTSLAQEAQALKDEMDELRQSSERA----GQLEATLTSCRRRLGELRELRR-QVRQL 334
Cdd:pfam05483 264 EESRDKANQLE-EKTKLQDEN--LKELIEKKDHLTKELEDIKMSLQRSmstqKALEEDLQIATKTICQLTEEKEaQMEEL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 335 EERNAGHAERTRQLE------DELRRAGSLRaqLEAQRRQVQELQGQRQEEAMKAEKWLFECRNLE---EKYESVTKEKE 405
Cdd:pfam05483 341 NKAKAAHSFVVTEFEattcslEELLRTEQQR--LEKNEDQLKIITMELQKKSSELEEMTKFKNNKEvelEELKKILAEDE 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 406 RLLAERDSLREANEELRCAQLQPRGLTQA------DPSLDPTSTP---------VDNLAAEILPAELRETLL-----RLQ 465
Cdd:pfam05483 419 KLLDEKKQFEKIAEELKGKEQELIFLLQArekeihDLEIQLTAIKtseehylkeVEDLKTELEKEKLKNIELtahcdKLL 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 466 LENKRLCrQEAADRERqeELQRHLEDANRARHGLE---TQHRLNQQQLSELRAQVEDLQKALQEQGGKT--------EDA 534
Cdd:pfam05483 499 LENKELT-QEASDMTL--ELKKHQEDIINCKKQEErmlKQIENLEEKEMNLRDELESVREEFIQKGDEVkckldkseENA 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 535 ISILLKRKLEEHLQKLHEADL-----ELQRKREYIEELEPPTDS---------------------------STARRIEEL 582
Cdd:pfam05483 576 RSIEYEVLKKEKQMKILENKCnnlkkQIENKNKNIEELHQENKAlkkkgsaenkqlnayeikvnklelelaSAKQKFEEI 655
|
410 420
....*....|....*....|....*...
gi 154354985 583 QHNLQKKDADLRAMEERYRRYVDKARMV 610
Cdd:pfam05483 656 IDNYQKEIEDKKISEEKLLEEVEKAKAI 683
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
259-702 |
1.14e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 259 REDERLRCAELEREVAELQhrnQALTSLAQEAQALKDEMDELRQsseRAGQLEATLTSCRRRL-----GELRELRRQVRQ 333
Cdd:COG4913 276 YLRAALRLWFAQRRLELLE---AELEELRAELARLEAELERLEA---RLDALREELDELEAQIrgnggDRLEQLEREIER 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 334 LEERNAGHAERTRQLEDELRRAG----SLRAQLEAQRRQVQELQGQRQEEAMKAEKWLFEC----RNLEEKYESVTKEKE 405
Cdd:COG4913 350 LERELEERERRRARLEALLAALGlplpASAEEFAALRAEAAALLEALEEELEALEEALAEAeaalRDLRRELRELEAEIA 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 406 RLLAERDSLREANEELR---CAQLqprGLTQADPS-----LDPTST---------------------PVDNLAA-----E 451
Cdd:COG4913 430 SLERRKSNIPARLLALRdalAEAL---GLDEAELPfvgelIEVRPEeerwrgaiervlggfaltllvPPEHYAAalrwvN 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 452 ILPAELRETLLRLQLENKRLCRQEAADR------------------------------ERQEELQRH--------LEDAN 493
Cdd:COG4913 507 RLHLRGRLVYERVRTGLPDPERPRLDPDslagkldfkphpfrawleaelgrrfdyvcvDSPEELRRHpraitragQVKGN 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 494 RARHGLETQHRL---------NQQQLSELRAQVEDLQKALQEQGGKTEDAisillkRKLEEHLQKLHEADLELQRKREYI 564
Cdd:COG4913 587 GTRHEKDDRRRIrsryvlgfdNRAKLAALEAELAELEEELAEAEERLEAL------EAELDALQERREALQRLAEYSWDE 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 565 EELEpptdsSTARRIEELQ---HNLQKKDADLRAMEERyrryVDKARMvmqtmepkqrpaagappELHSLRTQLRERDVR 641
Cdd:COG4913 661 IDVA-----SAEREIAELEaelERLDASSDDLAALEEQ----LEELEA-----------------ELEELEEELDELKGE 714
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 154354985 642 IRHLEMDFEKSRSQREQEEKLLISAWYNMGMALQQRAGEERAPAHAQSFLAQQRLATNSRR 702
Cdd:COG4913 715 IGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERI 775
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
126-605 |
1.21e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 126 EKKQDHIQRIMTLEESVQHVVMEAIQELMTKDTPDSLSPETYGNFDSQSRRYYFLSEEAEEGDELQQRCLDLERQLMLLS 205
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 206 EEKQSLAQENAGLRERMGR--------PEGEGTpgltAKKLLLLQSQLEQLQEENFRLESGREDERLRCAELEREVAELQ 277
Cdd:PRK03918 259 EKIRELEERIEELKKEIEEleekvkelKELKEK----AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 278 HRNQALTSLAQEAQALKDEMDELRQSS---ERAGQLEATLTSCRRRLGELrELRRQVRQLEERNAGHAERTRQLEDELRR 354
Cdd:PRK03918 335 EKEERLEELKKKLKELEKRLEELEERHelyEEAKAKKEELERLKKRLTGL-TPEKLEKELEELEKAKEEIEEEISKITAR 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 355 AGSLRAQLEAQRRQVQELQGQR-----------------------------QEEAMKAEKWLFECRNLEEKYESVTKEKE 405
Cdd:PRK03918 414 IGELKKEIKELKKAIEELKKAKgkcpvcgrelteehrkelleeytaelkriEKELKEIEEKERKLRKELRELEKVLKKES 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 406 RLLAER---DSLREANEELRCAQLQPrgLTQADPSLDPTSTPVDNLAAEILpaELRETLLRLQLENKRLcrqeaadrerq 482
Cdd:PRK03918 494 ELIKLKelaEQLKELEEKLKKYNLEE--LEKKAEEYEKLKEKLIKLKGEIK--SLKKELEKLEELKKKL----------- 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 483 EELQRHLEDANRARHGLETQ-HRLNQQQLSELRAQVEDLQKALQE--QGGKTEDAISILLKR------KLEEHLQKLHEA 553
Cdd:PRK03918 559 AELEKKLDELEEELAELLKElEELGFESVEELEERLKELEPFYNEylELKDAEKELEREEKElkkleeELDKAFEELAET 638
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 154354985 554 DLELQRKREYIEELEPPTDSSTARRIEELQHNLQKKDADLRAMEERYRRYVD 605
Cdd:PRK03918 639 EKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRRE 690
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
268-538 |
