|
Name |
Accession |
Description |
Interval |
E-value |
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
179-689 |
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: 538.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 179 FLSEEVEEGDHLQQHYLDLERQLLLLSEEKQNLAQENAALRERVGRSEVESAPG-LTAKKLLLLQSQLEQLQEENFRLES 257
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGtPGGKKYLLLQKQLEQLQEENFRLET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 258 SREDDRLRCLELEREVAELQQRNQALTSLSQEAQALKDEMDELRQSSERARQLEATLNSCRRRLGELQELRRQVRQLEER 337
Cdd:pfam05622 81 ARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLGDLRRQVKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 338 NAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTERDSLREA 417
Cdd:pfam05622 161 NAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRET 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 418 NEELRCAQLQPRGLAQADLSLDPTPSGLENLAAEILPAELRETLVRLQLENKRL-CQQEAADRERQEELQRHLEEANRAR 496
Cdd:pfam05622 241 NEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLrLGQEGSYRERLTELQQLLEDANRRK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 497 HGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTED-------------KLHEADLELQRKREYIEELEPPTDSSTARR 563
Cdd:pfam05622 321 NELETQNRLANQRILELQQQVEELQKALQEQGSKAEDssllkqkleehleKLHEAQSELQKKKEQIEELEPKQDSNLAQK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 564 IEELQDSLQKKDADLRAMEERYRRYVDKARTVIQTLEPKQRPptVVSPEFHTLRSQLWERNLRIRQMEMDYEKSRRRQEQ 643
Cdd:pfam05622 401 IDELQEALRKKDEDMKAMEERYKKYVEKAKSVIKTLDPKQNP--ASPPEIQALKNQLLEKDKKIEHLERDFEKSKLQREQ 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1732634088 644 EEKLLISAWYSMGMALEHRAGEEHAP---AHAQSFLAQQRLATNARRGP 689
Cdd:pfam05622 479 EEKLIVTAWYNMGMALHRKAIEERLAglsSPGQSFLARQRQATNARRGL 527
|
|
| HkD_Hook2 |
cd22227 |
Hook domain found in protein Hook 2 (Hook2) and similar proteins; Hook2 is a ... |
7-156 |
9.79e-88 |
|
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: 271.36 E-value: 9.79e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 7 ELCGSLLTWLQTFQVSPPCASPQDLSSGLAIAHVLNQIDPSWFNNEWLQGISEDSSPSWRLKVRKLEKILQSLVEYSKNV 86
Cdd:cd22227 1 ELCDSLLTWLQTFQVPSPCSSYQDLTSGVAIAQVLNRIDPSWFNEAWLGRIKEDTGDNWRLKVSNLKKILQSLLEYYQDV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 87 LGHPVSDQHLPDVSLIGEFSNPAELGKLLQLVLGCAISCEKKQEYIQRIMTLEESVQHVVMEAIQELMTK 156
Cdd:cd22227 81 LGHQVSEDHLPDVNLIGEFSDDTELGKLLQLVLGCAISCEKKQEHIQQIMTLEESVQHVVMEAIQELLTK 150
|
|
| HOOK_N |
pfam19047 |
HOOK domain; This domain is found at the N-terminus of HOOK proteins. |
7-157 |
3.10e-86 |
|
HOOK domain; This domain is found at the N-terminus of HOOK proteins.
Pssm-ID: 465958 Cd Length: 151 Bit Score: 267.74 E-value: 3.10e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 7 ELCGSLLTWLQTFQVSPPCASPQDLSSGLAIAHVLNQIDPSWFNNEWLQGISEDSSPSWRLKVRKLEKILQSLVEYSKNV 86
Cdd:pfam19047 1 ELCDSLLTWLQTFNVPAPCATVEDLTDGVAMAQVLHQIDPSWFTEAWLSRIKEDVGDNWRLKVSNLKKILQSVVDYYQDV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1732634088 87 LGHPVSDQHLPDVSLIGEFSNPAELGKLLQLVLGCAISCEKKQEYIQRIMTLEESVQHVVMEAIQELMTKD 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 |
2.27e-75 |
|
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: 239.07 E-value: 2.27e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 9 CGSLLTWLQTFQVSPPCASPQDLSSGLAIAHVLNQIDPSWFNNEWLQGISEDSSPSWRLKVRKLEKILQSLVEYSKNVLG 88
Cdd:cd22222 1 CDSLLQWLQTFNLIAPHATAEDLSDGVAIAQVLNQIDPEYFSDSWLSKIKPDVGDNWRLKVSNLKKILKGIVDYYSEVLG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1732634088 89 HPVSDQHLPDVSLIGEFSNPAELGKLLQLVLGCAISCEKKQEYIQRIMTLEESVQHVVMEAIQELMT 155
Cdd:cd22222 81 QQISGFTMPDVNAIAEKEDPKELGRLLQLVLGCAVNCERKEEYIQAIMGLEESVQHVVMEAIQELMS 147
|
|
| HkD_Hook3 |
cd22226 |
Hook domain found in protein Hook 3 (Hook3) and similar proteins; Hook3 is an adaptor protein ... |
4-156 |
4.78e-63 |
|
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: 206.74 E-value: 4.78e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 4 DKAELCGSLLTWLQTFQVSPPCASPQDLSSGLAIAHVLNQIDPSWFNNEWLQGISEDSSPSWRLKVRKLEKILQSLVEYS 83
Cdd:cd22226 1 DRAELCESLLTWIQTFNVDAPCQTVEDLTSGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1732634088 84 KNVLGHPVSDQHLPDVSLIGEFSNPAELGKLLQLVLGCAISCEKKQEYIQRIMTLEESVQHVVMEAIQELMTK 156
Cdd:cd22226 81 HEILGQQINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMSK 153
|
|
| HkD_Hook1 |
cd22225 |
Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a ... |
8-157 |
4.85e-63 |
|
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: 206.63 E-value: 4.85e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 8 LCGSLLTWLQTFQVSPPCASPQDLSSGLAIAHVLNQIDPSWFNNEWLQGISEDSSPSWRLKVRKLEKILQSLVEYSKNVL 87
Cdd:cd22225 1 LCDSLIIWLQTFNTAAPCQTVQDLTSGVAMAQVLHQIDSSWFDESWLSRIKEDVGDNWRIKMSNLKKILQGIVDYYHEFL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 88 GHPVSDQHLPDVSLIGEFSNPAELGKLLQLVLGCAISCEKKQEYIQRIMTLEESVQHVVMEAIQELMTKD 157
Cdd:cd22225 81 DQQISEFLLPDLNRIAEHSDPVELGRLLQLILGCAVNCEKKQEHIQNIMTLEESVQHVVMTAIQELMSKE 150
|
|
| HkD_SF |
cd22211 |
Hook domain-containing proteins superfamily; The Hook domain superfamily includes Hook adaptor ... |
11-154 |
4.40e-50 |
|
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: 171.30 E-value: 4.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 11 SLLTWLQTFQVSPPCASPQDLSSGLAIAHVLNQIDPSWFNNEWLQgiSEDSSPSWRLKVRKLEKILQSLVEYSKNVLGHP 90
Cdd:cd22211 3 ALLAWINTFPLSSPVESLDDLSDGVVLAEILSQIDPSYFDSEWLE--SRDSSDNWVLKLNNLKKLYRSLSKYYREVLGQQ 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1732634088 91 VSDQHLPDVSLIGEFSNPAELGKLLQLVLGCAISCEKKQEYIQRIMTLEESVQHVVMEAIQELM 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 |
6.77e-24 |
|
Hook domain found in the Hook-related protein (HkRP) family; The HkRP family includes Daple, Girdin and Gipie. Daple, also called Dvl-associating protein with a high frequency of leucine residues, or coiled-coil domain-containing protein 88C (CCDC88C), or Hook-related protein 2 (HkRP2), is a novel non-receptor nucleotide exchange factor (GEF) required for activation of guanine nucleotide-binding proteins (G-proteins) during non-canonical Wnt signaling. Girdin, also called Akt phosphorylation enhancer (APE), or coiled-coil domain-containing protein 88A (CCDC88A), or G alpha-interacting vesicle-associated protein (GIV), or Girders of actin filament, or Hook-related protein 1 (HkRP1), is a bifunctional modulator of guanine nucleotide-binding proteins (G proteins). It acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein G(i) alpha subunits. It also acts as a guanine nucleotide dissociation inhibitor for guanine nucleotide-binding protein G(s) subunit alpha GNAS. In addition, Girdin plays an essential role in cell migration. Gipie, also called GRP78-interacting protein induced by ER stress, or coiled-coil domain-containing protein 88B (CCDC88B), or brain leucine zipper domain-containing protein, or Hook-related protein 3 (HkRP3), is a novel actin cytoskeleton-binding protein and Akt substrate that regulates cell migratory responses in various biological contexts. It acts as a positive regulator of T-cell maturation and inflammatory function. As a microtubule-binding protein, Gipie regulates lytic granule clustering and NK cell killing. All family members contain a conserved globular Hook domain which folds as a variant of the helical calponin homology (CH) domain.
Pssm-ID: 411794 Cd Length: 149 Bit Score: 98.05 E-value: 6.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 8 LCGSLLTWLQTFQVSPPCA-SPQDLSSGLAIAHVLNQIDPSWFNnewlQGISEDSSPSWRLKVRKLEKILQSLVEYSKNV 86
Cdd:cd22223 2 LSSPLVTWAKTFADDGSAElSYTDLVDGVFLNNVMLQIDPRPFS----EVSNRNVDDDVNARIQNLDLLLRNIKSFYQEV 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1732634088 87 LGHPVSdQHLPDVSLIGEFSNP----AELGKLLQLVLGCAISCEKKQEYIQRIMTLEESVQHVVMEAIQEL 153
Cdd:cd22223 78 LQQLIV-MKLPDILTIGREPESeqslEELEKLLLLLLGCAVQCERKEEFIERIKNLDLEVQHALVACIQEV 147
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
254-583 |
7.26e-14 |
|
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: 75.48 E-value: 7.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 254 RLESSREDDRLR--CLELEREVAELQQrnqALTSLSQEAQALKDEMDELRQSSERA-RQLEATLNSCRRRLGELQELRRQ 330
Cdd:TIGR02168 672 ILERRREIEELEekIEELEEKIAELEK---ALAELRKELEELEEELEQLRKELEELsRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 331 VRQLEERNAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEkwlfecRNLEEKCDLVTKEKERLLTE 410
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR------EALDELRAELTLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 411 RDSLREANEELRCAQLQPRGLAQ--ADLSLDPTPSGLENLAAEILPAELRETLVRLQLENKRLCQQEAADRERQEELQRH 488
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEqiEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 489 LEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQggktEDKLHEadlELQRKREYIEELEPPTDSSTA---RRIE 565
Cdd:TIGR02168 903 LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL----QERLSE---EYSLTLEEAEALENKIEDDEEearRRLK 975
|
330
....*....|....*....
