|
Name |
Accession |
Description |
Interval |
E-value |
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
186-719 |
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: 644.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 186 ELQEALAEKEELKQRCQELDMQVTALQDEKNSLVSENEMMNEKLDQLDgSFDDPNTMVAKKYFHVQLQLEQLQEENYRLE 265
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLE-SGDDSGTPGGKKYLLLQKQLEQLQEENFRLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 266 AAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEVYRQKLQDLNDLRKQVKSLQE 345
Cdd:pfam05622 80 TARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLGDLRRQVKLLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 346 TNMMYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKE 425
Cdd:pfam05622 160 RNAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 426 TNEELRCSKAQQDHLNQADSSATKSY---ENLAAEIMPVEYREVFIRLQHENKMLRLQQEGTENERIEQLQEQLEQKHRK 502
Cdd:pfam05622 240 TNEELRCAQLQQAELSQADALLSPSSdpgDNLAAEIMPAEIREKLIRLQHENKMLRLGQEGSYRERLTELQQLLEDANRR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 503 MNELETEQRLSKERIGELQQQIEDLQKSLQEQgsKSEGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDISQN- 581
Cdd:pfam05622 320 KNELETQNRLANQRILELQQQVEELQKALQEQ--GSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNl 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 582 AQKISELEAALQKKDEDMKAMEERYKMYLEKARNVIKTLDPKLNPAS-AEIMLLRKQLAEKDRRIEILESECKVAKF-RD 659
Cdd:pfam05622 398 AQKIDELQEALRKKDEDMKAMEERYKKYVEKAKSVIKTLDPKQNPASpPEIQALKNQLLEKDKKIEHLERDFEKSKLqRE 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 660 YEEKLIVSAWYNKSLAFQKLGMESRLVSGASackdsvaaaPARSFLAQQRHITSTRRNLS 719
Cdd:pfam05622 478 QEEKLIVTAWYNMGMALHRKAIEERLAGLSS---------PGQSFLARQRQATNARRGLS 528
|
|
| HkD_Hook1 |
cd22225 |
Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a ... |
15-163 |
6.51e-96 |
|
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: 293.30 E-value: 6.51e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 15 CDSLIIWLQTFKTASPCQDVKQLTNGVTMAQVLHQIDVAWFSESWLSRIKDDVGDNWRIKASNLKKVLHGITSYYHEFLG 94
Cdd:cd22225 2 CDSLIIWLQTFNTAAPCQTVQDLTSGVAMAQVLHQIDSSWFDESWLSRIKEDVGDNWRIKMSNLKKILQGIVDYYHEFLD 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157818007 95 QQISEELIPDLNQITESSDPVELGRLLQLILGCAVNCEKKQEHIKNIMTLEESVQHVVMTAIQELMSKE 163
Cdd:cd22225 82 QQISEFLLPDLNRIAEHSDPVELGRLLQLILGCAVNCEKKQEHIQNIMTLEESVQHVVMTAIQELMSKE 150
|
|
| HOOK_N |
pfam19047 |
HOOK domain; This domain is found at the N-terminus of HOOK proteins. |
15-163 |
6.19e-87 |
|
HOOK domain; This domain is found at the N-terminus of HOOK proteins.
Pssm-ID: 465958 Cd Length: 151 Bit Score: 270.05 E-value: 6.19e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 15 CDSLIIWLQTFKTASPCQDVKQLTNGVTMAQVLHQIDVAWFSESWLSRIKDDVGDNWRIKASNLKKVLHGITSYYHEFLG 94
Cdd:pfam19047 3 CDSLLTWLQTFNVPAPCATVEDLTDGVAMAQVLHQIDPSWFTEAWLSRIKEDVGDNWRLKVSNLKKILQSVVDYYQDVLG 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157818007 95 QQISEELIPDLNQITESSDPVELGRLLQLILGCAVNCEKKQEHIKNIMTLEESVQHVVMTAIQELMSKE 163
Cdd:pfam19047 83 QQISDFLLPDVNLIGEHSDPAELGRLLQLILGCAVNCEKKQEYIQQIMTLEESVQHVVMTAIQELMSKD 151
|
|
| HkD_Hook |
cd22222 |
Hook domain found in Hook family of microtubule-binding proteins; The Hook family includes ... |
15-161 |
3.14e-83 |
|
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: 260.26 E-value: 3.14e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 15 CDSLIIWLQTFKTASPCQDVKQLTNGVTMAQVLHQIDVAWFSESWLSRIKDDVGDNWRIKASNLKKVLHGITSYYHEFLG 94
Cdd:cd22222 1 CDSLLQWLQTFNLIAPHATAEDLSDGVAIAQVLNQIDPEYFSDSWLSKIKPDVGDNWRLKVSNLKKILKGIVDYYSEVLG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157818007 95 QQISEELIPDLNQITESSDPVELGRLLQLILGCAVNCEKKQEHIKNIMTLEESVQHVVMTAIQELMS 161
Cdd:cd22222 81 QQISGFTMPDVNAIAEKEDPKELGRLLQLVLGCAVNCERKEEYIQAIMGLEESVQHVVMEAIQELMS 147
|
|
| HkD_Hook3 |
cd22226 |
Hook domain found in protein Hook 3 (Hook3) and similar proteins; Hook3 is an adaptor protein ... |
15-162 |
4.85e-69 |
|
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: 223.31 E-value: 4.85e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 15 CDSLIIWLQTFKTASPCQDVKQLTNGVTMAQVLHQIDVAWFSESWLSRIKDDVGDNWRIKASNLKKVLHGITSYYHEFLG 94
Cdd:cd22226 6 CESLLTWIQTFNVDAPCQTVEDLTSGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEILG 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157818007 95 QQISEELIPDLNQITESSDPVELGRLLQLILGCAVNCEKKQEHIKNIMTLEESVQHVVMTAIQELMSK 162
Cdd:cd22226 86 QQINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMSK 153
|
|
| HkD_Hook2 |
cd22227 |
Hook domain found in protein Hook 2 (Hook2) and similar proteins; Hook2 is a ... |
15-162 |
8.36e-68 |
|
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: 219.75 E-value: 8.36e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 15 CDSLIIWLQTFKTASPCQDVKQLTNGVTMAQVLHQIDVAWFSESWLSRIKDDVGDNWRIKASNLKKVLHGITSYYHEFLG 94
Cdd:cd22227 3 CDSLLTWLQTFQVPSPCSSYQDLTSGVAIAQVLNRIDPSWFNEAWLGRIKEDTGDNWRLKVSNLKKILQSLLEYYQDVLG 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157818007 95 QQISEELIPDLNQITESSDPVELGRLLQLILGCAVNCEKKQEHIKNIMTLEESVQHVVMTAIQELMSK 162
Cdd:cd22227 83 HQVSEDHLPDVNLIGEFSDDTELGKLLQLVLGCAISCEKKQEHIQQIMTLEESVQHVVMEAIQELLTK 150
|
|
| HkD_SF |
cd22211 |
Hook domain-containing proteins superfamily; The Hook domain superfamily includes Hook adaptor ... |
16-161 |
1.85e-49 |
|
Hook domain-containing proteins superfamily; The Hook domain superfamily includes Hook adaptor proteins, Hook-related proteins and nuclear mitotic apparatus protein (NuMA). They share an N-terminal conserved globular Hook domain, which folds as a variant of the helical calponin homology (CH) domain with an extended alpha-helix. The Hook domain is responsible for the binding of microtubule. The Hook family includes microtubule-binding proteins, Hook1-3. Hook1 is required for spermatid differentiation. Hook2 contributes to the establishment and maintenance of centrosome function. Hook3 is an adaptor protein for microtubule-dependent intracellular vesicle and protein trafficking, and is involved in Golgi and endosome transport. Hook proteins are components of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex. The Hook-related protein (HkRP) family includes Daple, Girdin and Gipie. Daple, also called Dvl-associating protein with a high frequency of leucine residues, or coiled-coil domain-containing protein 88C(CCDC88C), or Hook-related protein 2 (HkRP2), is a novel non-receptor nucleotide exchange factor (GEF) required for activation of guanine nucleotide-binding proteins (G-proteins) during non-canonical Wnt signaling. Girdin, also called Akt phosphorylation enhancer (APE), or coiled-coil domain-containing protein 88A (CCDC88A), or G alpha-interacting vesicle-associated protein (GIV), or Girders of actin filament, or Hook-related protein 1 (HkRP1), is a bifunctional modulator of guanine nucleotide-binding proteins (G proteins). Gipie, also called GRP78-interacting protein induced by ER stress, or coiled-coil domain-containing protein 88B(CCDC88B), or brain leucine zipper domain-containing protein, or Hook-related protein 3 (HkRP3), is a novel actin cytoskeleton-binding protein and Akt substrate that regulates cell migratory responses in various biological contexts. NuMA, also called nuclear mitotic apparatus protein 1, or nuclear matrix protein-22 (NMP-22), or SP-H antigen, is a microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignment and the segregation of chromosomes during mitotic cell division.