1.39e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 268 ELEREVAELQHRNQALTSLAQEAQALKDEMDELRQsserAGQLEATLTSCRRRLgELRELRRQVRQLEERNAGHAERTRQ 347
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRELAERYAAARERLAE----LEYLRAALRLWFAQR-RLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 348 LEDELRRAGSLRAQLEAQRRQvqelQGQRQEEAMKAEKwlfecrnleekyESVTKEKERLLAERDSLREAneelrCAQLQ 427
Cdd:COG4913 314 LEARLDALREELDELEAQIRG----NGGDRLEQLEREI------------ERLERELEERERRRARLEAL-----LAALG 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 428 prgltqadpsldptstpvdnLAAEILPAELRETLLRLQLENKRLCRQEAADRERQEELQRHLEDANRARHGLETQHRLNQ 507
Cdd:COG4913 373 --------------------LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
250 260 270
....*....|....*....|....*....|.
gi 154354985 508 QQLSELRAQVEDLQKALQEQGGKTEDAISIL 538
Cdd:COG4913 433 RRKSNIPARLLALRDALAEALGLDEAELPFV 463
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
180-418 |
1.63e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.53 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 180 LSEEAEEGDELQQRCLDLERQLMLLSEEKQSLAQENAGLRERMGRPE---GEGTPGLTAKKLLLLQSQLEQLQEENFRLE 256
Cdd:TIGR02169 725 IEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEedlHKLEEALNDLEARLSHSRIPEIQAELSKLE 804
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 257 SGREDERLRCAELEREVAELQHRNQALTSLAQEAQALKDEMDElrQSSERAGQLEATLTSCRRRLGELRELRRQVRQLEE 336
Cdd:TIGR02169 805 EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE--QIKSIEKEIENLNGKKEELEEELEELEAALRDLES 882
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 337 RNAGHAERTRQLEDELRRAGSLRAQLEAQRRQVQELQGQRQEEAMKAEKWLFECRNL----------EEKYESVTKEKER 406
Cdd:TIGR02169 883 RLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPkgedeeipeeELSLEDVQAELQR 962
|
250
....*....|..
gi 154354985 407 LLAERDSLREAN 418
Cdd:TIGR02169 963 VEEEIRALEPVN 974
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
267-422 |
5.63e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 5.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 267 AELEREVAELQHRNQALTSLAQEAQALKDEMDELRQ----SSERAGQLEATLTSCRRRLGEL-RELRRQVRQLEERNAGH 341
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERriaaLARRIRALEQELAALEAELAELeKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 342 AERTRQL------------------EDELRRAGSLRAQLEAQRRQVQELQGQRQEEAMKAEKWLFECRNLEEKYESVTKE 403
Cdd:COG4942 107 AELLRALyrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170
....*....|....*....
gi 154354985 404 KERLLAERDSLREANEELR 422
Cdd:COG4942 187 RAALEALKAERQKLLARLE 205
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
268-566 |
8.62e-05 |
|
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: 45.94 E-value: 8.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 268 ELEREVAELQHRNQALTSLAQEAQALKDEmdELRQS---SERAGQLEATLTSCRRRLGELRELRRQV-RQLEERNAGHAE 343
Cdd:pfam01576 451 EAEGKNIKLSKDVSSLESQLQDTQELLQE--ETRQKlnlSTRLRQLEDERNSLQEQLEEEEEAKRNVeRQLSTLQAQLSD 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 344 RTRQLEDElrrAGSLRAQLEAQRRQVQELQGQRQEEAMKAEkwlfECRNLEEKYESVTKEKERLLAERDSLREANEELRC 423
Cdd:pfam01576 529 MKKKLEED---AGTLEALEEGKKRLQRELEALTQQLEEKAA----AYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEK 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 424 AQLQ-PRGLTQADPSLDPTSTPVDNLAAEILPAELRETLLRLQLENKRLCRQEAADRERQ-----EELQRHLEDANRARH 497
Cdd:pfam01576 602 KQKKfDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQlraemEDLVSSKDDVGKNVH 681
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 498 GLETQHRLNQQQLSELRAQVEDLQKALQEqggkTEDAisillKRKLEEHLQKLH-EADLELQRKREYIEE 566
Cdd:pfam01576 682 ELERSKRALEQQVEEMKTQLEELEDELQA----TEDA-----KLRLEVNMQALKaQFERDLQARDEQGEE 742
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
289-626 |
1.06e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.50 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 289 EAQALKDEMDELRQSSERAGQLEATLTScrrrlgELRELRRQVRQLEERNAGHAERTRQLEdelrragslRAQLEAQRRQ 368
Cdd:pfam17380 297 EQERLRQEKEEKAREVERRRKLEEAEKA------RQAEMDRQAAIYAEQERMAMERERELE---------RIRQEERKRE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 369 VQELQgqRQEEAMKAEKwlfecrnleekyesvTKEKERLLAERDSLRE-ANEELRCAQLQPRGLTQADPSLDPTSTPVDN 447
Cdd:pfam17380 362 LERIR--QEEIAMEISR---------------MRELERLQMERQQKNErVRQELEAARKVKILEEERQRKIQQQKVEMEQ 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 448 LAAEILPAELREtLLRLQLENKR---LCRQEAADRERQEELQRHLEDANRARHGLETQHRLNQQQLSELRAQVedLQKAL 524
Cdd:pfam17380 425 IRAEQEEARQRE-VRRLEEERARemeRVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKI--LEKEL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 525 QEqggKTEDAISILLKRK-LEEHLQKLHEADLELQRKREYIEELEPPTDSSTARRIEELQHNLQKKDADLRAMEeryrRY 603
Cdd:pfam17380 502 EE---RKQAMIEEERKRKlLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAME----RE 574
|
330 340
....*....|....*....|...