gi 1732634088 566 ELQDSLQK-KDADLRAMEE 583
Cdd:TIGR02168 976 RLENKIKElGPVNLAAIEE 994
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
324-701 |
2.09e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.82 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 324 LQELRRQVRQLeERNAGHAERTRQLEEEL--RRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKcdlVT 401
Cdd:COG1196 195 LGELERQLEPL-ERQAEKAERYRELKEELkeLEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE---LE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 402 KEKERLLTERDSLREANEELRcaqlqprglaqadlsldptpsgleNLAAEIlpAELRETLVRLQLENKRLCQQEAADRER 481
Cdd:COG1196 271 ELRLELEELELELEEAQAEEY------------------------ELLAEL--ARLEQDIARLEERRRELEERLEELEEE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 482 QEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDKLHEADLELQRKREYIEELEpptdsSTA 561
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA-----ELA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 562 RRIEELQDSLQKKDADLRAMEERYRRYVDKARTVIQTLEPKQRpptvvspEFHTLRSQLWERNLRIRQMEMDYEKSRRRQ 641
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE-------ALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 642 EQEEKLLISAWYSMGMALEHRAGEEHAPAHAQSFLAQQRLATNARRGPLGRQALSLRPTD 701
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
|
| HkD_Daple |
cd22228 |
Hook domain found in Daple (Dvl-associating protein with a high frequency of leucine residues) ... |
12-153 |
4.93e-13 |
|
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: 67.26 E-value: 4.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 12 LLTWLQTFQvspPCASPQ--------DLSSGLAIAHVLNQIDPSWFNnewlQGISEDSSPSWRLKVRKLEKILQSLVEYS 83
Cdd:cd22228 6 LVTWVKTFG---PLGFGSedklsmymDLVDGVFLNKIMLQIDPRPTN----QRVNKHVNNDVNLRIQNLTILVRHIKTYY 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1732634088 84 KNVLGHPVSdQHLPDVSLIGEfsNP------AELGKLLQLVLGCAISCEKKQEYIQRIMTLEESVQHVVMEAIQEL 153
Cdd:cd22228 79 QEVLQQLIV-MNLPNVLMIGK--DPlsgksmEEIKKMLLLVLGCAVQCERKEEFIERIKQLDIETQAAIVSHIQEV 151
|
|
| HkD_Girdin |
cd22229 |
Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation ... |
12-153 |
2.60e-12 |
|
Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation enhancer (APE), or coiled-coil domain-containing protein 88A (CCDC88A), or G alpha-interacting vesicle-associated protein (GIV), or Girders of actin filament, or Hook-related protein 1 (HkRP1), is a bifunctional modulator of guanine nucleotide-binding proteins (G proteins). It acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein G(i) alpha subunits. It also acts as a guanine nucleotide dissociation inhibitor for guanine nucleotide-binding protein G(s) subunit alpha GNAS. In addition, Girdin plays an essential role in cell migration.
Pssm-ID: 411800 Cd Length: 156 Bit Score: 65.20 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 12 LLTWLQTFQVSPPCASPQ-----DLSSGLAIAHVLNQIDPSWFNNEWLQGISEDSSpswrLKVRKLEKILQSLVEYSKNV 86
Cdd:cd22229 9 LVTWVKTFGPLATGNGTPldeyvALVDGVFLNEVMLQINPKSSNQRVNKKVNNDAS----LRIQNLSILVKQIKLYYQET 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1732634088 87 LGHPVSdQHLPDVSLIGE--FSNPA--ELGKLLQLVLGCAISCEKKQEYIQRIMTLEESVQHVVMEAIQEL 153
Cdd:cd22229 85 LQQLIM-MSLPNVLVLGRnpLSEQGteEMKKLLLLLLGCAVQCERKEEFIERIQTLDFDTKAAVAAHIQEV 154
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
255-525 |
3.49e-12 |
|
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: 70.10 E-value: 3.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 255 LESSREDDRLRCLELEREVAELQQRNQALTSlsQEAQALKDEMDELrqSSERArQLEATLNSCRRRLGELQELRRQ-VRQ 333
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGE--EEQLRVKEKIGEL--EAEIA-SLERSIAEKERELEDAEERLAKlEAE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 334 LEERNAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTERDS 413
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 414 LREANEELRCAQLQPRG-LAQADLSLDPTPSGLENLAAEIlpAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEA 492
Cdd:TIGR02169 411 LQEELQRLSEELADLNAaIAGIEAKINELEEEKEDKALEI--KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKL 488
|
250 260 270
....*....|....*....|....*....|...
gi 1732634088 493 NRARHGLEAQQRLNQQQLSELRAQVEELQKALQ 525
Cdd:TIGR02169 489 QRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
271-583 |
1.55e-11 |
|
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: 67.79 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 271 REVAELQQRNQALTSLSQEAQALKDEMDELRQsseRARQLEATLNSCRRRLGELQelrRQVRQLEERNAGHAERTRQLEE 350
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIEN---RLDELSQELSDASRKIGEIE---KEIEQLEQEEEKLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 351 ELRragSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDlvtkeKERLLTERDSLREANEELRCAQLQPRG 430
Cdd:TIGR02169 745 DLS---SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS-----HSRIPEIQAELSKLEEEVSRIEARLRE 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 431 LAQADLSLDptpsgLENLAAEILPAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQL 510
Cdd:TIGR02169 817 IEQKLNRLT-----LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 511 SELRAQVEELQKALQEQGGKTEDK-LHEADLE--LQRKREYIEELEPPT-----DSSTARRIEELQDSLQKKDADLRAME 582
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQIEKKrKRLSELKakLEALEEELSEIEDPKgedeeIPEEELSLEDVQAELQRVEEEIRALE 971
|
.
gi 1732634088 583 E 583
Cdd:TIGR02169 972 P 972
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
267-542 |
3.37e-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: 67.00 E-value: 3.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 267 LELEREVAELQQRNQALTSLSQEAQALKDEMDELRQSSERAR----QLEATLNSCRrrlGELQELRRQVRQLEERNAGHA 342
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRlevsELEEEIEELQ---KELYALANEISRLEQQKQILR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 343 ERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKwlfECRNLEEKCDLVTKEKERLLTERDSLREANEELR 422
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE---ELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 423 CAQLQPRglaqadlsldptpSGLENLAAEIlpAELRETLVRLQLENKRLCQQ-----EAADRERQEELQRHLEEANRARH 497
Cdd:TIGR02168 386 SKVAQLE-------------LQIASLNNEI--ERLEARLERLEDRRERLQQEieellKKLEEAELKELQAELEELEEELE 450
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1732634088 498 GLEAQQRLNQQQLSELRAQVEELQKALQeqggKTEDKLHEADLEL 542
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQALD----AAERELAQLQARL 491
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
389-678 |
8.16e-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: 62.38 E-value: 8.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 389 ECRNLEEKCDLVTKEKERLLTERDSLREANEELRcaqlqpRGLAQADLSLDPTPSGLENLAAEIlpAELRETLVRLQLEN 468
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLR------KELEELSRQISALRKDLARLEAEV--EQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 469 KRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGK-----------------T 531
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaanlrerleslerriaaT 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 532 EDKLHEADLELQRKREYIEELEPPTDSSTArRIEELQDSLQKKDADLRAMEERYRRYVDKARTVIQTLEpkqrpptVVSP 611
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEE-LIEELESELEALLNERASLEEALALLRSELEELSEELR-------ELES 908
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1732634088 612 EFHTLRSQLWERNLRIRQMEMDYEKSR-RRQEQEEKLLISAWYSMGMALEHRAGEEHAPAHAQSFLAQ 678
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGLEvRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
180-582 |
8.25e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 8.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 180 LSEEVEEGDHLQQHYLDLERQLLLLSEEKQNLAQENAALRERVGRSEVESApgLTAKKLLLLQSQLEQLQEENFRLESSR 259
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL--EAEAELAEAEEELEELAEELLEALRAA 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 260 EDDRLRCLELEREVAELQQRNQALtsLSQEAQALKDEMDELRQSSERARQLEATLNSCRRRLGELQELRRQVRQLEERNA 339
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERL--EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 340 GHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEK------------WLFECRNLEEKC------DLVT 401
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLrglagavavligVEAAYEAALEAAlaaalqNIVV 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 402 KEKERLLTERDSLREAN----EELRCAQLQPRGLAQADLSLDPTPSGLENLAAEILPAELRETLVRLQLENKRLC----- 472
Cdd:COG1196 554 EDDEVAAAAIEYLKAAKagraTFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVaarle 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 473 -----------------------------------QQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQV 517
Cdd:COG1196 634 aalrravtlagrlrevtlegeggsaggsltggsrrELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAE 713
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1732634088 518 EELQKALQEQGGKTEDKLHEADLELQRKREYIEELEPPTDSSTAR--RIEELQDSLQKKDADLRAME 582
Cdd:COG1196 714 EERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEppDLEELERELERLEREIEALG 780
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
256-647 |
2.26e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.93 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 256 ESSREDDRLRCLELEREVAELQQRNQALTSLSQEAQAlKDEMDELRQSSERARQLEATLNSCRRRLGELQElrrqvrqle 335
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE-ARKADELKKAEEKKKADEAKKAEEKKKADEAKK--------- 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 336 ernagHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTERDSLR 415
Cdd:PTZ00121 1310 -----KAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAK 1384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 416 EANEELRCA-QLQPRGLAQADLSLDPTPSGLENLAAEILPAELREtlVRLQLENKRlcqqEAADRERQEELQRHLEEANR 494
Cdd:PTZ00121 1385 KKAEEKKKAdEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEE--KKKADEAKK----KAEEAKKADEAKKKAEEAKK 1458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 495 ARHGLEAQQRlnQQQLSELRAQVEELQKAlQEQGGKTEDKLHEADlELQRKREYIEELEPPTDSSTARRIEELQDSLQKK 574
Cdd:PTZ00121 1459 AEEAKKKAEE--AKKADEAKKKAEEAKKA-DEAKKKAEEAKKKAD-EAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAK 1534
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1732634088 575 DAD--LRAMEERYRRYVDKARTVIQTLEPKQRPPTVVSPEfhtlrsqlwERNLRIRQMEMDYEKSRRRQEQEEKL 647
Cdd:PTZ00121 1535 KADeaKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEE---------DKNMALRKAEEAKKAEEARIEEVMKL 1600
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
268-422 |
2.28e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 268 ELEREVAELQQRNQALTSLSQEAQALKDEMDELRQSSERA-----------------RQLEATLNSCRRRLGELQELRRQ 330
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLaeyswdeidvasaereiAELEAELERLDASSDDLAALEEQ 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 331 VRQLEERNAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKE-KERLLT 409
Cdd:COG4913 694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERElRENLEE 773
|
170
....*....|...
gi 1732634088 410 ERDSLREANEELR 422
Cdd:COG4913 774 RIDALRARLNRAE 786
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
268-535 |
3.15e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 268 ELEREVAELQQRNQALTSLSQEAQALKDEMDELRQsserARQLEATLNSCRRRLgELQELRRQVRQLEERNAGHAERTRQ 347
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRELAERYAAARERLAE----LEYLRAALRLWFAQR-RLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 348 LEEELRRAGSLRAQLEAQRRQvqelQGQWQEEAmkaekwlfecrnLEEKCDLVTKEKERLLTERDSLREAneelrcaqlq 427
Cdd:COG4913 314 LEARLDALREELDELEAQIRG----NGGDRLEQ------------LEREIERLERELEERERRRARLEAL---------- 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 428 prgLAQADLSLDPTPSGLENLAaeilpAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQrlnq 507
Cdd:COG4913 368 ---LAALGLPLPASAEEFAALR-----AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK---- 435
|
250 260
....*....|....*....|....*...