Pssm-ID: 411792 Cd Length: 145 Bit Score: 170.15 E-value: 1.85e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 16 DSLIIWLQTFKTASPCQDVKQLTNGVTMAQVLHQIDVAWFSESWLSriKDDVGDNWRIKASNLKKVLHGITSYYHEFLGQ 95
Cdd:cd22211 2 AALLAWINTFPLSSPVESLDDLSDGVVLAEILSQIDPSYFDSEWLE--SRDSSDNWVLKLNNLKKLYRSLSKYYREVLGQ 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157818007 96 QISEELIPDLNQITESSDPVELGRLLQLILGCAVNCEKKQEHIKNIMTLEESVQHVVMTAIQELMS 161
Cdd:cd22211 80 QLSDLPLPDLSAIARDGDEEEIVKLLELVLGAAVQCENKEEYIARIQQLDESTQAELMLIIQEVLE 145
|
|
| HkD_HkRP |
cd22223 |
Hook domain found in the Hook-related protein (HkRP) family; The HkRP family includes Daple, ... |
17-159 |
7.81e-26 |
|
Hook domain found in the Hook-related protein (HkRP) family; The HkRP family includes Daple, Girdin and Gipie. Daple, also called Dvl-associating protein with a high frequency of leucine residues, or coiled-coil domain-containing protein 88C (CCDC88C), or Hook-related protein 2 (HkRP2), is a novel non-receptor nucleotide exchange factor (GEF) required for activation of guanine nucleotide-binding proteins (G-proteins) during non-canonical Wnt signaling. Girdin, also called Akt phosphorylation enhancer (APE), or coiled-coil domain-containing protein 88A (CCDC88A), or G alpha-interacting vesicle-associated protein (GIV), or Girders of actin filament, or Hook-related protein 1 (HkRP1), is a bifunctional modulator of guanine nucleotide-binding proteins (G proteins). It acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein G(i) alpha subunits. It also acts as a guanine nucleotide dissociation inhibitor for guanine nucleotide-binding protein G(s) subunit alpha GNAS. In addition, Girdin plays an essential role in cell migration. Gipie, also called GRP78-interacting protein induced by ER stress, or coiled-coil domain-containing protein 88B (CCDC88B), or brain leucine zipper domain-containing protein, or Hook-related protein 3 (HkRP3), is a novel actin cytoskeleton-binding protein and Akt substrate that regulates cell migratory responses in various biological contexts. It acts as a positive regulator of T-cell maturation and inflammatory function. As a microtubule-binding protein, Gipie regulates lytic granule clustering and NK cell killing. All family members contain a conserved globular Hook domain which folds as a variant of the helical calponin homology (CH) domain.
Pssm-ID: 411794 Cd Length: 149 Bit Score: 103.82 E-value: 7.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 17 SLIIWLQTFKTASPCQ-DVKQLTNGVTMAQVLHQIDVAWFSESWLSRIKDDVgdNWRIKasNLKKVLHGITSYYHEFLGQ 95
Cdd:cd22223 5 PLVTWAKTFADDGSAElSYTDLVDGVFLNNVMLQIDPRPFSEVSNRNVDDDV--NARIQ--NLDLLLRNIKSFYQEVLQQ 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157818007 96 QISEELiPDLNQITESSDP----VELGRLLQLILGCAVNCEKKQEHIKNIMTLEESVQHVVMTAIQEL 159
Cdd:cd22223 81 LIVMKL-PDILTIGREPESeqslEELEKLLLLLLGCAVQCERKEEFIERIKNLDLEVQHALVACIQEV 147
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
271-618 |
8.05e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.40 E-value: 8.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 271 YRVHCEELEKQLIEFQHRNDELTSLAEEtraLKDEIDVLRATSDKANKLESTVEVYRQKLQDL--NDLRKQVKSLQETNM 348
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDRLEDILNE---LERQLKSLERQAEKAERYKELKAELRELELALlvLRLEELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 349 MYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLieqRDTLKETNE 428
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL---ERQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 429 ELRCSKAQQDHLNQADSSATKSYENLAAEImpVEYREVFIRLQHENKMLrlqqegteNERIEQLQEQLEQKHRKMNELET 508
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEELKEEL--ESLEAELEELEAELEEL--------ESRLEELEEQLETLRSKVAQLEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 509 EQRLSKERIGELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDISQNAQKISEL 588
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEA 473
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 157818007 589 EAALQKKDED----------MKAMEERYKMYLEKARNVIK 618
Cdd:TIGR02168 474 EQALDAAERElaqlqarldsLERLQENLEGFSEGVKALLK 513
|
|
| HkD_Daple |
cd22228 |
Hook domain found in Daple (Dvl-associating protein with a high frequency of leucine residues) ... |
18-159 |
1.79e-12 |
|
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: 65.72 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 18 LIIWLQTFKTASPCQDVK-----QLTNGVTMAQVLHQIDVAWFSEswlsRIKDDVGDNWRIKASNLKKVLHGITSYYHEF 92
Cdd:cd22228 6 LVTWVKTFGPLGFGSEDKlsmymDLVDGVFLNKIMLQIDPRPTNQ----RVNKHVNNDVNLRIQNLTILVRHIKTYYQEV 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157818007 93 LGQQISEELiPDLNQIteSSDPV------ELGRLLQLILGCAVNCEKKQEHIKNIMTLEESVQHVVMTAIQEL 159
Cdd:cd22228 82 LQQLIVMNL-PNVLMI--GKDPLsgksmeEIKKMLLLVLGCAVQCERKEEFIERIKQLDIETQAAIVSHIQEV 151
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
291-651 |
3.58e-12 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 70.15 E-value: 3.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 291 ELTSLAEETRALKDEIDVLRATSDkaNKLESTVEVYRQKLQDL-NDLRKQVKSLQETNMMYMHNTVSLEEELKK-ANAAR 368
Cdd:pfam15921 232 EISYLKGRIFPVEDQLEALKSESQ--NKIELLLQQHQDRIEQLiSEHEVEITGLTEKASSARSQANSIQSQLEIiQEQAR 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 369 AQLETYKRQVQDLHTKLSSeskradtLAFEMKRLEEKHETLLKEKERlieqrdTLKETNEELRCSKAQQDHLNQADSSAT 448
Cdd:pfam15921 310 NQNSMYMRQLSDLESTVSQ-------LRSELREAKRMYEDKIEELEK------QLVLANSELTEARTERDQFSQESGNLD 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 449 KSYENLAAEImpvEYREVFIRLQHENKMLRLQQEGTENERIEQLQEQLEQKHRKMNELETeqrLSKERIGELQQQIEDLQ 528
Cdd:pfam15921 377 DQLQKLLADL---HKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEA---LLKAMKSECQGQMERQM 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 529 KSLQEQGSKSEGESSskLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDISQNAQKISELEAALQKKDEDMKAMEERYKM 608
Cdd:pfam15921 451 AAIQGKNESLEKVSS--LTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDL 528
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 157818007 609 YLEKARNvIKTLDPKLNPASAEIMLLRKQLAEKDRRIEILESE 651
Cdd:pfam15921 529 KLQELQH-LKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQ 570
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
168-651 |
5.67e-12 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 69.38 E-value: 5.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 168 PASDAVGELEQQLKRALEELQEAlaEKEELKQRCQELDMQVTALQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAKky 247
Cdd:pfam15921 242 PVEDQLEALKSESQNKIELLLQQ--HQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMR-- 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 248 fHVQLQLEQLQEENYRLEAAKDDYRVHCEELEKQLI----EFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLES-- 321
Cdd:pfam15921 318 -QLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVlansELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSle 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 322 ----------------TVEVYRQKLQD-------LNDLRKQVKSLQETNM-MYMHNTVSLEEELKKANAARAQLETYK-- 375
Cdd:pfam15921 397 keqnkrlwdrdtgnsiTIDHLRRELDDrnmevqrLEALLKAMKSECQGQMeRQMAAIQGKNESLEKVSSLTAQLESTKem 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 376 --RQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKETNEELRCSKAQQDHLNQADSSATKSYEN 453
Cdd:pfam15921 477 lrKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQ 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 454 LAAEIMPVEyrevFIRLQHENKMLRLQQEGTENERIE----QLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQK 529
Cdd:pfam15921 557 MAEKDKVIE----ILRQQIENMTQLVGQHGRTAGAMQvekaQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLEL 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 530 SlqeqgsksegesssklKQKL-EAHMEKLTEVHEELQKKQELIEDLQP---DISQNAQKISELEAALQKKDEDMKAMEER 605