gi 154354985 604 VDKARMVMQTMEPKQRPAAGAPP 626
Cdd:pfam17380 575 REMMRQIVESEKARAEYEATTPI 597
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
456-663 |
1.09e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 456 ELRETLLRLQLENKRLCRQEAADRERQEELQRHLEDANRARHGLETQHRLNQQQLSELRAQVEDLQKALqeqgGKTEDAI 535
Cdd:TIGR02169 713 DASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL----NDLEARL 788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 536 SILLKRKLEEHLQKLHEadlELQRKREYIEELEPPTDSSTARR--IEELQHNLQKKDADLRAMEERYRRYVDKARMVMQT 613
Cdd:TIGR02169 789 SHSRIPEIQAELSKLEE---EVSRIEARLREIEQKLNRLTLEKeyLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE 865
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 154354985 614 MEPKQRPAAGAPPELHS----LRTQLRERDVRIRHLEMDFEKSRSQREQEEKLL 663
Cdd:TIGR02169 866 LEEELEELEAALRDLESrlgdLKKERDELEAQLRELERKIEELEAQIEKKRKRL 919
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
260-527 |
1.35e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 260 EDERLRCAELEREVAELQHRNQaltSLAQEAQALKDEMDELRQSSERAGQL-EATLTScrrRLGELRELRRQVRQLEERN 338
Cdd:PRK04863 840 RQLNRRRVELERALADHESQEQ---QQRSQLEQAKEGLSALNRLLPRLNLLaDETLAD---RVEEIREQLDEAEEAKRFV 913
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 339 AGHAERTRQLEDELRRAGSLRAQLEAQRRQVQELQGQRQEEAMK--AEKWLFECRN----------LEEKYESVTKEKER 406
Cdd:PRK04863 914 QQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQafALTEVVQRRAhfsyedaaemLAKNSDLNEKLRQR 993
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 407 LLAERDSLREANEELRCAQLQPRGLTQADPSLDPT-STPVDNLAAeiLPAELRETLLRLQLEnkrlcrQEAADRERQEEL 485
Cdd:PRK04863 994 LEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSyDAKRQMLQE--LKQELQDLGVPADSG------AEERARARRDEL 1065
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 154354985 486 QRHLEDANRARHGLETQHRLNQQQLSELRAQVEDLQKALQEQ 527
Cdd:PRK04863 1066 HARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEM 1107
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
143-585 |
1.49e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.34 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 143 QHVVMEAIQELMTKDTPDSLSPETYGNFDSQSRRYYFLSEEAEEGDELQQRCLDLERQLMLLSEEKQSLAQENAGLRERM 222
Cdd:TIGR00618 64 LNSLYAAPSEAAFAELEFSLGTKIYRVHRTLRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDYKTF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 223 GR----PEGEGTPGLTAKKLLLLQSQLEQLQEENFRLESGREDERLRCAELEREVaelqhrnqaltsLAQEAQALKDEMD 298
Cdd:TIGR00618 144 TRvvllPQGEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAEL------------LTLRSQLLTLCTP 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 299 ELRQS-SERAGQLEATLTSCRRRLGELRELRRQVRQLEERNAGHAERTRQLEDELRRAGSLRAQLEAQRRQVQELQGQRQ 377
Cdd:TIGR00618 212 CMPDTyHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 378 EEAMKAE-KWLFECRNLEEKYESVTKEKERLLAERDSLREANEELRCAQLQPRGLTQADPSLDPTSTPVDNLAAEILPAE 456
Cdd:TIGR00618 292 AAPLAAHiKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREIS 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 457 LRETLLRLQLenKRLCRQEAADRERQEELQRHLEDANRARHGLETQH---RLNQQQLSELRAQVEDLQK--ALQEQGGKT 531
Cdd:TIGR00618 372 CQQHTLTQHI--HTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTsafRDLQGQLAHAKKQQELQQRyaELCAAAITC 449
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 154354985 532 EDAISILLKRKLEEHLQKLHEADLELQRKREYIEElEPPTDSSTARRIEELQHN 585
Cdd:TIGR00618 450 TAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQ-ETRKKAVVLARLLELQEE 502
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
288-441 |
1.82e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 288 QEAQALKDEMDELRQSSERAGQLEATLTSCRRRLGELRELRRQVRQLEERN-----------AGHAERTRQLEDELRRAG 356
Cdd:PRK04863 496 DVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLgknlddedeleQLQEELEARLESLSESVS 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 357 SLRAQLEAQRRQVQELQGQRQEEAMKAEKWL----------------FECRNLEEKYESVTKEKER-LLAERDSLREANE 419
Cdd:PRK04863 576 EARERRMALRQQLEQLQARIQRLAARAPAWLaaqdalarlreqsgeeFEDSQDVTEYMQQLLEREReLTVERDELAARKQ 655
|
170 180
....*....|....*....|..