gi 1732634088 508 qqlSELRAQVEELQKALQEQGGKTEDKL 535
Cdd:COG4913 436 ---SNIPARLLALRDALAEALGLDEAEL 460
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
256-646 |
3.41e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.97 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 256 ESSREDDRLRCLELEREVAELQQRNQALTSLSQ----EAQALKDEMDELrqsSERARQLEATLNSCRRRLGELQE----L 327
Cdd:PRK02224 271 EREREELAEEVRDLRERLEELEEERDDLLAEAGlddaDAEAVEARREEL---EDRDEELRDRLEECRVAAQAHNEeaesL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 328 RRQVRQLEERNAGHAERTRQLEEELRRAgslRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKER- 406
Cdd:PRK02224 348 REDADDLEERAEELREEAAELESELEEA---REAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDEl 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 407 ----------LLTERDSLREAN---EELRCAQL-QPRGLAQADLSLDPTPSGLENLAAEILPAELRETLVRLQLENKRLC 472
Cdd:PRK02224 425 rereaeleatLRTARERVEEAEallEAGKCPECgQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 473 QQEAADRERQEELQRHLEEANRARHGLEAQQRLnqqQLSELRAQVEELQKALQEQGGKTEDKLHEADLELQRKREYIEEL 552
Cdd:PRK02224 505 VEAEDRIERLEERREDLEELIAERRETIEEKRE---RAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKL 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 553 EPPTDSSTA-RRIEELQDSLQKKDADLRAMEERyrryvdkaRTVIQTLEpKQRpptvvspefhtlRSQLWERNLRIRQME 631
Cdd:PRK02224 582 AELKERIESlERIRTLLAAIADAEDEIERLREK--------REALAELN-DER------------RERLAEKRERKRELE 640
|
410
....*....|....*
gi 1732634088 632 MDYEKSRRRQEQEEK 646
Cdd:PRK02224 641 AEFDEARIEEAREDK 655
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
268-527 |
1.05e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 55.73 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 268 ELEREVAELQQRNQaltSLSQEAQALKDEMDELRQSSERARQLE-----ATLNSCRRRLGELQELRRQVRQleernagHA 342
Cdd:PRK04863 848 ELERALADHESQEQ---QQRSQLEQAKEGLSALNRLLPRLNLLAdetlaDRVEEIREQLDEAEEAKRFVQQ-------HG 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 343 ERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMK--AEKWLFECRN----------LEEKCDLVTKEKERLLTE 410
Cdd:PRK04863 918 NALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQafALTEVVQRRAhfsyedaaemLAKNSDLNEKLRQRLEQA 997
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 411 RDSLREANEELRCAQLQPRGLAQADLSLDPTPSGLENLAAEiLPAELRETLVRLQLEnkrlcqQEAADRERQEELQRHLE 490
Cdd:PRK04863 998 EQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQE-LKQELQDLGVPADSG------AEERARARRDELHARLS 1070
|
250 260 270
....*....|....*....|....*....|....*..
gi 1732634088 491 EANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQ 527
Cdd:PRK04863 1071 ANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEM 1107
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
180-526 |
1.32e-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: 55.06 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 180 LSEEVEEGDHLQQHYLDLERQLLLLSEEKQnlaQENAALRERVGRSEVESAPGltAKKLLLLQSQLEQLQEENFRLESSR 259
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKELEELS---RQISALRKDLARLEAEVEQL--EERIAQLSKELTELEAEIEELEERL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 260 EDDRLRCLELEREVAELQQR-NQALTSLSQEAQALKDEMDELRQSSERARQLEATLNSCRRRLGELQ-ELRRQVRQLEER 337
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQiEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATErRLEDLEEQIEEL 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 338 NaghaERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKwlfECRNLEEKCDLVTKEKERLLTERDSLREA 417
Cdd:TIGR02168 851 S----EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS---ELEELSEELRELESKRSELRRELEELREK 923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 418 NE---------ELRCAQLQPRGLAQADLSLDPTPSGLENLAAEilPAELRETLVRLQLENKRL-------CQQEAADRER 481
Cdd:TIGR02168 924 LAqlelrleglEVRIDNLQERLSEEYSLTLEEAEALENKIEDD--EEEARRRLKRLENKIKELgpvnlaaIEEYEELKER 1001
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1732634088 482 QEELQRHLEEANRARHGLE-AQQRLNQQQLSELRAQVEELQKALQE 526
Cdd:TIGR02168 1002 YDFLTAQKEDLTEAKETLEeAIEEIDREARERFKDTFDQVNENFQR 1047
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
268-595 |
1.33e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.07 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 268 ELEREVAELQQRNQALTSLSQEAQALKDEMDELR----QSSERARQLEATLNSCRRRLGE--LQELRRQVRQLEERNAGH 341
Cdd:TIGR02169 731 EEEKLKERLEELEEDLSSLEQEIENVKSELKELEarieELEEDLHKLEEALNDLEARLSHsrIPEIQAELSKLEEEVSRI 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 342 AERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEamKAEkwlfecrnLEEKCDLVTKEKERLLTErdslreaneel 421
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ--IKS--------IEKEIENLNGKKEELEEE----------- 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 422 rcaqlqprglaqadlsldptpsgLENLAAEIlpAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEA 501
Cdd:TIGR02169 870 -----------------------LEELEAAL--RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKA 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 502 QQRLNQQQLSELraqvEELQKALQEQGGKTEDkLHEADLELQRKREYIEELEPPTD------SSTARRIEELQDSLQKKD 575
Cdd:TIGR02169 925 KLEALEEELSEI----EDPKGEDEEIPEEELS-LEDVQAELQRVEEEIRALEPVNMlaiqeyEEVLKRLDELKEKRAKLE 999
|
330 340
....*....|....*....|
gi 1732634088 576 ADLRAMEERYRRYVDKARTV 595
Cdd:TIGR02169 1000 EERKAILERIEEYEKKKREV 1019
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
268-647 |
3.36e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 3.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 268 ELEREVAELQQRNQALtslsQEAQALKDEMDELRQSSERARQLEATLNSCRRRLGEL----QELRRQVRQLEERNAGHAE 343
Cdd:COG4717 99 ELEEELEELEAELEEL----REELEKLEKLLQLLPLYQELEALEAELAELPERLEELeerlEELRELEEELEELEAELAE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 344 RTRQLEEELRRAG-SLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERlLTERDSLREANEELR 422
Cdd:COG4717 175 LQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA-AALEERLKEARLLLL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 423 CAQLQPRGLAQADLSLDPTPSGLENLAAEILPAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEaq 502
Cdd:COG4717 254 IAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLP-- 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 503 QRLNQQQLSELRAQVEELQKALQEQGGktedklHEADLELQRKREYIEELEPPTDSST----------ARRIEELQDSLQ 572
Cdd:COG4717 332 PDLSPEELLELLDRIEELQELLREAEE------LEEELQLEELEQEIAALLAEAGVEDeeelraaleqAEEYQELKEELE 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 573 KKDADLRAMEERYRRYVDKA-----RTVIQTLEPKQRpptVVSPEFHTLRSQLWERNLRIRQMEMDYEKSRRRQEQEEKL 647
Cdd:COG4717 406 ELEEQLEELLGELEELLEALdeeelEEELEELEEELE---ELEEELEELREELAELEAELEQLEEDGELAELLQELEELK 482
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
254-648 |
4.01e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 4.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 254 RLESSREDDRLRCLELEREV--AELQQRNQALTSLSQEAQALKDEMDELRQS--------SERARQLEATLNSCRRRLGE 323
Cdd:COG1196 308 EERRRELEERLEELEEELAEleEELEELEEELEELEEELEEAEEELEEAEAElaeaeealLEAEAELAEAEEELEELAEE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 324 LQELRRQVRQLEERNAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKE 403
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 404 KERLLTE-RDSLREANEELRCAQLQPRGLAQADLSLDPTPSGLENLAAEILPAELRETLVRLQLENKRLCQQEAAD---- 478
Cdd:COG1196 468 LLEEAALlEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAlaaa 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 479 -----RERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDkLHEADLELQRKREYIEE-- 551
Cdd:COG1196 548 lqnivVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASD-LREADARYYVLGDTLLGrt 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 552 LEPPTDSSTARRIEELQDSLQKKDADLRAMEERYRRYVDKARTVIQTLEPKQRpptvvspefhtLRSQLWERNLRIRQME 631
Cdd:COG1196 627 LVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEA-----------ELEELAERLAEEELEL 695
|
410
....*....|....*..
gi 1732634088 632 MDYEKSRRRQEQEEKLL 648
Cdd:COG1196 696 EEALLAEEEEERELAEA 712
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
286-583 |
4.86e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 4.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 286 LSQEAQALKDEMDELRQSSERARQLEATLNSCRRRLGElqELRRQVRQLEERNAGHAERTRQLEE-----ELRRAGSLRA 360
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAD--EAKKAEEAKKADEAKKAEEKKKADElkkaeELKKAEEKKK 1565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 361 QLEAQR-RQVQELQGQWQEEAMKAEKwlfecRNLEEKCDLVTKEKErllTERDSLREANEE-LRCAQLQPRGLAQADLSL 438
Cdd:PTZ00121 1566 AEEAKKaEEDKNMALRKAEEAKKAEE-----ARIEEVMKLYEEEKK---MKAEEAKKAEEAkIKAEELKKAEEEKKKVEQ 1637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 439 DPTPSGLENLAAEILPAELRETLVRLQLENKRlcqqEAADRERQEELQRHLEEANRARHGL--EAQQRLNQQQLSELRAQ 516
Cdd:PTZ00121 1638 LKKKEAEEKKKAEELKKAEEENKIKAAEEAKK----AEEDKKKAEEAKKAEEDEKKAAEALkkEAEEAKKAEELKKKEAE 1713
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1732634088 517 ----VEELQKALQEQGGKTEDKLHEADlELQRKREyieelEPPTDSSTARRIEELQDSLQKKDADLRAMEE 583
Cdd:PTZ00121 1714 ekkkAEELKKAEEENKIKAEEAKKEAE-EDKKKAE-----EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE 1778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
171-554 |
5.05e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 5.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 171 DTQSRRYYFLSEEVEEGDHLQQHYLDLERQLLLLSEEKQNLAQENAALRERvgRSEVESAPGLTAKKLLLLQSQLEQLQE 250
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA--LAELEEEEEEEEEALEEAAEEEAELEE 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 251 ENFRLESSREDDRLRCLELEREVAELQQRNQALTSLSQEAQALKDEMDELRQSSERARQLEATlnscRRRLGELQELRRQ 330
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL----RGLAGAVAVLIGV 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 331 VRQLE------------ERNAGHAERTRQLEEELRRAGSLRA------QLEAQRRQVQELQGQWQEEAMKAEKWLFECRN 392
Cdd:COG1196 533 EAAYEaaleaalaaalqNIVVEDDEVAAAAIEYLKAAKAGRAtflpldKIRARAALAAALARGAIGAAVDLVASDLREAD 612
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 393 LEEKCDLVTKEKERLLTERDSLREANEELRCAQLQPRGLAQADLSLDPTPSGLENLAAEILPAELRETLVRLQLENKRLC 472
Cdd:COG1196 613 ARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE 692
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 473 QQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDKLHEADL-------ELQRK 545
Cdd:COG1196 693 LELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPdleelerELERL 772
|
....*....