Cdd:pfam15921 633 E----------------KVKLvNAGSERLRAVKDIKQERDQLLNEVKTsrnELNSLSEDYEVLKRNFRNKSEEMETTTNK 696
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 157818007 606 YKMYL-------EKARNVIKTLDPKLNPASAEIMLLRKQLAEKDRRIEILESE 651
Cdd:pfam15921 697 LKMQLksaqselEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSK 749
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
154-651 |
7.81e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.93 E-value: 7.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 154 TAIQELMSKEIVSSPASDAVGELEQqLKRALEELQEAL----AEKEELKQRCQELDMQVTALQDEKNSLVSENEMMNEKL 229
Cdd:TIGR02168 420 QQEIEELLKKLEEAELKELQAELEE-LEEELEELQEELerleEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 230 DQLDGSFDDPNTMVAKKY----FHVQLQLEQLQEENYR------LEAAKDDYRVHCEELEKQLIEFQHRNdeltslaEET 299
Cdd:TIGR02168 499 ENLEGFSEGVKALLKNQSglsgILGVLSELISVDEGYEaaieaaLGGRLQAVVVENLNAAKKAIAFLKQN-------ELG 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 300 RALKDEIDVLRATSDKANKLEStVEVYRQKLQDLNDLRKQVKSLQEtNMMYMHNTVSLEEELKKANAARAQLETYKRQVQ 379
Cdd:TIGR02168 572 RVTFLPLDSIKGTEIQGNDREI-LKNIEGFLGVAKDLVKFDPKLRK-ALSYLLGGVLVVDDLDNALELAKKLRPGYRIVT 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 380 DLHTKLS--------SESKRADTLA--FEMKRLEEKHETLLKE----KERLIEQRDTLKETNEELRCSKAQQDHLNQADS 445
Cdd:TIGR02168 650 LDGDLVRpggvitggSAKTNSSILErrREIEELEEKIEELEEKiaelEKALAELRKELEELEEELEQLRKELEELSRQIS 729
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 446 SATKSYENLAAEIMPVEYRevFIRLQHENKMLRlQQEGTENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIE 525
Cdd:TIGR02168 730 ALRKDLARLEAEVEQLEER--IAQLSKELTELE-AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD 806
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 526 DLQKSLQEQGSK--SEGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDISQNAQKISELEAALQKKDEDMKAME 603
Cdd:TIGR02168 807 ELRAELTLLNEEaaNLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 157818007 604 ERYKMY---LEKARNVIKTLDPKLNPASAEIMLLRKQLAEKDRRIEILESE 651
Cdd:TIGR02168 887 EALALLrseLEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR 937
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
368-651 |
1.32e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 368 RAQLETYKRQVQD--LHTKLSSESKRADTLAF---------EMKRLEEKHETLLKEKERLIEQRDTLKETNEELRcskAQ 436
Cdd:COG1196 199 ERQLEPLERQAEKaeRYRELKEELKELEAELLllklreleaELEELEAELEELEAELEELEAELAELEAELEELR---LE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 437 QDHLNQADSSATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGTENERIEQLQEQLEQkhrKMNELETEQRLSKER 516
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE---ELEELEEELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 517 IGELQQQIEDLQKSLQEQgSKSEGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQpdisQNAQKISELEAALQKKD 596
Cdd:COG1196 353 LEEAEAELAEAEEALLEA-EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE----ALLERLERLEEELEELE 427
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 157818007 597 EDMKAMEERykmyLEKARNVIKTLDPKLNPASAEIMLLRKQLAEKDRRIEILESE 651
Cdd:COG1196 428 EALAELEEE----EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
171-641 |
1.58e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 67.76 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 171 DAVGELEQQLKraleELQEALAEKEELKQRCQEldmqvtaLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAKKyfhv 250
Cdd:PRK02224 206 ERLNGLESELA----ELDEEIERYEEQREQARE-------TRDEADEVLEEHEERREELETLEAEIEDLRETIAET---- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 251 qlqleqlqeenyrlEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRAT-SDKANKLESTVEVYRQK 329
Cdd:PRK02224 271 --------------EREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREElEDRDEELRDRLEECRVA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 330 LQDLND----LRKQVKSLQETNMMYMHNTVSLEEELKkanAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEK 405
Cdd:PRK02224 337 AQAHNEeaesLREDADDLEERAEELREEAAELESELE---EAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDF 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 406 HETLLKEKERLIEQRDTLKETNEELRCSKAQQDHLNQADSSATKSYENLAAEIMPV--EYREVFIRLQHENKMLRLQQEG 483
Cdd:PRK02224 414 LEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETieEDRERVEELEAELEDLEEEVEE 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 484 TEN--ERIEQLQEQLEQKHRKMNELET-EQRLS--KERIGELQQQIEDLQKSLQEqgsksegessskLKQKLEAHMEKLT 558
Cdd:PRK02224 494 VEErlERAEDLVEAEDRIERLEERREDlEELIAerRETIEEKRERAEELRERAAE------------LEAEAEEKREAAA 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 559 EVHEELQKKQELIEDLQPDISQNAQKISELEA----------------ALQKKDEDMKAMEERYKMYLEKARNVIKTLDP 622
Cdd:PRK02224 562 EAEEEAEEAREEVAELNSKLAELKERIESLERirtllaaiadaedeieRLREKREALAELNDERRERLAEKRERKRELEA 641
|
490
....*....|....*....
gi 157818007 623 KLNPASAEIMLLRKQLAEK 641
Cdd:PRK02224 642 EFDEARIEEAREDKERAEE 660
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
169-651 |
1.72e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 67.76 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 169 ASDA---VGELEQQLKRALEELQEALAEKEElkqrcQELDMQVTALQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAK 245
Cdd:PRK02224 171 ASDArlgVERVLSDQRGSLDQLKAQIEEKEE-----KDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 246 kyfHVQLQLEQLqeenyRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEEtraLKDEIDVLRATSDKANKLESTVEV 325
Cdd:PRK02224 246 ---HEERREELE-----TLEAEIEDLRETIAETEREREELAEEVRDLRERLEE---LEEERDDLLAEAGLDDADAEAVEA 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 326 YRQKLQD--------LNDLRKQVKSLQETNMMYMHNTVSLEEELKKA-----------NAARAQLETYKRQVQDLHTKLS 386
Cdd:PRK02224 315 RREELEDrdeelrdrLEECRVAAQAHNEEAESLREDADDLEERAEELreeaaeleselEEAREAVEDRREEIEELEEEIE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 387 SESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKETNEELRCSKAQQDHLNQADSSATKSYENLAAEIMPV--EYR 464
Cdd:PRK02224 395 ELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETieEDR 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 465 EVFIRLQHENKMLRLQQEGTEN--ERIEQLQEQLEQKHRKMNELET-EQRLS--KERIGELQQQIEDLQKSLQEqgskse 539
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVEErlERAEDLVEAEDRIERLEERREDlEELIAerRETIEEKRERAEELRERAAE------ 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 540 gessskLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDISQNAQ------KISELEAALQKKDEDMKAMEERYKMYLEKA 613
Cdd:PRK02224 549 ------LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKEriesleRIRTLLAAIADAEDEIERLREKREALAELN 622
|
490 500 510
....*....|....*....|....*....|....*...
gi 157818007 614 RnviktldpklnpasaeimLLRKQLAEKDRRIEILESE 651
Cdd:PRK02224 623 D------------------ERRERLAEKRERKRELEAE 642
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
276-593 |
2.17e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 276 EELEKQLiefqhrnDELT---SLAEETRALKDEIDVLRA--TSDKANKLESTVEVYRQKLQDL-NDLRKQVKSLQETNMM 349
Cdd:COG1196 196 GELERQL-------EPLErqaEKAERYRELKEELKELEAelLLLKLRELEAELEELEAELEELeAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 350 YMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKETNEE 429
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 430 LrcsKAQQDHLNQADSSATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGTENERIEQLQEQLEQkhrKMNELETE 509
Cdd:COG1196 349 A---EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE---RLERLEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 510 QRLSKERIGELQQQIEDLQKSLQEQgskseGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDISQNAQKISELE 589
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEA-----AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
....