gi 154354985 420 ELrcaQLQPRGLTQADPSLDPT 441
Cdd:PRK04863 656 AL---DEEIERLSQPGGSEDPR 674
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
450-663 |
2.06e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 450 AEILPAELRETLLRLQlenkrlcrQEAADRERQEELQRHLEDAN-----RARHGLETQHRLNQQQLSELRAQVEDLQKAL 524
Cdd:TIGR02169 189 LDLIIDEKRQQLERLR--------REREKAERYQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEKLTEEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 525 QEQgGKTEDAISILLKRKLEEHLQKLHEADLELQRKreyIEELEPPTdSSTARRIEELQHNLQKKDADLRAMEERYRRYV 604
Cdd:TIGR02169 261 SEL-EKRLEEIEQLLEELNKKIKDLGEEEQLRVKEK---IGELEAEI-ASLERSIAEKERELEDAEERLAKLEAEIDKLL 335
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 154354985 605 DKARMVMQTMEPKQRPAAGAPPELHSLRTQLRERDVRIRHLEMDFEKSRSQREQEEKLL 663
Cdd:TIGR02169 336 AEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
323-410 |
2.60e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 44.30 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 323 ELRELRRQVRQLE--------ERNAGHAERTRQLEDEL----RRAGSLRAQLEAQRRQVQELQGQRQEEAMKAEKwLFEC 390
Cdd:COG0542 412 ELDELERRLEQLEiekealkkEQDEASFERLAELRDELaeleEELEALKARWEAEKELIEEIQELKEELEQRYGK-IPEL 490
|
90 100
....*....|....*....|
gi 154354985 391 RNLEEKYESVTKEKERLLAE 410
Cdd:COG0542 491 EKELAELEEELAELAPLLRE 510
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
260-567 |
4.43e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 260 EDERLRCAELEREVAElqhrnqaltslaqeaqaLKDEMDELRQSSERAGQLEATltscRRRLGELRELRRQVRQL-EERN 338
Cdd:PRK02224 471 EEDRERVEELEAELED-----------------LEEEVEEVEERLERAEDLVEA----EDRIERLEERREDLEELiAERR 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 339 AGHAERTRQLEDELRRAGSLRAQLEAQRRQVQELQGQRQEEAMKAEKwlfecrnLEEKYESVTKEKERLLAERDSLREan 418
Cdd:PRK02224 530 ETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAE-------LNSKLAELKERIESLERIRTLLAA-- 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 419 eelrcaqlqprgltqadpsldptstpVDNLAAEIlpAELRETLLRLQLENKRLCRQEAADRERQEELQRHLEDANRarhg 498
Cdd:PRK02224 601 --------------------------IADAEDEI--ERLREKREALAELNDERRERLAEKRERKRELEAEFDEARI---- 648
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 154354985 499 leTQHRLNQQQLSELRAQVEDLQKALQEQGGKTEDAISiLLKRKLEEhLQKLHEADLELQRKREYIEEL 567
Cdd:PRK02224 649 --EEAREDKERAEEYLEQVEEKLDELREERDDLQAEIG-AVENELEE-LEELRERREALENRVEALEAL 713
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
395-627 |
5.77e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 5.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 395 EKYESVTKEKERLLAERDSLREANEEL--RCAQLQPRgLTQADPSLDPTSTPVDNLAAEIlpAELRETLLRLQLENKRLc 472
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFikRTENIEEL-IKEKEKELEEVLREINEISSEL--PELREELEKLEKEVKEL- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 473 rqeAADRERQEELQRHLEDANRARHGLETQHRLNQQQLSELRAQVEDLQKALQEQGGKTEDAIS-ILLKRKLEEHLQKLH 551
Cdd:PRK03918 234 ---EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyIKLSEFYEEYLDELR 310
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 154354985 552 EADLELQRKREYIEELEPPTD--SSTARRIEELQHNLQKKDADLRAMEERYRRYvDKARMVMQTMEPKQRPAAGAPPE 627
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKelEEKEERLEELKKKLKELEKRLEELEERHELY-EEAKAKKEELERLKKRLTGLTPE 387
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
268-598 |
8.13e-04 |
|
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: 43.11 E-value: 8.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 268 ELEREVAELQHRNQALTSLAQEAQALKDEMDELRQSSERAGQLEATLTSCRRRLGELRELrrqVRQLEERNAGHAERTRQ 347
Cdd:TIGR00606 180 SATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREI---VKSYENELDPLKNRLKE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 348 LEDELRRAGSLRAQLEAQRRQVQELQGQRQEEAMKAEKWLF----ECRNLEEKYESVTKEKERLLAerDSLREANEELRC 423
Cdd:TIGR00606 257 IEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQgtdeQLNDLYHNHQRTVREKERELV--DCQRELEKLNKE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 424 AQLQPRGLTQADPSLDPTSTPVDNLAAEILPAELRETLLRLQLENKRLcrqeaadrERQEELQRHLEDANR-ARHGLETQ 502
Cdd:TIGR00606 335 RRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGF--------ERGPFSERQIKNFHTlVIERQEDE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 503 HRLNQQQLSELraqvEDLQKALQEQGGKTEDAISiLLKRKLEEHLQKLHEADLELQRKREYIEELEPPTDsstarRIEEL 582
Cdd:TIGR00606 407 AKTAAQLCADL----QSKERLKQEQADEIRDEKK-GLGRTIELKKEILEKKQEELKFVIKELQQLEGSSD-----RILEL 476
|
330
....*....|....*.