gi 1732634088 546 REYIEELEP 554
Cdd:COG1196 773 EREIEALGP 781
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
181-534 |
5.43e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 5.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 181 SEEVEEGDHLQQhyldlERQLLLLSEEKQNLAQENAALRERVGRSEVESAPGLTAKKLLLLQSQLEQLqeenfRLESSRE 260
Cdd:PTZ00121 1466 AEEAKKADEAKK-----KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK-----KAEEAKK 1535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 261 DDRLRCLELEREVAELQQ-----RNQALTSLSQEAQALKDEMDELRQSSERARQLEATLNSCRRRLGELQELRRQVRQLE 335
Cdd:PTZ00121 1536 ADEAKKAEEKKKADELKKaeelkKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 336 ERNAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTERDSLR 415
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALK 1695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 416 EANEELRCAQLQPRGLAQadlsldptpsglENLAAEILPAELRETLVRLQlenkRLCQQEAADRERQEELQRHLEEANRA 495
Cdd:PTZ00121 1696 KEAEEAKKAEELKKKEAE------------EKKKAEELKKAEEENKIKAE----EAKKEAEEDKKKAEEAKKDEEEKKKI 1759
|
330 340 350
....*....|....*....|....*....|....*....
gi 1732634088 496 RHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDK 534
Cdd:PTZ00121 1760 AHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
180-588 |
6.08e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 6.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 180 LSEEVEEGDHLQQHYLDLERQLLLLSEEKQNLAQENAALRERVGRSEVESAPGLTAKKLLLLQSQLEQLQEENFRLES-- 257
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEErl 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 258 -SREDDRLRCLELEREVAELQQR-NQALTSLSQEA-QALKDEMDELRQSSERARQLEATLNSCRRrlgELQELRRQVRQL 334
Cdd:COG4717 156 eELRELEEELEELEAELAELQEElEELLEQLSLATeEELQDLAEELEELQQRLAELEEELEEAQE---ELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 335 E-ERNAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTERDS 413
Cdd:COG4717 233 EnELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 414 LREANEELRCAQLQPRGLAQAD-----LSLDPTPSGLENLAAEILPAELRETLVRLQLENKRLCQQEAAD---------- 478
Cdd:COG4717 313 LEELEEEELEELLAALGLPPDLspeelLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEdeeelraale 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 479 -RERQEELQRHLEEANR--ARHGLEAQQRLNQQQLSELRAQVEELQKALQEqggkTEDKLHEADLELQRKREYIEELEpp 555
Cdd:COG4717 393 qAEEYQELKEELEELEEqlEELLGELEELLEALDEEELEEELEELEEELEE----LEEELEELREELAELEAELEQLE-- 466
|
410 420 430
....*....|....*....|....*....|...
gi 1732634088 556 tdssTARRIEELQDSLQKKDADLRAMEERYRRY 588
Cdd:COG4717 467 ----EDGELAELLQELEELKAELRELAEEWAAL 495
|
|
| HkD_Gipie |
cd22230 |
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar ... |
8-153 |
6.11e-07 |
|
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: 49.83 E-value: 6.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 8 LCGSLLTWLQTFQ------------------VSPPCASPQ--DLSSGLAIAHVLNQIDPSWFNNEWLQGIseDSSPSWRl 67
Cdd:cd22230 4 MSGALVTWALGFEglvgeeedslgfpeeeeeEGTLDAEKRflRLSNGDLLNRVMGIIDPSPRGGPRMRGD--DGPAAHR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 68 kVRKLEKILQSLVEYSKNVLgHPVSDQHLPDVSLIGE--FSNPA--ELGKLLQLVLGCAISCEKKQEYIQRIMTLEESVQ 143
Cdd:cd22230 81 -VQNLHILWGRLRDFYQEEL-QQLILSPPPDLQVMGRdpFTEEAvqELEKLLRLLLGAAVQCERRELFIRHIQGLDLDVQ 158
|
170
....*....|
gi 1732634088 144 HVVMEAIQEL 153
Cdd:cd22230 159 AELAEAIQEV 168
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
287-651 |
1.56e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 287 SQEAQALKDEMDELRQSSERARQLEATLNSCRRRLGELQ----ELRRQVRQLE-ERNagHAERTRQLEEELR-RAGSLRA 360
Cdd:TIGR02169 152 PVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDliidEKRQQLERLRrERE--KAERYQALLKEKReYEGYELL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 361 -QLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDlvtkEKERLLTERDSLREANEELRCAQLQPRglaqadlsLD 439
Cdd:TIGR02169 230 kEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLE----EIEQLLEELNKKIKDLGEEEQLRVKEK--------IG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 440 PTPSGLENLAAEIlpAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEE 519
Cdd:TIGR02169 298 ELEAEIASLERSI--AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 520 LQKALQEqggkTEDKLHEADLELQRKREYIEELEpptdsstaRRIEELQDSLQKKDADLRAMEERYRRYVDKARTVIQTL 599
Cdd:TIGR02169 376 VDKEFAE----TRDELKDYREKLEKLKREINELK--------RELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1732634088 600 EPKQRPPTVVSPEFHTLRSQLWERNLRIRQMEMDYEKSRRRQEQEEKLLISA 651
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEA 495
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
282-526 |
1.90e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 282 ALTSLSQEAQALKDEMDELRQSSERARQLEATLNSCRRRL-GELQELRRQVRQLEERNAGHAERTRQLEEELRRagsLRA 360
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALlKQLAALERRIAALARRIRALEQELAALEAELAE---LEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 361 QLEAQRRQVQELQGQWQEEAMKAEKwlfecrnleekcdLVTKEKERLLTERDSLREANEELRCAqlqpRGLAQADLSLdp 440
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYR-------------LGRQPPLALLLSPEDFLDAVRRLQYL----KYLAPARREQ-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 441 tpsgLENLAAEIlpAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEEL 520
Cdd:COG4942 152 ----AEELRADL--AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
....*.
gi 1732634088 521 QKALQE 526
Cdd:COG4942 226 EALIAR 231
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
288-453 |
2.98e-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: 50.72 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 288 QEAQALKDEMDELRQSSERARQLEATLNSCRRRLGELQELRRQVRQLEERNAGHAERTRQLEEELRRAGSLRAQLEAQ-- 365
Cdd:COG3096 495 QTARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQaa 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 366 ---------RRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLV----------------TKEKERLLT-ERDSLREANE 419
Cdd:COG3096 575 eaveqrselRQQLEQLRARIKELAARAPAWLAAQDALERLREQSgealadsqevtaamqqLLEREREATvERDELAARKQ 654
|
170 180 190
....*....|....*....|....*....|....*
gi 1732634088 420 ELrcaQLQPRGLAQADLSLDPTPSGL-ENLAAEIL 453
Cdd:COG3096 655 AL---ESQIERLSQPGGAEDPRLLALaERLGGVLL 686
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
205-647 |
3.80e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 205 SEEKQNLAQENAALRERVGRSEVESAPGLTAKKLLLLQSQLEQLQEenfRLESSREDDRLRclelerEVAELQQRNQALT 284
Cdd:PTZ00121 1393 ADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKK---KAEEAKKADEAK------KKAEEAKKAEEAK 1463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 285 SLSQEAQalkdEMDELRQSSERARQLEATLNSCRRRLGELQELRRQVRQLEERNAGHAERTRQLEEELRRAGSLRAQLEA 364
Cdd:PTZ00121 1464 KKAEEAK----KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEA 1539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 365 QR----RQVQELQGQwqEEAMKAEkwlfECRNLEEKcdlvTKEKERlltERDSLREAnEELRCAQlQPRGLAQADLSLDP 440
Cdd:PTZ00121 1540 KKaeekKKADELKKA--EELKKAE----EKKKAEEA----KKAEED---KNMALRKA-EEAKKAE-EARIEEVMKLYEEE 1604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 441 TPSGLENLAAEILPAELRETLVRLQLENKRLCQQEAADRE--RQEELQRHLEEANRARHGLEAQQRlnqqqlSELRAQVE 518
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEekKKAEELKKAEEENKIKAAEEAKKA------EEDKKKAE 1678
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 519 ELQKALQEQGGKTEDKLHEAdlELQRKREYIEELEpPTDSSTARRIEELQDSLQKKDADLRAMEERYRRYVDKARtviQT 598
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKEA--EEAKKAEELKKKE-AEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK---KD 1752
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1732634088 599 LEPKQRPPTVVSPEFHTLRSQLWERNLRIRQmEMDYEKSRRRQEQEEKL 647
Cdd:PTZ00121 1753 EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE-ELDEEDEKRRMEVDKKI 1800
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
254-600 |
6.02e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 6.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 254 RLESSREDDRLRCLELEREVAELQQRNQALTSLSQEAQALKDEMDELRQSS---ERARQLEATLNSCRRRLGELqELRRQ 330
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHelyEEAKAKKEELERLKKRLTGL-TPEKL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 331 VRQLEERNAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQG-----------------------------QWQEEAM 381
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelteehrkelleeytaelkRIEKELK 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 382 KAEKWLFECRNLEEKCDLVTKEKERLLTER---DSLREANEELRCAQLQPrgLAQADLSLDPTPSGLENLAAEILpaELR 458
Cdd:PRK03918 470 EIEEKERKLRKELRELEKVLKKESELIKLKelaEQLKELEEKLKKYNLEE--LEKKAEEYEKLKEKLIKLKGEIK--SLK 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 459 ETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQL--------------SELRAQVEELQKaL 524
Cdd:PRK03918 546 KELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELepfyneylelkdaeKELEREEKELKK-L 624
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1732634088 525 QEQGGKTEDKLHEADLELQRKREYIEELEPPTDSSTARRIEELQDSLQKKDADLRAMEERYRRYVDKARTVIQTLE 600
Cdd:PRK03918 625 EEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLK 700
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
265-646 |
6.05e-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: 49.95 E-value: 6.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 265 RCLELEREVAELQQRNQALTslsQEAQALKDEMDELRQsserARQLEATLNSCRRRLGELQE-LRRQVRQLEERNAGHAE 343
Cdd:COG3096 307 RLVEMARELEELSARESDLE---QDYQAASDHLNLVQT----ALRQQEKIERYQEDLEELTErLEEQEEVVEEAAEQLAE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 344 RTRQLEEELRRAGSLRAQLEAQRRQVQELQ---GQWQEeAMKAekwLFECRNLEEKCDL-VTKEKERLLTERDSLREANE 419
Cdd:COG3096 380 AEARLEAAEEEVDSLKSQLADYQQALDVQQtraIQYQQ-AVQA---LEKARALCGLPDLtPENAEDYLAAFRAKEQQATE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 420 ELRCAQlQPRGLAQADLS-LDPTPSGLENLAAEILPAELRETlVRLQLENKRLCQQEAadrERQEELQRHLEEAnrarhg 498
Cdd:COG3096 456 EVLELE-QKLSVADAARRqFEKAYELVCKIAGEVERSQAWQT-ARELLRRYRSQQALA---QRLQQLRAQLAEL------ 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 499 leaQQRLNQQQlselraQVEELQKALQEQGGKTEDKLHEADLELQRKREYIEELEPPTDSSTARRIEELQ--DSLQKKDA 576
Cdd:COG3096 525 ---EQRLRQQQ------NAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQqlEQLRARIK 595
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 577 DLRAMEERYRryvdKARTVIQTLEPKQRPPTVVSPEFHTLRSQLWERNlriRQMEMDYEKSRRRQEQEEK 646
Cdd:COG3096 596 ELAARAPAWL----AAQDALERLREQSGEALADSQEVTAAMQQLLERE---REATVERDELAARKQALES 658
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
256-570 |
6.22e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 6.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 256 ESSREDDRLRCLELEREVAELQQRNQALTSLSQEAQALKDEMDELRQS-----------SERARQLEATLNSCRRRLGEL 324
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAeelkkaeekkkAEEAKKAEEDKNMALRKAEEA 1586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 325 QELRRQ-----VRQLEERNAGHAERTRQLEEELRRAGSLRAQlEAQRRQVQELQGQWQEEAMKAEkwlfECRNLEEKcDL 399
Cdd:PTZ00121 1587 KKAEEArieevMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA-EEEKKKVEQLKKKEAEEKKKAE----ELKKAEEE-NK 1660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 400 VTKEKERLLTERDslREANEELRCAQLQPRGlaqadlsldptpsglenlAAEILPAELRETLVRLQLENKrlcqqEAADR 479
Cdd:PTZ00121 1661 IKAAEEAKKAEED--KKKAEEAKKAEEDEKK------------------AAEALKKEAEEAKKAEELKKK-----EAEEK 1715
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 480 ERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEElQKALQEQGGKTEDKLHEADLELQRK-REYIEELEPPTDS 558
Cdd:PTZ00121 1716 KKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE-KKKIAHLKKEEEKKAEEIRKEKEAViEEELDEEDEKRRM 1794
|
330
....*....|..