gi 157818007 590 AALQ 593
Cdd:COG1196 498 EAEA 501
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
353-651 |
3.21e-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: 67.02 E-value: 3.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 353 NTVSLEEELKKAnaaRAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKETNEELRc 432
Cdd:TIGR02169 668 FSRSEPAELQRL---RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELE- 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 433 skAQQDHLNQAdssatksYENLAAEIMPVEyrevfirlqhenkmlrlqqegtenERIEQLQEQLEQKHRKMNELEteQRL 512
Cdd:TIGR02169 744 --EDLSSLEQE-------IENVKSELKELE------------------------ARIEELEEDLHKLEEALNDLE--ARL 788
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 513 SKERIGELQQQIEDLQKSLQEQGSKSEGessskLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDISQNAQKI------- 585
Cdd:TIGR02169 789 SHSRIPEIQAELSKLEEEVSRIEARLRE-----IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIenlngkk 863
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157818007 586 SELEAALQKKDEDMKAMEERY---KMYLEKARNVIKTLDPKLNPASAEIMLLRKQLAEKDRRIEILESE 651
Cdd:TIGR02169 864 EELEEELEELEAALRDLESRLgdlKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
263-604 |
8.53e-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: 65.46 E-value: 8.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 263 RLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDV-LRATSDKANKLESTVEVYRQKLQDLNDLRKQV- 340
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqISALRKDLARLEAEVEQLEERIAQLSKELTELe 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 341 KSLQETNMMYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQR 420
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 421 DTLKETNEELRcskAQQDHLNQADSSATKSYENLAAEimpveyrevfirLQHEnkmlrLQQEGTENERIEQLQEQLEQKH 500
Cdd:TIGR02168 841 EDLEEQIEELS---EDIESLAAEIEELEELIEELESE------------LEAL-----LNERASLEEALALLRSELEELS 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 501 RKMNELETEQRLSKERIGELQQQIEDLQKSLQEqgsksegessskLKQKLEAHMEKLTEVHE-ELQKKQELIEDLQPDIS 579
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLEG------------LEVRIDNLQERLSEEYSlTLEEAEALENKIEDDEE 968
|
330 340
....*....|....*....|....*.
gi 157818007 580 QNAQKISELEAALQKKDE-DMKAMEE 604
Cdd:TIGR02168 969 EARRRLKRLENKIKELGPvNLAAIEE 994
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
175-532 |
1.42e-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: 65.08 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 175 ELEQQLKRALEELQEALAEKEELKQRCQELDMQVTALQDEKNSLVSENEMMNEKLDQLDGsfddpntmvakkyfhvqlql 254
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK-------------------- 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 255 eqlqeenyRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANK-LESTVEVYRQKLQDL 333
Cdd:TIGR02168 755 --------ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAeLTLLNEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 334 NDLRKQVKSLQETNMMYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMK-RLEEKHETLLKE 412
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRsELEELSEELREL 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 413 KERLIEQRDTLKETNE-----ELRCSKAQQDHLNQADsSATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQE----G 483
Cdd:TIGR02168 907 ESKRSELRRELEELREklaqlELRLEGLEVRIDNLQE-RLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKikelG 985
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 157818007 484 TENER-IEQLQEQleqkhrkmneleteqrlsKERIGELQQQIEDLQKSLQ 532
Cdd:TIGR02168 986 PVNLAaIEEYEEL------------------KERYDFLTAQKEDLTEAKE 1017
|
|
| HkD_Girdin |
cd22229 |
Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation ... |
18-159 |
1.85e-10 |
|
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: 59.80 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 18 LIIWLQTF-----KTASPCQDVKQLTNGVTMAQVLHQIDvawfSESWLSRIKDDVGDNWRIKASNLKKVLHGITSYYHEF 92
Cdd:cd22229 9 LVTWVKTFgplatGNGTPLDEYVALVDGVFLNEVMLQIN----PKSSNQRVNKKVNNDASLRIQNLSILVKQIKLYYQET 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157818007 93 LGQQISEELiPDL-----NQITESSDPvELGRLLQLILGCAVNCEKKQEHIKNIMTLEESVQHVVMTAIQEL 159
Cdd:cd22229 85 LQQLIMMSL-PNVlvlgrNPLSEQGTE-EMKKLLLLLLGCAVQCERKEEFIERIQTLDFDTKAAVAAHIQEV 154
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
309-640 |
2.50e-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: 64.31 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 309 LRATSDKANKLESTVEVYRQKLQDLNDLRKQVKSLqetnmmymhntvsLEEELKKANAARAQLETYKRQVQDLhtklsse 388
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKE-------------LEELSRQISALRKDLARLEAEVEQL------- 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 389 SKRADTLAFEMKRLEEKHETLLkekERLIEQRDTLKETNEELRCSKAQQDHLNQADSSATKSYENLAAEIMpvEYREVFI 468
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELE---ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT--LLNEEAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 469 RLQHENKMLRLQQEGTEnERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQGSKSegesssklkQ 548
Cdd:TIGR02168 821 NLRERLESLERRIAATE-RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL---------A 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 549 KLEAHMEKL-TEVHEELQKKQELIEDLQPDISQNAQKISELEAALQKKDEDMKAMEERYKMYLEKARNVIKTLDPKLNPA 627
Cdd:TIGR02168 891 LLRSELEELsEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEA 970
|
330
....*....|...
gi 157818007 628 SAEIMLLRKQLAE 640
Cdd:TIGR02168 971 RRRLKRLENKIKE 983
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
132-664 |
7.34e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 7.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 132 EKKQEHIKNIMTLEESVQHVVMTAIQELMSKEIVSSPASDAVGELEQQLKRALEELQEALAEKE---ELKQRCQELDMQV 208
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEeieELEKELESLEGSK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 209 TALQDEKNSLVSENEMMNEKLDQLDGSFDDPNTM--VAKKYFHVQLQLEQLQEENYRLEAAKDDYRVHCEELEKQLIEFQ 286
Cdd:PRK03918 255 RKLEEKIRELEERIEELKKEIEELEEKVKELKELkeKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 287 HRNDELTSLAEETRALKDEIDVLRatsdkanKLESTVEVYRQKLQDLNDLRKQVKSLQETNMMYMHNTVS-----LEEEL 361
Cdd:PRK03918 335 EKEERLEELKKKLKELEKRLEELE-------ERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEkakeeIEEEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 362 KKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRlEEKHETLLKEKERLIEQRDTLKETNEELRCSKAQQDHLN 441
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTE-EHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELE 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 442 QADSSATK--SYENLAAEIMPVEYR-EVFIRLQHENKMLRLQQEGTENERIEQLQEQLEQKHRKMNELETEQRLSKERIG 518
Cdd:PRK03918 487 KVLKKESEliKLKELAEQLKELEEKlKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLD 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 519 ELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHME--KLTEVHEELQKKQELIEDLQPDISQNAQKISELEAALQKKD 596
Cdd:PRK03918 567 ELEEELAELLKELEELGFESVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELR 646
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157818007 597 EDMKAMEERY-KMYLEKARNVIKTLDPKLNPASAEIMLLRKQLAEKDRRIEILESEckVAKFRDYEEKL 664
Cdd:PRK03918 647 KELEELEKKYsEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE--LEEREKAKKEL 713
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
290-616 |
8.03e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.39 E-value: 8.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 290 DELTSLAEETRALKDEIDVLRatsDKANKLESTVEVYRQKLQDLNdlrKQVKSLQEtnmmymhntvSLEEELKKANAARA 369
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQ---SELRRIENRLDELSQELSDAS---RKIGEIEK----------EIEQLEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 370 QLETYKRQVQDLHTKLSSESKRADTLAfemKRLEEKHETLLKEKERL--IEQRDT----------LKETNEELRCSKAQQ 437
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELE---ARIEELEEDLHKLEEALndLEARLShsripeiqaeLSKLEEEVSRIEARL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 438 DHLNQADSSATKSYENLAAEImpvEYREVFIRLQHENKMLRLQQEGTENERIEQLQEQLEQKHRKMNELETEQRLSKERI 517
Cdd:TIGR02169 815 REIEQKLNRLTLEKEYLEKEI---QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 518 GELQQQIEDLQKSLQEQGSK--SEGESSSKLKQKLEAHMEKLTE--------------------VHEELQKKQELIEDLQ 575
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQieKKRKRLSELKAKLEALEEELSEiedpkgedeeipeeelsledVQAELQRVEEEIRALE 971
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 157818007 576 P-------DISQNAQKISELEAALQKKDEDMKAMEERYKMYLEKARNV 616
Cdd:TIGR02169 972 PvnmlaiqEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
403-651 |
8.33e-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: 8.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 403 EEKHETLLKekerLIEQRDTLKETNEELRCSKAQQDHLnQADSSATKSYENLAAEIMPVEYREVFIRL-QHENKMLRLQQ 481
Cdd:TIGR02168 172 ERRKETERK----LERTRENLDRLEDILNELERQLKSL-ERQAEKAERYKELKAELRELELALLVLRLeELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 482 EGTENER--------IEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQGSKSEGessskLKQKLEAH 553
Cdd:TIGR02168 247 ELKEAEEeleeltaeLQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN-----LERQLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 554 MEKLTEVHEELQKKQELIEDLQPDISQNAQKISELEAALQKKDEDMKAMEERykmylekarnvIKTLDPKLNPASAEIML 633
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR-----------LEELEEQLETLRSKVAQ 390
|
250
....*....|....*...