gi 154354985 583 QHNLQKKDADLRAMEE 598
Cdd:TIGR00606 477 DQELRKAERELSKAEK 492
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
455-666 |
8.63e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 8.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 455 AELRETLLRLQLENKRLCRQEAADRERQEELQRHLEDANRARHGLETQHRLNQQQLSELRAQVEDLQKALQEQGGKTEDA 534
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 535 ISILLKRKLEEHLQKLHEAD--LELQRKREYIEELEpPTDSSTARRIEELQHNLQKKDADLRAMEERYRRYVDKARMVMQ 612
Cdd:COG4942 110 LRALYRLGRQPPLALLLSPEdfLDAVRRLQYLKYLA-PARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 154354985 613 TME----PKQRPAAGAPPELHSLRTQLRERDVRIRHLEMDFEKSRSQREQEEKLLISA 666
Cdd:COG4942 189 ALEalkaERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
261-599 |
8.84e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.02 E-value: 8.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 261 DERLRCAELEREVAELQHRNQALTslaQEAQALKDEMDELRQSSERAGQLEatltSCRRRLGELRE-LRRQVRQLEERNA 339
Cdd:COG3096 303 EEQYRLVEMARELEELSARESDLE---QDYQAASDHLNLVQTALRQQEKIE----RYQEDLEELTErLEEQEEVVEEAAE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 340 GHAERTRQLEDELRRAGSLRAQL--------EAQRRQVQELQG-QRQEEAmkaeKWLFECRNLE----EKYESVTKEKER 406
Cdd:COG3096 376 QLAEAEARLEAAEEEVDSLKSQLadyqqaldVQQTRAIQYQQAvQALEKA----RALCGLPDLTpenaEDYLAAFRAKEQ 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 407 LLAERdsLREANEELRCAQLQPRGLTQADPSLDPTSTPVDNLAA---------------------EILPAELRETLLRLQ 465
Cdd:COG3096 452 QATEE--VLELEQKLSVADAARRQFEKAYELVCKIAGEVERSQAwqtarellrryrsqqalaqrlQQLRAQLAELEQRLR 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 466 LEN------KRLCRQEAADRERQEELQRHLEDANRARHGLETQHRLNQQQLSELRAQVEDLQKALQEQGGK-----TEDA 534
Cdd:COG3096 530 QQQnaerllEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawlAAQD 609
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 154354985 535 ISILLKRKLEEHLQKLHEADLELQRKREYIEELEPPTDSSTARR------IEELQHNLQKKDADLRAMEER 599
Cdd:COG3096 610 ALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKqalesqIERLSQPGGAEDPRLLALAER 680
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
260-603 |
8.86e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.58 E-value: 8.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 260 EDERLRCAELEREVAELQHRNQALTslaQEAQALKDEMDELRQSSERAGQLEATLTSCRRRLGELRELRRQVRQLEER-- 337
Cdd:PRK01156 207 ADDEKSHSITLKEIERLSIEYNNAM---DDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERhm 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 338 ----NAGHAERTR---------QLEDELRRAGSLRAQL---EAQRRQVQELQGQRQE-EAMKAE-----KWLFECRNLEE 395
Cdd:PRK01156 284 kiinDPVYKNRNYindyfkyknDIENKKQILSNIDAEInkyHAIIKKLSVLQKDYNDyIKKKSRyddlnNQILELEGYEM 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 396 KYESVTKEKERLLAERDSLREANEELRCAQLQPRGLTQADPsldptstpvdnlaaEILPAELRETLLRLQLENKRLcrqe 475
Cdd:PRK01156 364 DYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDP--------------DAIKKELNEINVKLQDISSKV---- 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 476 AADRERQEELQRHLEDANRARHGLETQHRLNQQQLSELRAQVEDLQKALQEQGGKTEDAIsillkRKLEEHLQKLHEADL 555
Cdd:PRK01156 426 SSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKI-----REIEIEVKDIDEKIV 500
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 154354985 556 ELQRKREYIEELEPPTDSSTARRIEELQHNLQKKDADLRAMEERYRRY 603
Cdd:PRK01156 501 DLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKY 548
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
188-615 |
9.37e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 9.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 188 DELQQRCLDLERQLMLLSEEKQSLAQENAGLRERMgrpegegtpgltakkllllqsqleqlqeenfrlesgrederlrcA 267
Cdd:TIGR02169 705 DELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL--------------------------------------------E 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 268 ELEREVAELQhrnQALTSLAQEAQALKDEMDELRqssERAGQLEATLTSCRRRLGE--LRELRRQVRQLEERNAGHAERT 345
Cdd:TIGR02169 741 ELEEDLSSLE---QEIENVKSELKELEARIEELE---EDLHKLEEALNDLEARLSHsrIPEIQAELSKLEEEVSRIEARL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 346 RQLEDELRRAGSLRAQLEAQRrqvQELQGQRQEeamkaekwlfecrnLEEKYESVTKEKERLLAErdsLREANEELRCAQ 425
Cdd:TIGR02169 815 REIEQKLNRLTLEKEYLEKEI---QELQEQRID--------------LKEQIKSIEKEIENLNGK---KEELEEELEELE 874
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 426 LQPRgltqadpsldptstpvdnlaaeilpaELRETLLRLQLENKRLCRQEAADRERQEELQRHLEDANRARHGLETQHRL 505
Cdd:TIGR02169 875 AALR--------------------------DLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA 928
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 506 NQQQLSELraqvEDLQKALQEQGGKTEDAISILLKR-KLEEHLQKLHEADLELqrkreyIEELEpptdsSTARRIEELQH 584
Cdd:TIGR02169 929 LEEELSEI----EDPKGEDEEIPEEELSLEDVQAELqRVEEEIRALEPVNMLA------IQEYE-----EVLKRLDELKE 993
|
410 420 430
....*....|....*....|....*....|..