gi 1732634088 559 STARRIEELQDS 570
Cdd:PTZ00121 1795 EVDKKIKDIFDN 1806
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
405-600 |
6.29e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 6.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 405 ERLLTERDSLREANEELRCAQLQPRGLAQadlsldptpsgLENLAAEIlpAELRETLVRLQLENKRLCQQEAadRERQEE 484
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLEP-----------IRELAERY--AAARERLAELEYLRAALRLWFA--QRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 485 LQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDKLhEADL--------ELQRKREYIEE----- 551
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQL-EREIerlereleERERRRARLEAllaal 371
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1732634088 552 -LEPPTDsstARRIEELQDSLQKKDADLRAMEERYRRYVDKARTVIQTLE 600
Cdd:COG4913 372 gLPLPAS---AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR 418
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
268-599 |
1.08e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 49.07 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 268 ELEREVAELQQRNQALTSLSQEAQ----ALKDEMDELRQSSERARQ-LEATLNSCRRRLGELQELRRQVrqleernagha 342
Cdd:pfam12128 601 ELRERLDKAEEALQSAREKQAAAEeqlvQANGELEKASREETFARTaLKNARLDLRRLFDEKQSEKDKK----------- 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 343 erTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEE---------AMKAEKWLFECRNLEEKCDLVTKEKERLLTERDS 413
Cdd:pfam12128 670 --NKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEqkeqkrearTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKA 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 414 LREANEELRCAQLQprglaqadlSLDPTPSGLENLAAEIlpaelrETLVRlQLENKRLCQQEAADRERQEELQRHLEEAN 493
Cdd:pfam12128 748 ELKALETWYKRDLA---------SLGVDPDVIAKLKREI------RTLER-KIERIAVRRQEVLRYFDWYQETWLQRRPR 811
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 494 RARHGLEAQQRLN--QQQLSELRAQVEELQKALQEQGGKTEDKLHEADLELQRKREYIEEL----EPPTDSSTARRIEEL 567
Cdd:pfam12128 812 LATQLSNIERAISelQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLatlkEDANSEQAQGSIGER 891
|
330 340 350
....*....|....*....|....*....|..
gi 1732634088 568 QDSLQKKDADLRAMEERYRRYVDKARTVIQTL 599
Cdd:pfam12128 892 LAQLEDLKLKRDYLSESVKKYVEHFKNVIADH 923
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
286-647 |
1.32e-05 |
|
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: 48.81 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 286 LSQEAQALKDEMDELRQSSERARQLEATLNSCRRRLGELQELRRQVRQLE-------------------ERNAGHAERTR 346
Cdd:TIGR00618 224 LEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRaqeavleetqerinrarkaAPLAAHIKAVT 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 347 QLEE-------ELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLE---EKCDLVTKEKERLLTERDSLRE 416
Cdd:TIGR00618 304 QIEQqaqrihtELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRdahEVATSIREISCQQHTLTQHIHT 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 417 ANEELRCAQLQPRGLAQADLSLDptpsgleNLAAEILPAELRETLVRLQLenKRLCQQEAADRERQEELQRHLEEANRAR 496
Cdd:TIGR00618 384 LQQQKTTLTQKLQSLCKELDILQ-------REQATIDTRTSAFRDLQGQL--AHAKKQQELQQRYAELCAAAITCTAQCE 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 497 HGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDKLHEADLELQRKREYIEEL-----------EPPTDSSTARRIE 565
Cdd:TIGR00618 455 KLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCihpnparqdidNPGPLTRRMQRGE 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 566 ----ELQDSLQKKDADLRAMEERYRRYVDKARTVIQTLEPKQRPPTVVSPEFHTLRsQLWERNLRIRQMEMDYEKSRRRQ 641
Cdd:TIGR00618 535 qtyaQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQ-NITVRLQDLTEKLSEAEDMLACE 613
|
....*.
gi 1732634088 642 EQEEKL 647
Cdd:TIGR00618 614 QHALLR 619
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
456-645 |
1.53e-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: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 456 ELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKAL--------QEQ 527
Cdd:TIGR02169 713 DASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALndlearlsHSR 792
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 528 GGKTEDKLHEADLELQRKREYIEELEPPTDSSTARRiEELQDSLQKKDADLRAMEERYRRYVDKARTVIQTLEPKQRPPT 607
Cdd:TIGR02169 793 IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK-EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE 871
|
170 180 190
....*....|....*....|....*....|....*...
gi 1732634088 608 VVSPEFHTLRSQLWERNLRIRQMEMDYEKSRRRQEQEE 645
Cdd:TIGR02169 872 ELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
206-593 |
2.46e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 206 EEKQNLAQEnaALRERVGRSEVESAPGLTAKKLLLLQSQLEQLQEENFR-LESSREDDRLRCLELEREVAELQQRNQALT 284
Cdd:PTZ00121 1094 EEAFGKAEE--AKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARkAEEARKAEDAKRVEIARKAEDARKAEEARK 1171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 285 SLSQEAQALKDEMDELRQSSERARQLEATLNSCRRRLGELQELRRQVRQLEERNA---GHAERTRQLEEELRRAGSLRAQ 361
Cdd:PTZ00121 1172 AEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAeavKKAEEAKKDAEEAKKAEEERNN 1251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 362 LEAQRRQVQELQGQWQ-------EEAMKAEkwlfECRNLEEKCDLVTKEKERLLTERDSLREANEELRCAQLQPRGLAQA 434
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARrqaaikaEEARKAD----ELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA 1327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 435 DLSLDPTPSGLENL--AAEILPAELRETLVRLQLENKRlcqqEAADRERQEELQRHLEEANRarhglEAQQRlnqQQLSE 512
Cdd:PTZ00121 1328 KKKADAAKKKAEEAkkAAEAAKAEAEAAADEAEAAEEK----AEAAEKKKEEAKKKADAAKK-----KAEEK---KKADE 1395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 513 LRAQVEELQKALQEQGGKTEDKlHEADlELQRKREYIEEL-EPPTDSSTARRIEELqdslqKKDADLRAMEERYRRYVDK 591
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAK-KKAD-EAKKKAEEKKKAdEAKKKAEEAKKADEA-----KKKAEEAKKAEEAKKKAEE 1468
|
..
gi 1732634088 592 AR 593
Cdd:PTZ00121 1469 AK 1470
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
381-593 |
3.41e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 381 MKAEKWLFECRNLEEKCDLVTKEKERLLTERDSLREANEELRCAQLQPRGLAQADLSLDPTPSGLENLAAEILPAELRET 460
Cdd:COG4717 40 LAFIRAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 461 LVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDKLHEADL 540
Cdd:COG4717 120 KLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1732634088 541 ELQRKREYIEELEpptdsstaRRIEELQDSLQKKDADLRAMEERYRRYVDKAR 593
Cdd:COG4717 200 ELEELQQRLAELE--------EELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
260-580 |
5.45e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 260 EDDRLRCLELEREVAElqqrnqaltslsqeaqaLKDEMDELRQSSERARQLEATlnscRRRLGELQELRRQVRQL-EERN 338
Cdd:PRK02224 471 EEDRERVEELEAELED-----------------LEEEVEEVEERLERAEDLVEA----EDRIERLEERREDLEELiAERR 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 339 AGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKwlfecrnLEEKCDLVTKEKERLLTERDSLREan 418
Cdd:PRK02224 530 ETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAE-------LNSKLAELKERIESLERIRTLLAA-- 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 419 eelrcaqlqprglaqadlsldptpsgLENLAAEIlpAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRArhg 498
Cdd:PRK02224 601 --------------------------IADAEDEI--ERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIE--- 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 499 lEAQQRlnQQQLSELRAQVEELQKALQEQGGKTEDKLHEADLELQRKREYIEELEppTDSSTARRIEELQD---SLQKKD 575
Cdd:PRK02224 650 -EARED--KERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERRE--ALENRVEALEALYDeaeELESMY 724
|
....*
gi 1732634088 576 ADLRA 580
Cdd:PRK02224 725 GDLRA 729
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
298-584 |
5.55e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 5.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 298 DELRQSSERARQLEATLnSCRRrlgelqELRRQVRQLEERNAGHAERTRQLEEELRRAGSLRAQLEAQR---------RQ 368
Cdd:PRK04863 273 DYMRHANERRVHLEEAL-ELRR------ELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASdhlnlvqtaLR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 369 VQELQGQWQEEAMKAEKwlfecrNLEEKCDLVTKEKERLLTERDSLREANEELRCAQ------------LQPRGL----- 431
Cdd:PRK04863 346 QQEKIERYQADLEELEE------RLEEQNEVVEEADEQQEENEARAEAAEEEVDELKsqladyqqaldvQQTRAIqyqqa 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 432 ------AQADLSLDP-TPSGLENLAAEILPAELRETLVRLQLENKRLCQQEAADR------------------------- 479
Cdd:PRK04863 420 vqalerAKQLCGLPDlTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQfeqayqlvrkiagevsrseawdvar 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 480 --ERQEELQRHL---EEANRARHGlEAQQRLNQQQlselraQVEELQKALQEQGGKTEDKLHEADLELQRKREYIEELEP 554
Cdd:PRK04863 500 elLRRLREQRHLaeqLQQLRMRLS-ELEQRLRQQQ------RAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSE 572
|
330 340 350
....*....|....*....|....*....|
gi 1732634088 555 PTDSSTARRiEELQDSLQKKDADLRAMEER 584
Cdd:PRK04863 573 SVSEARERR-MALRQQLEQLQARIQRLAAR 601
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
253-573 |
5.70e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 5.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 253 FRLESSREDDRLRCLELEREVAELqqrNQALTSLSQEAQALKDEMdelrQSSERARQLEATLNSCRRRLGELQE-LRRQV 331
Cdd:PRK04863 296 YTSRRQLAAEQYRLVEMARELAEL---NEAESDLEQDYQAASDHL----NLVQTALRQQEKIERYQADLEELEErLEEQN 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 332 RQLEERNAGHAERTRQLEEELRRAGSLRAQL--------EAQRRQVQELQGQWQEEamKAEKWL----FECRNLEEKCD- 398
Cdd:PRK04863 369 EVVEEADEQQEENEARAEAAEEEVDELKSQLadyqqaldVQQTRAIQYQQAVQALE--RAKQLCglpdLTADNAEDWLEe 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 399 LVTKEKErlLTERdsLREANEELRCAQLQPRGLAQAdLSLdptpsgLENLAAEILPAE----LRETLVRLQlENKRLCQQ 474
Cdd:PRK04863 447 FQAKEQE--ATEE--LLSLEQKLSVAQAAHSQFEQA-YQL------VRKIAGEVSRSEawdvARELLRRLR-EQRHLAEQ 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 475 EAADRERQEELQRHLEEANRARHGL-EAQQRLNQQQLSElrAQVEELQKALQEQGGKTEDKLHEADLELQRKREYIEELE 553
Cdd:PRK04863 515 LQQLRMRLSELEQRLRQQQRAERLLaEFCKRLGKNLDDE--DELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQ 592
|
330 340
....*....|....*....|..