gi 157818007 634 LRKQLAEKDRRIEILESE 651
Cdd:TIGR02168 391 LELQIASLNNEIERLEAR 408
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
410-663 |
9.36e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.39 E-value: 9.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 410 LKEKERLIEQRDTLKETNEELRCSKAQQDHLNQADSSATKSYENLAAEIMpveyrevfiRLQHENKMLrLQQEGTENERI 489
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIG---------EIEKEIEQL-EQEEEKLKERL 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 490 EQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQGSKSEGESSsklkQKLEAHMEKLTEVHEELQKKQE 569
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI----PEIQAELSKLEEEVSRIEARLR 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 570 LIE----DLQPDISQNAQKISELE----------AALQKKDEDMKAMEERYKMYLEKARNVIKTLDPKLNPASAEIMLLR 635
Cdd:TIGR02169 816 EIEqklnRLTLEKEYLEKEIQELQeqridlkeqiKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE 895
|
250 260
....*....|....*....|....*...
gi 157818007 636 KQLAEKDRRIEILESECKVAKFRDYEEK 663
Cdd:TIGR02169 896 AQLRELERKIEELEAQIEKKRKRLSELK 923
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
414-650 |
1.49e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 414 ERLIEQRDTLKETNEELRCSKAQQDHLNQADSSATKsYENLAAEIMPVEYREVFIRLQHENKMLRLQQEgteneRIEQLQ 493
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLEPIRELAER-YAAARERLAELEYLRAALRLWFAQRRLELLEA-----ELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 494 EQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQgsksegessskLKQKLEAHMEKLTEVHEELQKKQELIED 573
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ-----------LEREIERLERELEERERRRARLEALLAA 370
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157818007 574 LQPDISQNAQKISELEAALQKKDEDMKAMEERykmylekarnviktLDPKLNPASAEIMLLRKQLAEKDRRIEILES 650
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAAALLEALEEELEA--------------LEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
363-664 |
1.63e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.62 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 363 KANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLE-------EKHET----LLKEKERLIEQRDT----LKETN 427
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAEryqallkEKREYegyeLLKEKEALERQKEAierqLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 428 EELRCSKAQQDHLNQADSSATKSYENLAAEIMPVEyrevfirlqhENKMLRLQQEGTENE-RIEQLQEQLEQKHRKMNEL 506
Cdd:TIGR02169 251 EELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG----------EEEQLRVKEKIGELEaEIASLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 507 ETEQRLSKERIGELQQQIEDLQKSLQEQGSKSE--GESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDISQNAQK 584
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDklTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 585 ISELEAALQKKDEDMKAMEERykmyLEKARNVIKTLDPKLNPASAEIMLLRKQLAEKDRRIEILeseckVAKFRDYEEKL 664
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEE----LADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL-----AADLSKYEQEL 471
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
178-620 |
2.14e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.82 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 178 QQLKRALEELQEALA----EKEELKQRCQELDMQVTALQDEKNSLVSENEMMNEKLDQLDGSFDDpntmVAKKYFHVQLQ 253
Cdd:PRK02224 254 ETLEAEIEDLRETIAeterEREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREE----LEDRDEELRDR 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 254 LEQLQEENYRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETR-----------ALKDEIDVLRATSDKANKLEST 322
Cdd:PRK02224 330 LEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAReavedrreeieELEEEIEELRERFGDAPVDLGN 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 323 VEVYRQKLQ-DLNDLRKQVKSLqETNMMYMHNTVSLEEELKKA----------------------NAARAQLETYKRQVQ 379
Cdd:PRK02224 410 AEDFLEELReERDELREREAEL-EATLRTARERVEEAEALLEAgkcpecgqpvegsphvetieedRERVEELEAELEDLE 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 380 DLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKETNEELRCSKAQQDHLN----QADSSATKSYENLA 455
Cdd:PRK02224 489 EEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEaeaeEKREAAAEAEEEAE 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 456 AEIMPV-----EYREVFIRLQHENKMLRLQQEGTENE-RIEQLQEQLEQKhrkmNELETEQRlskERIGELQQQIEDLQK 529
Cdd:PRK02224 569 EAREEVaelnsKLAELKERIESLERIRTLLAAIADAEdEIERLREKREAL----AELNDERR---ERLAEKRERKRELEA 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 530 SLQEqgsksegESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDISQNAQKISELEAAlqkkDEDMKAMEERyKMY 609
Cdd:PRK02224 642 EFDE-------ARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEEL----RERREALENR-VEA 709
|
490
....*....|.
gi 157818007 610 LEKARNVIKTL 620
Cdd:PRK02224 710 LEALYDEAEEL 720
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
175-662 |
2.53e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 175 ELEQQLKRALEELQEALAEKEELKQRCQELDMQVTALQDEKNSLVSENEMMNEKLDqldgsfddpntmvakkyfHVQLQL 254
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA------------------RLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 255 EQLQEENYRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEID--VLRATSDKANKLESTVEVYRQKLQD 332
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEeaLLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 333 LNDLRKQVKSLQETNMMYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKE 412
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 413 KERLIEQRDTLKETNEELRCSK-AQQDHLNQADSSATKSYENLAAEIMPVEYREVFIRLQHENK---------MLRLQQE 482
Cdd:COG1196 472 AALLEAALAELLEELAEAAARLlLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAyeaaleaalAAALQNI 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 483 GTENERIEQLQEQLEQKHRK----------------MNELETEQRLSKERIGELQQQIEDLQKSLQEQGSKSEGESSSKL 546
Cdd:COG1196 552 VVEDDEVAAAAIEYLKAAKAgratflpldkiraraaLAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAR 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 547 KQKLEAHMEKLTEVHEELQKKQELIEDLQPDISQNAQKISELEAALQKKDEDMKAMEERYKMYLEKARNVIKTLDPKLNP 626
Cdd:COG1196 632 LEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711
|
490 500 510
....*....|....*....|....*....|....*.
gi 157818007 627 ASAEIMLLRKQLAEKDRRIEILESECKVAKFRDYEE 662
Cdd:COG1196 712 AEEERLEEELEEEALEEQLEAEREELLEELLEEEEL 747
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
279-593 |
2.81e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.85 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 279 EKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKAN-KLESTVEVYRQKLQDLNDLRKQVKSLQETNMMYMHNTV-S 356
Cdd:TIGR02169 219 EKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTeEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIgE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 357 LEEELKKAnaaRAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKETNEELRCSKAQ 436
Cdd:TIGR02169 299 LEAEIASL---ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 437 QDHLNQADSSATKSYenlaaeimpveyREVFIRLQHENKMLRLQQEgtenerieQLQEQLEQKHRKMNELETEQRLSKER 516
Cdd:TIGR02169 376 VDKEFAETRDELKDY------------REKLEKLKREINELKRELD--------RLQEELQRLSEELADLNAAIAGIEAK 435
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157818007 517 IGELQQQIEDLQKSLQEQgsksegesssklKQKLEAHMEKLTEVHEELQKKQELIEDLQPDISQNAQKISELEAALQ 593
Cdd:TIGR02169 436 INELEEEKEDKALEIKKQ------------EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAR 500
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
263-592 |
3.06e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 263 RLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATsdkanklestvevYRQKLQDLNDLRKQVKS 342
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE-------------EYELLAELARLEQDIAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 343 LQETNmmyMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAfemKRLEEKHETLLKEKERLIEQRDT 422
Cdd:COG1196 307 LEERR---RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE---AELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 423 LKETNEELRCSKAQQDHLNQADSSATKSYENLAAEImpveyrevfIRLQHENKMLRLQQEGTENERIEQLQEQLEQKHRK 502
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERL---------ERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 503 MNELETEQRLSKERIGELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEELQKKQELiEDLQPDISQNA 582
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL-RGLAGAVAVLI 530
|
330
....*....|
gi 157818007 583 QKISELEAAL 592
Cdd:COG1196 531 GVEAAYEAAL 540
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
130-656 |
9.71e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 9.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 130 NCEKKQEHIKNIMTLEESVQHVVMTAIQELMSKEIVSSPASDAV----GELEQQLKRALEELQEALAEKEELKQRCQELD 205
Cdd:TIGR02168 299 RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELeeklEELKEELESLEAELEELEAELEELESRLEELE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 206 MQVTALQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAKkyfhvqLQLEQLQEENYRLEAAKDDYRVHCEELEKQLIEF 285
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER------LQQEIEELLKKLEEAELKELQAELEELEEELEEL 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 286 QHRND----ELTSLAEETRALKDEIDVLRATSDKANKLESTVEVYRQKLQDLNDLRKQVKSLQETNMMYMH---NTVSLE 358
Cdd:TIGR02168 453 QEELErleeALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGvlsELISVD 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 359 EELKKA-----------------NAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRD 421
Cdd:TIGR02168 533 EGYEAAieaalggrlqavvvenlNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDP 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 422 TLKETNEELRCSKAQQDHLNQADSSATKSYEN-----LAAEIMPVEYREVFIRLQHENKMLRLQQEGTENER-IEQLQEQ 495
Cdd:TIGR02168 613 KLRKALSYLLGGVLVVDDLDNALELAKKLRPGyrivtLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEkIEELEEK 692
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 496 LEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQgskseGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQ 575
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISAL-----RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 576 PDISQNAQKISELEAALQKKDEDMKAMEERYKMY---LEKARNVIKTLDPKLNPASAEIMLLRKQLAEKDRRIEILESEC 652
Cdd:TIGR02168 768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847
|
....