gi 154354985 585 NLQKKDADLRAMEERYRRYVDKARMV-MQTME 615
Cdd:TIGR02169 994 KRAKLEEERKAILERIEEYEKKKREVfMEAFE 1025
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
381-596 |
1.47e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 381 MKAEKWLFECRNLEEKYESVTKEKERLLAERDSLREANEELRCAQLQPRGLTQADPSLDPTSTPVDNLAAEILPAELRET 460
Cdd:COG4717 40 LAFIRAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 461 LLRLQLENKRLCRQEAADRERQEELQRHLEDANRARHGLETQHRLNQQQLSELRAQVEDLQKALQEQGGKTEDAISILLK 540
Cdd:COG4717 120 KLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 154354985 541 RkLEEHLQKLHEADLELQRKREYIEELEPPTDS-STARRIEELQHNLQKKDADLRAM 596
Cdd:COG4717 200 E-LEELQQRLAELEEELEEAQEELEELEEELEQlENELEAAALEERLKEARLLLLIA 255
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
269-662 |
1.56e-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: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 269 LEREVAELQHRNQALTSLAQEAQALKDEMD-ELRQSserAGQLEATLTSCRRRLGELRELRRQVRQLEERNAGHAERTRQ 347
Cdd:pfam15921 76 IERVLEEYSHQVKDLQRRLNESNELHEKQKfYLRQS---VIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 348 ledELRRAGSLRAQ-LEAQRRQVQELQgqrqEEAMKAEKWLFECRNLEEKYESVTKEKerlLAERDSLreaneelrcAQL 426
Cdd:pfam15921 153 ---ELEAAKCLKEDmLEDSNTQIEQLR----KMMLSHEGVLQEIRSILVDFEEASGKK---IYEHDSM---------STM 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 427 QPRGLTQA-DPSLDPTSTPVDNLAAEILPAELRETLLRLQLENK-RLCRQEAADR------ERQEELQRHLEDANRAR-- 496
Cdd:pfam15921 214 HFRSLGSAiSKILRELDTEISYLKGRIFPVEDQLEALKSESQNKiELLLQQHQDRieqlisEHEVEITGLTEKASSARsq 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 497 -HGLETQHRLNQQQ-----------LSELRAQVEDLQKALQEQGGKTEDaisillkrKLEEHLQKLHEADLELQRKREYI 564
Cdd:pfam15921 294 aNSIQSQLEIIQEQarnqnsmymrqLSDLESTVSQLRSELREAKRMYED--------KIEELEKQLVLANSELTEARTER 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 565 EELEPPTdSSTARRIEELQHNLQKKDADLRAMEERYRRYVDKarmvmqtmepkqrpAAGAPPELHSLRTQLRERDVRIRH 644
Cdd:pfam15921 366 DQFSQES-GNLDDQLQKLLADLHKREKELSLEKEQNKRLWDR--------------DTGNSITIDHLRRELDDRNMEVQR 430
|
410 420
....*....|....*....|
gi 154354985 645 LE--MDFEKSRSQREQEEKL 662
Cdd:pfam15921 431 LEalLKAMKSECQGQMERQM 450
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
262-501 |
1.87e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 262 ERLRCAELEREVAELQHRNQALTSLAQEAQALKDEMDELRQSSERAGQLEATLTSCRRRLGELRELRRQVRQLEERNAGH 341
Cdd:COG1196 575 TFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGE 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 342 AERTRQLEDELRRAGSLRAQLEAQRRQVQELQGQRQEEAMKAEKWLfecRNLEEKYESVTKEKERLLAERDSLREANEEL 421
Cdd:COG1196 655 GGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL---AEEEEERELAEAEEERLEEELEEEALEEQLE 731
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 422 RcaQLQPRGLTQADPSLDPTSTPVDNLAAEILPAELRETLLRLQLENKRLCR------QEAAD-RERQEELQRHLEDANR 494
Cdd:COG1196 732 A--EREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPvnllaiEEYEElEERYDFLSEQREDLEE 809
|
....*..
gi 154354985 495 ARHGLET 501
Cdd:COG1196 810 ARETLEE 816
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
150-538 |
2.13e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 150 IQELMTKDTPDSLSPETYGNFDSQSRRYYFLSEEA--EEGDELQQRCLDLERQLMLLSEEKQSLAQENAGLRERMGRPEG 227
Cdd:PRK01156 372 IESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAikKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNG 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 228 EGTPGLTAKKLLLLQSQLEQLQEENfrlESGREDERLRcaELEREVAELQHRNQALTSLaqEAQALKDEMDELRQSSERA 307
Cdd:PRK01156 452 QSVCPVCGTTLGEEKSNHIINHYNE---KKSRLEEKIR--EIEIEVKDIDEKIVDLKKR--KEYLESEEINKSINEYNKI 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 308 GQLEATLTSCRRRLGELRELRRQVRQLEER-NAGHAERTRQLEDELRRAGSLRA--QLEAQRRQVQELQGQRQEeamkAE 384
Cdd:PRK01156 525 ESARADLEDIKIKINELKDKHDKYEEIKNRyKSLKLEDLDSKRTSWLNALAVISliDIETNRSRSNEIKKQLND----LE 600
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 385 KWLFECRNLEEKYESVTKekerllaerDSLREANEELRCAQLQPRGLTQADPSLDPTSTPVDNLAAEIlpAELRETLLRL 464
Cdd:PRK01156 601 SRLQEIEIGFPDDKSYID---------KSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQI--AEIDSIIPDL 669
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 154354985 465 QLENKRLCRQEaadrERQEELQRHLEDANRARHGLETQHRLNQQQLSELRAQVEDLQKALqEQGGKTEDAISIL 538
Cdd:PRK01156 670 KEITSRINDIE----DNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETL-ESMKKIKKAIGDL 738
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
343-525 |
2.69e-03 |
|
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: 40.88 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 343 ERTRQLEDELRRAGSLRAQLEAQRRQVQELQG---------QRQEEAMKAEKWLFECRNLEEKYESVTKEKERLLAERDS 413
Cdd:pfam05557 380 ERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGgykqqaqtlERELQALRQQESLADPSYSKEEVDSLRRKLETLELERQR 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 414 LREANEELRcAQLQPRGLTQadpSLDPTSTPV----DNLAAEILPAeLRETLLRLQLENKRLcrqeaadRERQEELQRHL 489
Cdd:pfam05557 460 LREQKNELE-MELERRCLQG---DYDPKKTKVlhlsMNPAAEAYQQ-RKNQLEKLQAEIERL-------KRLLKKLEDDL 527
|
170 180 190
....*....|....*....|....*....|....*.