gi 1732634088 554 PPTDSSTARRIE--ELQDSLQK 573
Cdd:PRK04863 593 ARIQRLAARAPAwlAAQDALAR 614
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
323-422 |
6.94e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 46.23 E-value: 6.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 323 ELQELRRQVRQLE-ERNAGHAERTRQLEEelrRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVT 401
Cdd:COG0542 412 ELDELERRLEQLEiEKEALKKEQDEASFE---RLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIP 488
|
90 100
....*....|....*....|.
gi 1732634088 402 KEKERLLTERDSLREANEELR 422
Cdd:COG0542 489 ELEKELAELEEELAELAPLLR 509
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
259-600 |
1.05e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 259 REDDRLRCLELEREVAELQQRnqaLTSLSQEAQALKDEMDELRQSSERARQLEATLNSCRRRLG--ELQELRRQVRQLEE 336
Cdd:COG4913 276 YLRAALRLWFAQRRLELLEAE---LEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgdRLEQLEREIERLER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 337 RNAGHAERTRQLEEELRRAG----SLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKcdlVTKEKERLLTERD 412
Cdd:COG4913 353 ELEERERRRARLEALLAALGlplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRD---LRRELRELEAEIA 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 413 SLREANEELRCAQLQPRGLAQADLSLDPT-----------------------------------PSGLENLAAEILPAEL 457
Cdd:COG4913 430 SLERRKSNIPARLLALRDALAEALGLDEAelpfvgelievrpeeerwrgaiervlggfaltllvPPEHYAAALRWVNRLH 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 458 RETLVRLQL--ENKRLCQQEAADR-------------------------------ERQEELQRH--------LEEANRAR 496
Cdd:COG4913 510 LRGRLVYERvrTGLPDPERPRLDPdslagkldfkphpfrawleaelgrrfdyvcvDSPEELRRHpraitragQVKGNGTR 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 497 HGLEAQQRL---------NQQQLSELRAQVEELQKALQEQGGKTEdKLHEADLELQRKREYIEELEPPTDS-----STAR 562
Cdd:COG4913 590 HEKDDRRRIrsryvlgfdNRAKLAALEAELAELEEELAEAEERLE-ALEAELDALQERREALQRLAEYSWDeidvaSAER 668
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1732634088 563 RIEELQD-----------------SLQKKDADLRAMEERYRRYVDKARTVIQTLE 600
Cdd:COG4913 669 EIAELEAelerldassddlaaleeQLEELEAELEELEEELDELKGEIGRLEKELE 723
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
254-595 |
1.32e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 254 RLESSREDDRLRCLELEREVAELQQRNQALTSLSQEAQALKDEMDELRQSSERARQLEATLNSCRRRLGELQELRRQVRQ 333
Cdd:PRK03918 218 ELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIK 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 334 LEERNAGHAERTRQLEEELrraGSLRAQLEAQRRQVQELQgqwqeeamkaekwlfecrNLEEKCDLVTKEKERLLTERDS 413
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRL---SRLEEEINGIEERIKELE------------------EKEERLEELKKKLKELEKRLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 414 LREANEELRCAQLQPRGLAQadLSLDPTPSGLENLAAEILPAELRETLVRLQLENkrLCQQEAADRERQEELQRHLEEAN 493
Cdd:PRK03918 357 LEERHELYEEAKAKKEELER--LKKRLTGLTPEKLEKELEELEKAKEEIEEEISK--ITARIGELKKEIKELKKAIEELK 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 494 RARH-----GLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTED---KLHEADLELQRKREYIEELEpptdssTARRIE 565
Cdd:PRK03918 433 KAKGkcpvcGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKlrkELRELEKVLKKESELIKLKE------LAEQLK 506
|
330 340 350
....*....|....*....|....*....|.
gi 1732634088 566 ELQDSLQKKDA-DLRAMEERYRRYVDKARTV 595
Cdd:PRK03918 507 ELEEKLKKYNLeELEKKAEEYEKLKEKLIKL 537
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
332-552 |
1.65e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 332 RQLEERNAGHAERTRQLEEELRRagsLRAQLEAQRRQVQELQGQWQEEAMKAEKwlfecRNLEEKCDLVTKEKERLLTER 411
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPE---LRKELEEAEAALEEFRQKNGLVDLSEEA-----KLLLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 412 DSLREANEELRcAQLQPRGLAQADLSLDPTPSGLENLAAEiLPAELRETLVRLQLENKRLC----QQEAADRERQEELQR 487
Cdd:COG3206 236 AEAEARLAALR-AQLGSGPDALPELLQSPVIQQLRAQLAE-LEAELAELSARYTPNHPDVIalraQIAALRAQLQQEAQR 313
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1732634088 488 HLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQggktedklheadLELQRKREYIEEL 552
Cdd:COG3206 314 ILASLEAELEALQAREASLQAQLAQLEARLAELPELEAEL------------RRLEREVEVAREL 366
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
253-575 |
1.88e-04 |
|
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: 44.71 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 253 FRLESSREDDRLRCLELERE-VAELQQRNQALT-SLSQEAQALKDEMDELRQSSERARQLEATLNSCRRRLGELQELRRQ 330
Cdd:pfam05483 101 LKQKENKLQENRKIIEAQRKaIQELQFENEKVSlKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 331 VRQLEERNAGHAERTRQLEEELRRAGS-----LRAQLEAQRRQVQELQGQWQEEAMKAEKWLfeCRNLEEKCDLVTKEKE 405
Cdd:pfam05483 181 TRQVYMDLNNNIEKMILAFEELRVQAEnarleMHFKLKEDHEKIQHLEEEYKKEINDKEKQV--SLLLIQITEKENKMKD 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 406 RLLTERDSLREANEELRCAQLQPRGLAQADLSLDPTPSGLENLAAEILPAELRETLVR--LQLENKRLCQQeaadrerQE 483
Cdd:pfam05483 259 LTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEedLQIATKTICQL-------TE 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 484 ELQRHLEEANRARhgleAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDKLHEADLELQRKREYIEELEPPTDSSTArR 563
Cdd:pfam05483 332 EKEAQMEELNKAK----AAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEV-E 406
|
330
....*....|..
gi 1732634088 564 IEELQDSLQKKD 575
Cdd:pfam05483 407 LEELKKILAEDE 418
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
253-422 |
2.06e-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: 44.73 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 253 FRLESSREDDRLRC-LELEREVAELQQRNQaltslsQEAQALKDEMDELRQSSERARQLEAtlnscrRRLGELQELR-RQ 330
Cdd:pfam17380 383 LQMERQQKNERVRQeLEAARKVKILEEERQ------RKIQQQKVEMEQIRAEQEEARQREV------RRLEEERAREmER 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 331 VRQLEERNAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKW-LFECRNLEEKCDLVTKEKERLLT 409
Cdd:pfam17380 451 VRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQaMIEEERKRKLLEKEMEERQKAIY 530
|
170
....*....|...
gi 1732634088 410 ERDSLREANEELR 422
Cdd:pfam17380 531 EEERRREAEEERR 543
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
449-646 |
3.13e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 449 AAEILPAELRETLVRLQLENKRLCQQEAADRERQEELQRH---LEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQ 525
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALerrIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 526 EQGGKTEDKLheADLELQRKREYIEELEPPTDSS-TARRIEELQDSLQKKDADLRAMEERYRRYVDKARTVIQTLEPKQR 604
Cdd:COG4942 101 AQKEELAELL--RALYRLGRQPPLALLLSPEDFLdAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1732634088 605 PPTVVSPEFHTLRSQLWERNLRIRQMEMDYEKSRRRQEQEEK 646
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
268-526 |
4.22e-04 |
|
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: 43.63 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 268 ELEREVAELQQRNQALTSLSQEAQALKDEmdELRQS---SERARQLEATLNSCRRRLGELQELRRQV-RQLEERNAGHAE 343
Cdd:pfam01576 451 EAEGKNIKLSKDVSSLESQLQDTQELLQE--ETRQKlnlSTRLRQLEDERNSLQEQLEEEEEAKRNVeRQLSTLQAQLSD 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 344 RTRQLEEElrrAGSLRAQLEAQRRQVQELQGQWQEEAMKAEkwlfECRNLEEKCDLVTKEKERLLTERDSLREANEELRC 423
Cdd:pfam01576 529 MKKKLEED---AGTLEALEEGKKRLQRELEALTQQLEEKAA----AYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEK 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 424 AQ------LQPRGLAQADLSLDPTPSGLENLAAEILPAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARH 497
Cdd:pfam01576 602 KQkkfdqmLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVH 681
|
250 260
....*....|....*....|....*....
gi 1732634088 498 GLEAQQRLNQQQLSELRAQVEELQKALQE 526
Cdd:pfam01576 682 ELERSKRALEQQVEEMKTQLEELEDELQA 710
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
268-386 |
4.68e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 268 ELEREVAELQQRnqaLTSLSQEAQALKDEMDELRQS-SERARQLEATLNSCRRRL-GELQELRRQVRQLEERNAGHAERT 345
Cdd:COG3206 274 ELEAELAELSAR---YTPNHPDVIALRAQIAALRAQlQQEAQRILASLEAELEALqAREASLQAQLAQLEARLAELPELE 350
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1732634088 346 RQLEEELRRAGSLRAQLEAQRRQVQELQgqwQEEAMKAEKW 386
Cdd:COG3206 351 AELRRLEREVEVARELYESLLQRLEEAR---LAEALTVGNV 388
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
267-441 |
5.28e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 267 LELEREVAELQQRNQAltslSQEAQALKDEMDELRQSSERARQLEATLNSCRRRLGELQELRRQVRQLEERN-------- 338
Cdd:PRK04863 479 YQLVRKIAGEVSRSEA----WDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLgknldded 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 339 ---AGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWL----------------FECRNLEEKCDL 399
Cdd:PRK04863 555 eleQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLaaqdalarlreqsgeeFEDSQDVTEYMQ 634
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1732634088 400 VTKEKERLLT-ERDSLREANEELrcaQLQPRGLAQADLSLDPT 441
Cdd:PRK04863 635 QLLERERELTvERDELAARKQAL---DEEIERLSQPGGSEDPR 674
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
263-378 |
5.77e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.15 E-value: 5.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 263 RLRcLELEREVAELQQRNQALTSLSQEAQALKDEMDELrqSSERARQLEAtlnscrrrlgELQELRRQVRQLEERNagHA 342
Cdd:COG0542 401 RVR-MEIDSKPEELDELERRLEQLEIEKEALKKEQDEA--SFERLAELRD----------ELAELEEELEALKARW--EA 465
|
90 100 110
....*....|....*....|....*....|....*.