gi 157818007 653 KVAK 656
Cdd:TIGR02168 848 EELS 851
|
|
| HkD_Gipie |
cd22230 |
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar ... |
36-159 |
1.15e-08 |
|
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar proteins; Gipie, also called coiled-coil domain-containing protein 88B (CCDC88B), or brain leucine zipper domain-containing protein, or Hook-related protein 3 (HkRP3), is a novel actin cytoskeleton-binding protein and Akt substrate that regulates cell migratory responses in various biological contexts. It acts as a positive regulator of T-cell maturation and inflammatory function. As a microtubule-binding protein, Gipie regulates lytic granule clustering and NK cell killing.
Pssm-ID: 411801 Cd Length: 170 Bit Score: 55.22 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 36 QLTNGVTMAQVLHQIDVAwfSESWLSRIKDDVGDNWRIKasNLKKVLHGITSYYHEFLGQQIseeLIPDLNQITESSDPV 115
Cdd:cd22230 46 RLSNGDLLNRVMGIIDPS--PRGGPRMRGDDGPAAHRVQ--NLHILWGRLRDFYQEELQQLI---LSPPPDLQVMGRDPF 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 157818007 116 ------ELGRLLQLILGCAVNCEKKQEHIKNIMTLEESVQHVVMTAIQEL 159
Cdd:cd22230 119 teeavqELEKLLRLLLGAAVQCERRELFIRHIQGLDLDVQAELAEAIQEV 168
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
263-662 |
1.55e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.61 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 263 RLEAAKDDYRVHCEELEKQLIEfQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEVYRQKLQDLNDLRKQVKS 342
Cdd:PTZ00121 1225 KAEAVKKAEEAKKDAEEAKKAE-EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKK 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 343 LQETNMMyMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDT 422
Cdd:PTZ00121 1304 ADEAKKK-AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA 1382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 423 LKETNEELRCS----------KAQQDHLNQADSSATKSYE--NLAAEIMPVEyrEVFIRLQHENKMLRLQQEGTENERIE 490
Cdd:PTZ00121 1383 AKKKAEEKKKAdeakkkaeedKKKADELKKAAAAKKKADEakKKAEEKKKAD--EAKKKAEEAKKADEAKKKAEEAKKAE 1460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 491 QLQEQLEQKhRKMNELETEQRlSKERIGELQQQIEDLQKSLQE-QGSKSEGESSSKLKQKLEAHMEKLTEVHEELQKKQE 569
Cdd:PTZ00121 1461 EAKKKAEEA-KKADEAKKKAE-EAKKADEAKKKAEEAKKKADEaKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADE 1538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 570 LIEDLQPDISQNAQKISELEAALQ-KKDEDMKAMEERYKMYLEKARNVIKTLDPKLNPASAEIMLLRKQLAEKDRRIEil 648
Cdd:PTZ00121 1539 AKKAEEKKKADELKKAEELKKAEEkKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE-- 1616
|
410
....*....|....
gi 157818007 649 ESECKVAKFRDYEE 662
Cdd:PTZ00121 1617 EAKIKAEELKKAEE 1630
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
178-525 |
2.46e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 178 QQLKRALEELQEALA--EKEELKQRCQELDMQVTALQDEKNSLVSENEMMNEKLDQLDGSFddpntmvakkyfhvqlqle 255
Cdd:TIGR02168 216 KELKAELRELELALLvlRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEV------------------- 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 256 qlqeenyrleaakddyrvhcEELEKQLIEFQHRNDELTSLAEEtraLKDEIDVLRATSDKANKLESTVEVYRQKL-QDLN 334
Cdd:TIGR02168 277 --------------------SELEEEIEELQKELYALANEISR---LEQQKQILRERLANLERQLEELEAQLEELeSKLD 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 335 DLRKQVKSLQETNMMYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSE----SKRADTLAFEMKRLEEKHETLL 410
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKvaqlELQIASLNNEIERLEARLERLE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 411 KEKERLIEQRDTLKETNEELRCSKAQQ--DHLNQADSSATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGTENER 488
Cdd:TIGR02168 414 DRRERLQQEIEELLKKLEEAELKELQAelEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
|
330 340 350
....*....|....*....|....*....|....*..
gi 157818007 489 IEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIE 525
Cdd:TIGR02168 494 LERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIS 530
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
480-665 |
3.23e-08 |
|
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: 56.31 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 480 QQEGTENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQGSKSEGESSSKLK------------ 547
Cdd:COG4942 48 KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRlgrqpplallls 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 548 -----------QKLEAHMEKLTEVHEELQKKQELIEDLQPDISQNAQKISELEAALQKKDEDMKAMEERYKMYLEKARNV 616
Cdd:COG4942 128 pedfldavrrlQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 157818007 617 IKTLDPKLNPASAEIMLLRKQLAEKDRRIEILESECKVAKFRDYEEKLI 665
Cdd:COG4942 208 LAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
169-640 |
6.96e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 6.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 169 ASDAVGELEQQLKRALEELQEALAEKEELKQRCQELDMQVTALQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAKKYF 248
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 249 HVQLQLEQLQEENYRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANK-LESTVEVYR 327
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEaLEEAAEEEA 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 328 QKLQDLNDLRKQVKSLQETNMMYMHNTVSLEEELKKANAARAQLETYKRQVQD-----LHTKLSSESKRADTLAFEMKRL 402
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGflegvKAALLLAGLRGLAGAVAVLIGV 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 403 EEKHETLLKEKERLIEQRDTLKETNEELRCSKAQQDH---------LNQADSSATKSYENLAAEIMPVEYREVFIRLQHE 473
Cdd:COG1196 533 EAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAkagratflpLDKIRARAALAAALARGAIGAAVDLVASDLREAD 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 474 NKMLRLQQEGTENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAH 553
Cdd:COG1196 613 ARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE 692
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 554 MEKLTEVHEELQKKQELIEDLQPDISQNAQKISELEAALQKKDEDMKAMEERYKMYLEKARnVIKTLDPKLNPASAEIML 633
Cdd:COG1196 693 LELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEAL-EELPEPPDLEELERELER 771
|
....*..
gi 157818007 634 LRKQLAE 640
Cdd:COG1196 772 LEREIEA 778
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
169-662 |
6.98e-08 |
|
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: 55.88 E-value: 6.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 169 ASDAVGELEQQLKRALEELQEALAEKEELKQRCQELDMQVTALQDEKNSLVSENEMMNEKLDQL----DGSFDDPNTMVA 244
Cdd:pfam05483 266 SRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLteekEAQMEELNKAKA 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 245 KKYFHVQLQLEQLQEENYRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVE 324
Cdd:pfam05483 346 AHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKK 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 325 VYRQKLQDLNDLRKQVKSLQETNMMYMHNtvsLEEELkkaNAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLee 404
Cdd:pfam05483 426 QFEKIAEELKGKEQELIFLLQAREKEIHD---LEIQL---TAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKL-- 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 405 khetllkekerLIEQRDTLKETNEELRCSKAQQDHLNqadsSATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGT 484
Cdd:pfam05483 498 -----------LLENKELTQEASDMTLELKKHQEDII----NCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGD 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 485 ENE-RIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEqgsksegessskLKQKLEAHMEKLTEVHEE 563
Cdd:pfam05483 563 EVKcKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEE------------LHQENKALKKKGSAENKQ 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 564 LQKKQELIEDLQPDISQNAQKISELEAALQKKDEDMKAMEERYKMYLEKARNVI-------KTLDPKLNPASAEIM-LLR 635
Cdd:pfam05483 631 LNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIAdeavklqKEIDKRCQHKIAEMVaLME 710
|
490 500
....*....|....*....|....*..