gi 154354985 490 EDANRARhglETQHRLNQQQLSELRAQVEDLQKALQ 525
Cdd:pfam05557 528 EQVLRLP---ETTSTMNFKEVLDLRKELESAELKNQ 560
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
172-419 |
3.03e-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: 40.88 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 172 SQSRRYYFLSEEAEEGDELQQRCLDLERQLMLLSEEKQSLAQENAGLRERMGRPEGEGtpgltakkllllqsqlEQLQEE 251
Cdd:pfam17380 375 SRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEA----------------RQREVR 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 252 NFRLESGREDERLRCAELEREvaelqhrnqaltslaqeaqalkDEMDELRQSSERAGQLEATLTSCRRRLGELRELRRQV 331
Cdd:pfam17380 439 RLEEERAREMERVRLEEQERQ----------------------QQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKI 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 332 RQLEERnaghaERTRQLEDELRRAGSLRAQLEAQRRQVQELQGQRQ-EEAMKAEKWLFECRNLEEKYESVTKEKERLLA- 409
Cdd:pfam17380 497 LEKELE-----ERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREaEEERRKQQEMEERRRIQEQMRKATEERSRLEAm 571
|
250
....*....|..
gi 154354985 410 --ERDSLREANE 419
Cdd:pfam17380 572 erEREMMRQIVE 583
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
299-645 |
3.26e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 299 ELRQSSERAGQLEATLTSCRRRLGELRE-LRRQVRQLEErnagHAERTRQLEDELRRAGSLRAQLEAQRRQvQELQGQRQ 377
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQLAAEQYrLVEMARELAE----LNEAESDLEQDYQAASDHLNLVQTALRQ-QEKIERYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 378 EEAMKAEKwlfecrNLEEKYESVTKEKERLLAERDSLREANEELRCAQ------------LQPRGL--TQADPSLDPTST 443
Cdd:PRK04863 355 ADLEELEE------RLEEQNEVVEEADEQQEENEARAEAAEEEVDELKsqladyqqaldvQQTRAIqyQQAVQALERAKQ 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 444 -------PVDNLAA--EILPAELRE-TLLRLQLENKRLCRQEAADR-ERQEELQRHL------EDANRARHGLETQHRLN 506
Cdd:PRK04863 429 lcglpdlTADNAEDwlEEFQAKEQEaTEELLSLEQKLSVAQAAHSQfEQAYQLVRKIagevsrSEAWDVARELLRRLREQ 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 507 Q---QQLSELRAQVEDLQKALQEQggktEDAISIL--LKRKLEEHLQKLHEADLELQRKREYIEELEPPTDSSTARRIEE 581
Cdd:PRK04863 509 RhlaEQLQQLRMRLSELEQRLRQQ----QRAERLLaeFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMAL 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 582 LQH--NLQKKDADLRAMEERYRRYVDK--------------ARMVMQTMEPKQRPAAGAPPELHSLRTQLRERDVRIRHL 645
Cdd:PRK04863 585 RQQleQLQARIQRLAARAPAWLAAQDAlarlreqsgeefedSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERL 664
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
267-378 |
3.60e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 267 AELEREVAELQhrnQALTSLAQEAQALKDEMDELRQS-SERAGQLEATLTSCRRRL-GELRELRRQVRQLEERnaghAER 344
Cdd:COG3206 273 AELEAELAELS---ARYTPNHPDVIALRAQIAALRAQlQQEAQRILASLEAELEALqAREASLQAQLAQLEAR----LAE 345
|
90 100 110
....*....|....*....|....*....|....