gi 1732634088 343 ERtrqleEELRRAGSLRAQLEAQRRQVQELQGQWQE 378
Cdd:COG0542 466 EK-----ELIEEIQELKEELEQRYGKIPELEKELAE 496
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
328-646 |
7.63e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.80 E-value: 7.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 328 RRQVRQLEERNAGHAERTRQLEEelrragSLRAQLEAQRRQVQeLQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERL 407
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEE------AEKARQAEMDRQAA-IYAEQERMAMERERELERIRQEERKRELERIRQEEI 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 408 LTERDSLREAnEELRCAQLQPRGLAQADLSLDPTPSGLENLAAEILPAELREtlvrlqLENKRLCQQEAadreRQEELQR 487
Cdd:pfam17380 371 AMEISRMREL-ERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVE------MEQIRAEQEEA----RQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 488 HLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDKlheADLELQRKREYIEELEpptDSSTARRIEEL 567
Cdd:pfam17380 440 LEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDR---KRAEEQRRKILEKELE---ERKQAMIEEER 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 568 QDSLQKKDADLRA---MEERYRRYVDKARTVIQTLEPKQRPPtvvspefHTLRSQLWERNlRIRQMEMDYEKSRRRQEQE 644
Cdd:pfam17380 514 KRKLLEKEMEERQkaiYEEERRREAEEERRKQQEMEERRRIQ-------EQMRKATEERS-RLEAMEREREMMRQIVESE 585
|
..
gi 1732634088 645 EK 646
Cdd:pfam17380 586 KA 587
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
348-600 |
7.74e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 7.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 348 LEEELRRAGSLRAQLEAQRRQVQELQGQWQEE-AMKAEKWLFECRN-LEEKCDLVTKEKERLLTERDSLREANEElrcaq 425
Cdd:PRK02224 164 LEEYRERASDARLGVERVLSDQRGSLDQLKAQiEEKEEKDLHERLNgLESELAELDEEIERYEEQREQARETRDE----- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 426 lqprglaqADLSLD---PTPSGLENLAAEIlpAELRETlvrlqlenKRLCQQEAAD-RERQEELQRHLEEANRARHGLEA 501
Cdd:PRK02224 239 --------ADEVLEeheERREELETLEAEI--EDLRET--------IAETEREREElAEEVRDLRERLEELEEERDDLLA 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 502 QQRLNQQQLSELRAQVEELQKALQEqggkTEDKLHEADLELQRKREYIEELepptdSSTARRIEELQDSLQKKDADLRAM 581
Cdd:PRK02224 301 EAGLDDADAEAVEARREELEDRDEE----LRDRLEECRVAAQAHNEEAESL-----REDADDLEERAEELREEAAELESE 371
|
250
....*....|....*....
gi 1732634088 582 EERYRRYVDKARTVIQTLE 600
Cdd:PRK02224 372 LEEAREAVEDRREEIEELE 390
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
323-587 |
8.30e-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: 8.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 323 ELQELRRQVRQLEERNAGHAERTRQleeelrragsLRAQLEAQRRQVQELQGqwqeeaMKAEKWLFECRNLEEKCDLVTK 402
Cdd:COG3096 837 ELAALRQRRSELERELAQHRAQEQQ----------LRQQLDQLKEQLQLLNK------LLPQANLLADETLADRLEELRE 900
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 403 EKERLLTERDSLREANEelRCAQLQPrglaQADlSLDPTPSGLENLAAEILPAELRETLVRLQLE------NKRL----- 471
Cdd:COG3096 901 ELDAAQEAQAFIQQHGK--ALAQLEP----LVA-VLQSDPEQFEQLQADYLQAKEQQRRLKQQIFalsevvQRRPhfsye 973
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 472 --CQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLSE-----------LRAQVEELQKALQE--QGGKTEDKLH 536
Cdd:COG3096 974 daVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQynqvlaslkssRDAKQQTLQELEQEleELGVQADAEA 1053
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1732634088 537 EAdLELQRKREYIEELepptdSSTARRIEELQDSLQKKDADLRAMEERYRR 587
Cdd:COG3096 1054 EE-RARIRRDELHEEL-----SQNRSRRSQLEKQLTRCEAEMDSLQKRLRK 1098
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
325-561 |
1.15e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 325 QELRRQVRQLEERNAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEeamkaekwlfecrnLEEKCDLVTKEK 404
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRA--------------LEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 405 ERLLTERDSLREANEELRcAQLQPRGLAQADLSLDPTPSGL---ENLAAEILPAELRETLVRLQLEN-KRLCQQEAADRE 480
Cdd:COG4942 86 AELEKEIAELRAELEAQK-EELAELLRALYRLGRQPPLALLlspEDFLDAVRRLQYLKYLAPARREQaEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 481 RQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDKLHEADlELQRKREYIEELEPPTDSST 560
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE-ELEALIARLEAEAAAAAERT 243
|
.
gi 1732634088 561 A 561
Cdd:COG4942 244 P 244
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
253-596 |
1.30e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.02 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 253 FRLESSRedDRLRCLElerEVAELQQRNqaLTSLSQEAQALKDEMDELRQSSERA----RQLEATLNSCRRRLGELQELR 328
Cdd:pfam05483 261 FLLEESR--DKANQLE---EKTKLQDEN--LKELIEKKDHLTKELEDIKMSLQRSmstqKALEEDLQIATKTICQLTEEK 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 329 R-QVRQLEERNAGHAERTRQLE------EELRRAGSLRaqLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLE---EKCD 398
Cdd:pfam05483 334 EaQMEELNKAKAAHSFVVTEFEattcslEELLRTEQQR--LEKNEDQLKIITMELQKKSSELEEMTKFKNNKEvelEELK 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 399 LVTKEKERLLTERDSLREANEELRCAQLQPRGLAQA------DLSLDPTPSG---------LENLAAEILPAELRETLV- 462
Cdd:pfam05483 412 KILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQArekeihDLEIQLTAIKtseehylkeVEDLKTELEKEKLKNIELt 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 463 ----RLQLENKRLCQqEAADRERqeELQRHLEEANRARHGLE---AQQRLNQQQLSELRAQVEELQKALQEQGGKTEDKL 535
Cdd:pfam05483 492 ahcdKLLLENKELTQ-EASDMTL--ELKKHQEDIINCKKQEErmlKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKL 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 536 HEAD----------------------------LELQRKREYIEELEPPTDS---------------------------ST 560
Cdd:pfam05483 569 DKSEenarsieyevlkkekqmkilenkcnnlkKQIENKNKNIEELHQENKAlkkkgsaenkqlnayeikvnklelelaSA 648
|
410 420 430
....*....|....*....|....*....|....*.
gi 1732634088 561 ARRIEELQDSLQKKDADLRAMEERYRRYVDKARTVI 596
Cdd:pfam05483 649 KQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIA 684
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
206-693 |
1.32e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 206 EEKQNLAQENAALRERVGRSEVESApgltAKKLLLLQSQLEQLQEENFRLESSREDDRLRCLELEREVAELQQR-----N 280
Cdd:COG4913 262 ERYAAARERLAELEYLRAALRLWFA----QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgngG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 281 QALTSLSQEAQALKDEMDELRQSSERARQLEATLNScrRRLGELQELRRQVRQLEERNAGHAERTRQLEEELRRAGSLRA 360
Cdd:COG4913 338 DRLEQLEREIERLERELEERERRRARLEALLAALGL--PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 361 QLEAQRRQVQ-ELQGQWQ------EEAMKAEKWLfeCRNLEEK-------CDLV---TKEKE--------------RLLT 409
Cdd:COG4913 416 DLRRELRELEaEIASLERrksnipARLLALRDAL--AEALGLDeaelpfvGELIevrPEEERwrgaiervlggfalTLLV 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 410 ERDSLREANEELRCAQLQPR---GLAQADLSLDPTPSGLENLAAEIL---PAELRETLvrlqlenkrlcQQEAADR---- 479
Cdd:COG4913 494 PPEHYAAALRWVNRLHLRGRlvyERVRTGLPDPERPRLDPDSLAGKLdfkPHPFRAWL-----------EAELGRRfdyv 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 480 --ERQEELQRH--------LEEANRARHGLEAQQRL---------NQQQLSELRAQVEELQKALQEQGGKTEdKLHEADL 540
Cdd:COG4913 563 cvDSPEELRRHpraitragQVKGNGTRHEKDDRRRIrsryvlgfdNRAKLAALEAELAELEEELAEAEERLE-ALEAELD 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 541 ELQRKREYIEELEPPTDS-----STARRIEELQD---SLQKKDADLRAMEERyrryVDKARTVIQTLEpkqrpptvvsPE 612
Cdd:COG4913 642 ALQERREALQRLAEYSWDeidvaSAEREIAELEAeleRLDASSDDLAALEEQ----LEELEAELEELE----------EE 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 613 FHTLRSQLWERNLRIRQMEMDYEKSRRRQEQEEKLLISAWYSMGMALEHRAGEEHAPAHAQSFLAQQRLATNARRGPLGR 692
Cdd:COG4913 708 LDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
|
.
gi 1732634088 693 Q 693
Cdd:COG4913 788 E 788
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
253-584 |
1.53e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.88 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 253 FRLESSREDDRLRCLELEREVAELQQRNQALTSLSQEAQaLKDEMDELRQSSERARQLEATLNSCRRRLGELQELRRQvr 332
Cdd:pfam02463 673 KELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEE-LKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEE-- 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 333 qlEERNAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTERD 412
Cdd:pfam02463 750 --EEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 413 SLREANEELRCAQLQPRGLAQADLSLDPTPSGLENLAAEILPAELRETLVRLQLENKRLCQQEAADRERQEE-----LQR 487
Cdd:pfam02463 828 EKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKkeleeESQ 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 488 HLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDKLHEADLELQRKREYIEELEPPTDSSTARRIEEL 567
Cdd:pfam02463 908 KLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKE 987
|
330
....*....|....*..