gi 157818007 636 KQLAEKDRRIEILESECKVAKFRDYEE 662
Cdd:pfam05483 711 KHKHQYDKIIEERDSELGLYKNKEQEQ 737
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
262-664 |
1.53e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 262 YRLEAAKDDYRVHCEELEKQLIEFQHRNDELT------SLAEETRALKDEIDVLratSDKANKLESTVEVYRQKLQDLND 335
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEkllqllPLYQELEALEAELAEL---PERLEELEERLEELRELEEELEE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 336 LRKQVKSLQEtnmmymhntvSLEEELKK-ANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKE 414
Cdd:COG4717 168 LEAELAELQE----------ELEELLEQlSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 415 RLiEQRDTLKETNEELRCSKAQQDHLNQADSSATKSYE--NLAAEIMPVEYREVFIRLQHENKMLRLQQEGTENERIEQL 492
Cdd:COG4717 238 AA-ALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiaGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 493 QEQLEQKHRKmnELETEQRLSKERIGELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKL-TEVHEELQKKQELI 571
Cdd:COG4717 317 EEEELEELLA--ALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAgVEDEEELRAALEQA 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 572 EDLQpdisQNAQKISELEAALQKKDEDMKAMEERYKmyLEKARNVIKTLDPKLNPASAEIMLLRKQLAEKDRRIEILESE 651
Cdd:COG4717 395 EEYQ----ELKEELEELEEQLEELLGELEELLEALD--EEELEEELEELEEELEELEEELEELREELAELEAELEQLEED 468
|
410
....*....|...
gi 157818007 652 CKVAKFRDYEEKL 664
Cdd:COG4717 469 GELAELLQELEEL 481
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
181-614 |
2.10e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 181 KRALEEL----QEALAEKEELKQRCQELDMQVTALQDEKNSLVSENEMMNEKLDQldgsfDDPNTMVAKKYFHVQLQLEQ 256
Cdd:PTZ00121 1314 AKKADEAkkkaEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEA-----AEKKKEEAKKKADAAKKKAE 1388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 257 LQEENYRLEAAKDDYRVHCEELEKQLIEfQHRNDELTSLAEETRAlKDEIDVLRATSDKANKLESTVEVYRqKLQDLNDL 336
Cdd:PTZ00121 1389 EKKKADEAKKKAEEDKKKADELKKAAAA-KKKADEAKKKAEEKKK-ADEAKKKAEEAKKADEAKKKAEEAK-KAEEAKKK 1465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 337 RKQVKSLQETNmmymhntvSLEEELKKANAARAQLETYKRQVQDLHtKLSSESKRADTL--------AFEMKRLEEKHET 408
Cdd:PTZ00121 1466 AEEAKKADEAK--------KKAEEAKKADEAKKKAEEAKKKADEAK-KAAEAKKKADEAkkaeeakkADEAKKAEEAKKA 1536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 409 LLKEKERLIEQRDTLKETnEELRCS----KAQQDHLNQADSSATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGT 484
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKA-EELKKAeekkKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 485 ENERI--EQLQEQLEQKHRkmneleTEQRLSKERigELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAhmEKLTEVHE 562
Cdd:PTZ00121 1616 EEAKIkaEELKKAEEEKKK------VEQLKKKEA--EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA--EEAKKAEE 1685
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 157818007 563 ELQKKQELIEDlQPDISQNAQKISELEAALQKKDEDMKAMEERYKMYLEKAR 614
Cdd:PTZ00121 1686 DEKKAAEALKK-EAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAK 1736
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
175-609 |
5.04e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 5.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 175 ELEQQLKRALEELQEALAEKEELKQRCQELDMqVTALQDEKNSLvsENEMMNEKLDQLDGSFDDpntmVAKKYFHVQLQL 254
Cdd:PRK03918 335 EKEERLEELKKKLKELEKRLEELEERHELYEE-AKAKKEELERL--KKRLTGLTPEKLEKELEE----LEKAKEEIEEEI 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 255 EQLQEENYRLEAAKDDYRVHCEELEK---------QLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEV 325
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKKakgkcpvcgRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEK 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 326 YRQKLQDLNDLRKQVKSLQEtnmmymhntvsLEEELKKANAAraQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEk 405
Cdd:PRK03918 488 VLKKESELIKLKELAEQLKE-----------LEEKLKKYNLE--ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE- 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 406 hetLLKEKERLIEQRDTLKETNEELrcskaqqdhLNQADSSATKSYENLAAEIMPVE--YREvFIRLQHENKMLRlqqeg 483
Cdd:PRK03918 554 ---LKKKLAELEKKLDELEEELAEL---------LKELEELGFESVEELEERLKELEpfYNE-YLELKDAEKELE----- 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 484 TENERIEQLQEQLEQKHRKMNELETeqrlskeRIGELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEE 563
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETEK-------RLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKR 688
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 157818007 564 LQKKQELIEDLQPDISQNAQKISELEaALQKKDEDMKAMEERYKMY 609
Cdd:PRK03918 689 REEIKKTLEKLKEELEEREKAKKELE-KLEKALERVEELREKVKKY 733
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
265-663 |
5.86e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 5.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 265 EAAKDDYRVHCEELEKQlIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEVYRqKLQDLNDLRKQVKSLQ 344
Cdd:PTZ00121 1370 EKKKEEAKKKADAAKKK-AEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK-KADEAKKKAEEAKKAD 1447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 345 ETNmmymhntvSLEEELKKANAARAQLETyKRQVQDLHTKlSSESKRADTLAFEMKRLEEKHETLlKEKERLIEQRDTLK 424
Cdd:PTZ00121 1448 EAK--------KKAEEAKKAEEAKKKAEE-AKKADEAKKK-AEEAKKADEAKKKAEEAKKKADEA-KKAAEAKKKADEAK 1516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 425 ETNEELRCSKAQQDHLNQADSSATKSYENLAAEimpveyrevfirlqhENKMLRLQQEGTENERIEQLQEQLEQKHRKMN 504
Cdd:PTZ00121 1517 KAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD---------------ELKKAEELKKAEEKKKAEEAKKAEEDKNMALR 1581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 505 ELETEQRLSKERIGELQQ--------QIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTE---VHEELQKKQELIED 573
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKlyeeekkmKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEekkKAEELKKAEEENKI 1661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 574 LQPDISQNAQKISELEAALQKKDEDMKAMEERYKMYLEKARNVIKtldpklnpasaeimlLRKQLAEKDRRIEILESECK 653
Cdd:PTZ00121 1662 KAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE---------------LKKKEAEEKKKAEELKKAEE 1726
|
410
....*....|
gi 157818007 654 VAKFRDYEEK 663
Cdd:PTZ00121 1727 ENKIKAEEAK 1736
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
132-621 |
2.28e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 132 EKKQEHIKNIMTLEESVQHVVMTAIQELMSKEIvsspASDAVGELEQQLKRALEELQEALAEKEELKQRCQELDMQVTAL 211
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEE----LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 212 QDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAKKYFHVQLQLEQLQEENYRLEAAKDDYRVHCEELEKQLIEFQHRNDE 291
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 292 LTSLAEETRALKDEIDVLRATS-DKANKLESTVEVYRQKLQDLNDLRKQVKSLQETNMMYMHNTVSLEEELKKAN----- 365
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLaELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGlrgla 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 366 ---------------------AARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLK 424
Cdd:COG1196 524 gavavligveaayeaaleaalAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDL 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 425 ETNEELRCSKAQQDHLNQA--DSSATKSYENLAAEIMPVEYREVFIRL----QHENKMLRLQQEGTENERIEQLQEQLEQ 498
Cdd:COG1196 604 VASDLREADARYYVLGDTLlgRTLVAARLEAALRRAVTLAGRLREVTLegegGSAGGSLTGGSRRELLAALLEAEAELEE 683
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 499 KHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEvHEELQKKQELIEDLQPDI 578
Cdd:COG1196 684 LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE-EELLEEEALEELPEPPDL 762