gi 154354985 345 TRQLEDELRRagsLRAQLEAQRRQVQELQGQRQE 378
Cdd:COG3206 346 LPELEAELRR---LEREVEVARELYESLLQRLEE 376
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
366-667 |
4.93e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 366 RRQVQELQGQRQEeamkaekwlfecrnLEEKYESVTKEKERLLAERDSLREANEELRcaQLQPRGLTQADpsldptstpV 445
Cdd:COG4913 609 RAKLAALEAELAE--------------LEEELAEAEERLEALEAELDALQERREALQ--RLAEYSWDEID---------V 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 446 DNLAAEIlpAELRETLLRLQLEN---KRLCRQEAADRERQEELQRHLEDANRARHGLETQHRLNQQQLSELRAQVEDLQK 522
Cdd:COG4913 664 ASAEREI--AELEAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 523 ALQEQggktedaisillkrkleehlqklHEADLELQRKREYIEELEPPTDSSTARRIEELQhnlQKKDADLRAMEERYRR 602
Cdd:COG4913 742 LARLE-----------------------LRALLEERFAAALGDAVERELRENLEERIDALR---ARLNRAEEELERAMRA 795
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 154354985 603 YVDKARMVMQTMepkqRPAAGAPPELHSLRTQLRERDVrIRHLEmDFEKSRSQREQEEKLLISAW 667
Cdd:COG4913 796 FNREWPAETADL----DADLESLPEYLALLDRLEEDGL-PEYEE-RFKELLNENSIEFVADLLSK 854
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
254-422 |
5.71e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 254 RLESGREDERLRCAELEREVAELQHRNQALTSLAQEAQALKDEMDELRQSSERAGQLEATLTSCRRRLGELRELRRQVRQ 333
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 334 LEERNAGHAERTRQLEDELRRAGSLRAQLEAQRRQVQELQGQRQEEAMKAEKWLFECR---------NL--EEKYESVTK 402
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEreiealgpvNLlaIEEYEELEE 795
|
170 180
....*....|....*....|
gi 154354985 403 EKERLLAERDSLREANEELR 422
Cdd:COG1196 796 RYDFLSEQREDLEEARETLE 815
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
260-421 |
6.39e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 6.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 260 EDERLRCAELEREVAELQHRNQALTSLAQEAQALKDEMDELRQSSERAGQLEATLTSCRRRLGELRElrrQVRQLEERNA 339
Cdd:PRK02224 568 EEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRE---RKRELEAEFD 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 340 GhaERTRQLEDELRRAGSLRAQLEAQRRQVQELQGQRQEEAMKAEKWLFECRNLEEKYESVTKEKERLlaerDSLREANE 419
Cdd:PRK02224 645 E--ARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEAL----EALYDEAE 718
|
..
gi 154354985 420 EL 421
Cdd:PRK02224 719 EL 720
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
267-609 |
6.95e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.95 E-value: 6.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 267 AELEREVAELQHRNQALTSLAQEAQALKDEMDELRQSSERAGQLEaTLTSCRRRLGELRELRRQVRQLEeRNAGHAERTR 346
Cdd:TIGR00618 226 KELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIE-ELRAQEAVLEETQERINRARKAA-PLAAHIKAVT 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 347 QLED-------ELRRAGSLRAQLEAQRRQVQELQGQRQEEAMKAEKWLFECRNLEEKYESVTKEKErllaERDSLREANE 419
Cdd:TIGR00618 304 QIEQqaqrihtELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIRE----ISCQQHTLTQ 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 420 ELRCAQLQPRGLTQADPSLDPTSTPVDNLAAEILPAELRETLLRLQLenkrlcrqeaADRERQEELQRhledanrarhgl 499
Cdd:TIGR00618 380 HIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQL----------AHAKKQQELQQ------------ 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 500 etQHRLNQQQLSELRAQVEDLQKALQEQGGKTEDAISILLKRKLEEHLQKLHEADLELQRKREYIEE------------- 566
Cdd:TIGR00618 438 --RYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEpcplcgscihpnp 515
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 154354985 567 -----LEPPTDSSTARRIEELQHNLQKKDADLRAM--EERYRRYVDKARM 609
Cdd:TIGR00618 516 arqdiDNPGPLTRRMQRGEQTYAQLETSEEDVYHQltSERKQRASLKEQM 565
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
286-520 |
8.54e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 39.55 E-value: 8.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 286 LAQEAQALKDEMDELRQSSERAGQLEATLTSCRRRLGELRELRRQVRQLEErnAGHAERTRQLEDELRRAGSLRAQLEAQ 365
Cdd:COG3096 838 LAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLAD--ETLADRLEELREELDAAQEAQAFIQQH 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 366 RRQVQELQGQrqeeamkaekwLFECRNLEEKYESVTKEKERLLAERDSLR---EANEELRcAQLQPRGLTQADPSLDPTS 442
Cdd:COG3096 916 GKALAQLEPL-----------VAVLQSDPEQFEQLQADYLQAKEQQRRLKqqiFALSEVV-QRRPHFSYEDAVGLLGENS 983
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 154354985 443 TPVDNLaaeilpaelretllRLQLENKRLCRQEAadRERQEELQRHLEDANRARHGLETQHRLNQQQLSELRAQVEDL 520
Cdd:COG3096 984 DLNEKL--------------RARLEQAEEARREA--REQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEEL 1045
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
254-527 |
8.67e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 39.11 E-value: 8.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 254 RLESGREDERLRCAELEREVAELQhrnQALTSLAQEAQALKDEMDELRQSSERAGQLEATLTSCR-RRLGELRELRRQVR 332
Cdd:pfam07888 63 RYKRDREQWERQRRELESRVAELK---EELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRaAHEARIRELEEDIK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 333 QLEERNAGHAERTRQLEDELRRAGSLRAQLEAQRRQVQELQGQRQEEAMKAEKWLFECRN-LEEKYESVTKEKERLLAER 411
Cdd:pfam07888 140 TLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNsLAQRDTQVLQLQDTITTLT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154354985 412 DSLREAN----------EELRCAQ----LQPRGLTQADPSLDPTSTPVDNLAAEILPAELRETLLRLQLENKRLCRQEAA 477
Cdd:pfam07888 220 QKLTTAHrkeaeneallEELRSLQerlnASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGR 299
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 154354985 478 DRERQEelqrhledanraRHGLETQHRLNQQQLSELRAQVEDLQKALQEQ 527
Cdd:pfam07888 300 ARWAQE------------RETLQQSAEADKDRIEKLSAELQRLEERLQEE 337
|
|
| |