gi 1732634088 568 QDSLQKKDADLRAMEER 584
Cdd:pfam02463 988 ERYNKDELEKERLEEEK 1004
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
185-651 |
2.13e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.58 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 185 EEGDHLQQHYLDLERQLLLLSEEKQNLAQENAALRERVGRSEVESAPGLTAKKLLLLQSQLEQLQEENFRLESSREDDRL 264
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELER 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 265 RCLELEREVAELQQRNQALTSLSQEAQ-------ALKDEMDELRQSSERARQLEA---TLNSCRRRLGELQELRRQVRQ- 333
Cdd:TIGR02168 459 LEEALEELREELEEAEQALDAAERELAqlqarldSLERLQENLEGFSEGVKALLKnqsGLSGILGVLSELISVDEGYEAa 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 334 LEERNAGH--------AERTRQLEEELRRAGSLRAQ-LEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEK 404
Cdd:TIGR02168 539 IEAALGGRlqavvvenLNAAKKAIAFLKQNELGRVTfLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAL 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 405 ERLLTE---RDSLREANEELRcaQLQPRGL---AQADL---------SLDPTPSGLENLAAEIlpAELRETLVRLQLENK 469
Cdd:TIGR02168 619 SYLLGGvlvVDDLDNALELAK--KLRPGYRivtLDGDLvrpggvitgGSAKTNSSILERRREI--EELEEKIEELEEKIA 694
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 470 RLCQQEAADRERQEELQRHLEEANRARHGLEAQQ----------RLNQQQLSELRAQVEELQKALQEQGGKTEDKLHEAD 539
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRQIsalrkdlarlEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 540 LELQRKREYIEELEPptdsstarRIEELQDSLQKKDADLRAMEERYRRYVDKARTVIQTLEPKQRPPTVVSPEFHTLRSQ 619
Cdd:TIGR02168 775 EELAEAEAEIEELEA--------QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
490 500 510
....*....|....*....|....*....|..
gi 1732634088 620 LWERNLRIRQMEMDYEKSRRRQEQEEKLLISA 651
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEELESELEAL 878
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
319-538 |
2.35e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.21 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 319 RRLGEL----------QELRRQVRQLE--ERNAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQgqwQEEAMkaekW 386
Cdd:COG0497 119 RELGELlvdihgqhehQSLLDPDAQREllDAFAGLEELLEEYREAYRAWRALKKELEELRADEAERA---RELDL----L 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 387 LFECRNLEEkCDLVTKEKERLLTERDSLREAnEELRcaqlqpRGLAQADLSLDPTPSGLENLAAEI---------LPAEL 457
Cdd:COG0497 192 RFQLEELEA-AALQPGEEEELEEERRRLSNA-EKLR------EALQEALEALSGGEGGALDLLGQAlralerlaeYDPSL 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 458 RETLVRL-----QLEN-----KRLCQQEAADRERQEELQRHLEEANRA--RHGL----------EAQQRLNQ-----QQL 510
Cdd:COG0497 264 AELAERLesaliELEEaaselRRYLDSLEFDPERLEEVEERLALLRRLarKYGVtveellayaeELRAELAElensdERL 343
|
250 260
....*....|....*....|....*...
gi 1732634088 511 SELRAQVEELQKALQEQGgkteDKLHEA 538
Cdd:COG0497 344 EELEAELAEAEAELLEAA----EKLSAA 367
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
465-647 |
2.50e-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: 41.26 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 465 QLENKRLcQQEAADRERQEELQRHLEEANRARHG-LEAQQRLNQQQLSELRAQVEELQKALQEqggktedklheadlELQ 543
Cdd:pfam17380 295 KMEQERL-RQEKEEKAREVERRRKLEEAEKARQAeMDRQAAIYAEQERMAMERERELERIRQE--------------ERK 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 544 RKREYIEELEPPTDSSTARRIEELQDSLQKKDadlrameERYRRYVDKARTVIQTLEPKQRPPTVVSPEFHTLRSQLWE- 622
Cdd:pfam17380 360 RELERIRQEEIAMEISRMRELERLQMERQQKN-------ERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEa 432
|
170 180 190
....*....|....*....|....*....|...
gi 1732634088 623 --------RNLRIRQMEMDYEKSRRRQEQEEKL 647
Cdd:pfam17380 433 rqrevrrlEEERAREMERVRLEEQERQQQVERL 465
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
252-582 |
2.52e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.36 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 252 NFRLESSREDDRLRCLELEReVAELQQRNQALTSLSQEAQALKDEMDELrqsSERARQLEATLNscRRRLGELQELRRQV 331
Cdd:pfam12128 319 KDRSELEALEDQHGAFLDAD-IETAAADQEQLPSWQSELENLEERLKAL---TGKHQDVTAKYN--RRRSKIKEQNNRDI 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 332 RQLEERNAGHAE-RTRQLEEEL----RRAGSLRAQLEAQRRQVQELQGQWQ-----------------EEAMKAEKWLFE 389
Cdd:pfam12128 393 AGIKDKLAKIREaRDRQLAVAEddlqALESELREQLEAGKLEFNEEEYRLKsrlgelklrlnqatatpELLLQLENFDER 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 390 CRNLEEKCDLVTKEKERLLTERDSLR----EANEELRCAQL----QPRGLAQADLSLDPTPSGL------------ENLA 449
Cdd:pfam12128 473 IERAREEQEAANAEVERLQSELRQARkrrdQASEALRQASRrleeRQSALDELELQLFPQAGTLlhflrkeapdweQSIG 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 450 AEILPAELRET----------------LVRLQLENKRLCQQEAADRErqEELQRHLEEANRARHGLEAQQRLNQQQLSEL 513
Cdd:pfam12128 553 KVISPELLHRTdldpevwdgsvggelnLYGVKLDLKRIDVPEWAASE--EELRERLDKAEEALQSAREKQAAAEEQLVQA 630
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1732634088 514 RAQVEELQKALQeqggKTEDKLHEADLELQRKREYIEELEPPTDSSTARRIEELQDSLQKKDADLRAME 582
Cdd:pfam12128 631 NGELEKASREET----FARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLD 695
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
281-453 |
3.71e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.61 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 281 QALTSLSQEAQALKDEmDELRQSSERARQLEATLNSCRRRLGELQELRRQVRQLEERNAGHAERTRQLEEELRRAGS--- 357
Cdd:COG2433 380 EALEELIEKELPEEEP-EAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSeer 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 358 --LRAQLEAQRRQ--VQELQGQWQEEAMKAEKW------LFECRNLEEKCDLVTKEKERLLTeRDSLREANEELrcaqlq 427
Cdd:COG2433 459 reIRKDREISRLDreIERLERELEEERERIEELkrklerLKELWKLEHSGELVPVKVVEKFT-KEAIRRLEEEY------ 531
|
170 180
....*....|....*....|....*.
gi 1732634088 428 prGLAQADLSLDPTPSGLENLAAEIL 453
Cdd:COG2433 532 --GLKEGDVVYLRDASGAGRSTAELL 555
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
479-643 |
4.25e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.43 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 479 RERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTED---KLHEADLELQRKREYIEELEpP 555
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAlanEISRLEQQKQILRERLANLE-R 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 556 TDSSTARRIEELQDSLQKKDADLRAMEERY----------RRYVDKARTVIQTLEPKQRPPTV----VSPEFHTLRSQLW 621
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLeelkeeleslEAELEELEAELEELESRLEELEEqletLRSKVAQLELQIA 396
|
170 180
....*....|....*....|..
gi 1732634088 622 ERNLRIRQMEMDYEKSRRRQEQ 643
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRER 418
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
473-573 |
4.82e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.75 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 473 QQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEqggkTEDKLHEADLELQRKREYIEEL 552
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRA----LEQELAALEAELAELEKEIAEL 95
|
90 100
....*....|....*....|.
gi 1732634088 553 EpptdsstaRRIEELQDSLQK 573
Cdd:COG4942 96 R--------AELEAQKEELAE 108
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
170-682 |
5.12e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.43 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 170 FDTQSRRYYFLSEEVEEGD----HLQQHYLDLERQLLLLSEEKQNLAQENAALRERVGRSEVESAPglTAKKLLLLQSQL 245
Cdd:TIGR02168 283 IEELQKELYALANEISRLEqqkqILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE--LKEELESLEAEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 246 EQLQEENFRLESSREDDRLRCLELEREVAELQQRNQALTS----LSQEAQALKDEMDELRQ--SSERARQLEATLNSCRR 319
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNeierLEARLERLEDRRERLQQeiEELLKKLEEAELKELQA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 320 RLGELQ----ELRRQVRQLEERNAGHAERTRQLEEELRRAG----SLRAQLEAQRRQVQELQGQWQE--EAMKAEKW--- 386
Cdd:TIGR02168 441 ELEELEeeleELQEELERLEEALEELREELEEAEQALDAAErelaQLQARLDSLERLQENLEGFSEGvkALLKNQSGlsg 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 387 -------LFECRNLEEKC----------DLVTKEKERLLTERDSLREAN------------------EELRCAQLQPRGL 431
Cdd:TIGR02168 521 ilgvlseLISVDEGYEAAieaalggrlqAVVVENLNAAKKAIAFLKQNElgrvtflpldsikgteiqGNDREILKNIEGF 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 432 AQADLSLDPTPSGLENL----------------AAEILPA-ELRETLVRLQ--LENKRLCQQEAADRERQEELQR--HLE 490
Cdd:TIGR02168 601 LGVAKDLVKFDPKLRKAlsyllggvlvvddldnALELAKKlRPGYRIVTLDgdLVRPGGVITGGSAKTNSSILERrrEIE 680
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 491 EANRARHGLEAQQRLNQQQLSELRAQVEELQKA---LQEQGGKTEDKLHEADLELQRKREYIEelepptdsstarRIEEL 567
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEEleqLRKELEELSRQISALRKDLARLEAEVE------------QLEER 748
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 568 QDSLQKKDADLRAMEERYRRYVDKARTVIQTLEPK----QRPPTVVSPEFHTLRSQLWERNLRIRQMEMDYEKSRRRQEQ 643
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEieelEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
570 580 590
....*....|....*....|....*....|....*....
gi 1732634088 644 EEKLLISAWYSMGMALEHRAGEEHAPAHAQSFLAQQRLA 682
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEEL 867
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
274-526 |
7.69e-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: 7.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 274 AELQQRNQALTSLSQEAQALKDEMDELRQSSERARQLEATLN-------------------SCRRRLGELQELRRQVRQl 334
Cdd:COG3096 836 AELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNkllpqanlladetladrleELREELDAAQEAQAFIQQ- 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 335 eernagHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAE------------KWLFECRNLEEKCDLVTK 402
Cdd:COG3096 915 ------HGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFalsevvqrrphfSYEDAVGLLGENSDLNEK 988
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 403 EKERLLTERDSLREANEELRCAQLQPRGLAQADLSLDptpSGLENlAAEILpAELRETLVRLQLENkrlcQQEAADRERQ 482
Cdd:COG3096 989 LRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLK---SSRDA-KQQTL-QELEQELEELGVQA----DAEAEERARI 1059
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1732634088 483 EELQRHlEEANRARhgleaqQRLNQ--QQLSELRAQVEELQKALQE 526
Cdd:COG3096 1060 RRDELH-EELSQNR------SRRSQleKQLTRCEAEMDSLQKRLRK 1098
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
498-611 |
8.84e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.42 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634088 498 GLEAQQRLNQQQLSE---LRAQVEELQKALQEQGGKTEDKLHEADLELQRK-REYIEELEpptdSSTARRIEELQDSLQK 573
Cdd:PRK00409 524 SLEELERELEQKAEEaeaLLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEaQQAIKEAK----KEADEIIKELRQLQKG 599
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1732634088 574 KDADLRA--MEERYRRYVDKARTVIQTLEPKQRPPTVVSP 611
Cdd:PRK00409 600 GYASVKAheLIEARKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| |