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 579 SQNAQKISELEAALQKK-------DEDMKAMEERYKMY------LEKARN----VIKTLD 621
Cdd:COG1196 763 EELERELERLEREIEALgpvnllaIEEYEELEERYDFLseqredLEEAREtleeAIEEID 822
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
403-595 |
2.91e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 403 EEKHETLLKEKERLIEQRDTLKETNEELRcskAQQDHLNQADSSatksYENLAaeimpvEYREVFIRL-QHENKMLRLQQ 481
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALE---AELDALQERREA----LQRLA------EYSWDEIDVaSAEREIAELEA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 482 EGTE----NERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQ---KSLQEQGSKSEGESSSKLKQKLEAHm 554
Cdd:COG4913 676 ELERldasSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEeelDELQDRLEAAEDLARLELRALLEER- 754
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 157818007 555 eklteVHEELQKK--QELIEDLQPDISQNAQKISELEAALQKK 595
Cdd:COG4913 755 -----FAAALGDAveRELRENLEERIDALRARLNRAEEELERA 792
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
292-669 |
4.74e-06 |
|
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: 50.11 E-value: 4.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 292 LTSLAEETRALKDEIDVLRATSDKANKLESTVEVYRQKLQDLNDLRKQVKSLQETNMMYMHNTVS----LEEELKKANAA 367
Cdd:pfam05483 246 LIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMStqkaLEEDLQIATKT 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 368 RAQL-ETYKRQVQDLHTKLSSESKRADTLAFEMKRLEekhETLLKEKERLIEQRDTLKETNEELRCSKAQQDHLNQADSS 446
Cdd:pfam05483 326 ICQLtEEKEAQMEELNKAKAAHSFVVTEFEATTCSLE---ELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNN 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 447 ATKSYENLAAEIMPveyREVFIRLQHENKMLRLQQEGTENERIEQLQeqleQKHRKMNELETEQRLSKERIGELQQQIED 526
Cdd:pfam05483 403 KEVELEELKKILAE---DEKLLDEKKQFEKIAEELKGKEQELIFLLQ----AREKEIHDLEIQLTAIKTSEEHYLKEVED 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 527 LQKSLQEQGSKSEGESSSKLKQKLEAH--MEKLTEVHEELQKKQELI-------EDLQPDISQNAQKISELEAALQKKDE 597
Cdd:pfam05483 476 LKTELEKEKLKNIELTAHCDKLLLENKelTQEASDMTLELKKHQEDIinckkqeERMLKQIENLEEKEMNLRDELESVRE 555
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157818007 598 DMKAMEERYKMYLEKARNVIKTLDPKLNPASAEIML-------LRKQLAEKDRRIEILESECKVAKFRDYEEKLIVSAW 669
Cdd:pfam05483 556 EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKIlenkcnnLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAY 634
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
476-576 |
8.31e-06 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 49.31 E-value: 8.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 476 MLRLQQEGTENErIEQLQEQLEQKHRKMNELETEQRL-SKERIGELQQQIEDLQKSLQE-----QGSKSEGESSSKLKQK 549
Cdd:COG0542 401 RVRMEIDSKPEE-LDELERRLEQLEIEKEALKKEQDEaSFERLAELRDELAELEEELEAlkarwEAEKELIEEIQELKEE 479
|
90 100
....*....|....*....|....*..
gi 157818007 550 LEAHMEKLTEVHEELQKKQELIEDLQP 576
Cdd:COG0542 480 LEQRYGKIPELEKELAELEEELAELAP 506
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
327-584 |
8.52e-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: 48.61 E-value: 8.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 327 RQKLQDLNDLRKQVKSLQETnmmymhntvsLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKH 406
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKE----------LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 407 ETLlkeKERLIEQRDTLKEtneelRCSKAQQDHLNQADSSATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEgten 486
Cdd:COG4942 93 AEL---RAELEAQKEELAE-----LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA---- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 487 eRIEQLQEQLEQKHRKMNELETEQrlsKERIGELQQQIEDLQKSLQEqgsksegessskLKQKLEAHMEKLTEVHEELQK 566
Cdd:COG4942 161 -ELAALRAELEAERAELEALLAEL---EEERAALEALKAERQKLLAR------------LEKELAELAAELAELQQEAEE 224
|
250
....*....|....*...
gi 157818007 567 KQELIEDLQPDISQNAQK 584
Cdd:COG4942 225 LEALIARLEAEAAAAAER 242
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
357-604 |
9.35e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 9.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 357 LEEELKKANAARAQLETYKRQVQ----------------DLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQR 420
Cdd:PRK02224 164 LEEYRERASDARLGVERVLSDQRgsldqlkaqieekeekDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 421 DTLKETNEELRCSKAQQDHLNQADSSATKSYENLAAEIMpvEYREVFIRLQHENKMLR--LQQEGTENERIEQLQEQLEQ 498
Cdd:PRK02224 244 EEHEERREELETLEAEIEDLRETIAETEREREELAEEVR--DLRERLEELEEERDDLLaeAGLDDADAEAVEARREELED 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 499 KHRKMNELETEQRLS------------------KERIGELQQQIEDLQKSLQ--EQGSKSEGESSSKLKQKLEAHMEKLT 558
Cdd:PRK02224 322 RDEELRDRLEECRVAaqahneeaeslredaddlEERAEELREEAAELESELEeaREAVEDRREEIEELEEEIEELRERFG 401
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 157818007 559 EVHEELQKKQELIEDLQPDISQNAQKISELEAALQKKDEDMKAMEE 604
Cdd:PRK02224 402 DAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA 447
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
273-533 |
1.19e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 48.77 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 273 VHCEELEKQLIEFQHRndELTSLAEEtraLKDEIDVLRATSDKANKLESTVEVYrqKLQDLNDLRKQVKSlqetnmmymh 352
Cdd:PRK05771 31 VHIEDLKEELSNERLR--KLRSLLTK---LSEALDKLRSYLPKLNPLREEKKKV--SVKSLEELIKDVEE---------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 353 NTVSLEEELKKANAARAQLETYKRqvqdlhtKLSSESKRADTL-AFEmkrLEEKhetLLKEKERLIEQRDTLKETNEELr 431
Cdd:PRK05771 94 ELEKIEKEIKELEEEISELENEIK-------ELEQEIERLEPWgNFD---LDLS---LLLGFKYVSVFVGTVPEDKLEE- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 432 cSKAQQDHLNQADSSATKSYENLAAeIMPVEYREVFIRL--QHENKMLRLQQEGTENERIEQLQEQLEQKHRKMNELete 509
Cdd:PRK05771 160 -LKLESDVENVEYISTDKGYVYVVV-VVLKELSDEVEEElkKLGFERLELEEEGTPSELIREIKEELEEIEKERESL--- 234
|
250 260
....*....|....*....|....
gi 157818007 510 qrlsKERIGELQQQIEDLQKSLQE 533
Cdd:PRK05771 235 ----LEELKELAKKYLEELLALYE 254
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
182-618 |
1.50e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 182 RALEELQEALAEKEELKQRCQELDMQVTALQDEKNSLVSENEMMNEKLDQLDgsfddpntmvakkyfhvqlqleqLQEEN 261
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE-----------------------KLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 262 YRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTvevyrQKLQDLNDLRKQVK 341
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSL-----ATEEELQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 342 SLQETNMMYMHNTVSLEEELKKANAARAQLET------YKRQVQDLHTKLSSESKRAdTLAFEMKRLEEKHETLLK---- 411
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENeleaaaLEERLKEARLLLLIAAALL-ALLGLGGSLLSLILTIAGvlfl 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 412 -------EKERLIEQRDTLKETNEELRCSKAQQDhLNQADSSATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGT 484
Cdd:COG4717 282 vlgllalLFLLLAREKASLGKEAEELQALPALEE-LEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 485 ENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQGSKSEGESSSKLKQkleahmEKLTEVHEEL 564
Cdd:COG4717 361 EELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEA------LDEEELEEEL 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 157818007 565 QKKQELIEDLQPDISQNAQKISELEAALQK--KDEDMKAMEERYKMYLEKARNVIK 618
Cdd:COG4717 435 EELEEELEELEEELEELREELAELEAELEQleEDGELAELLQELEELKAELRELAE 490
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
368-620 |
1.60e-05 |
|
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: 48.20 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 368 RAQLETYKRQVqdlhtklssESKRADTLAFEMKRLEEKhETLLKEKERlieQRDTLKETNEELRCSKAQQDHLNQADSSA 447
Cdd:pfam17380 352 RIRQEERKREL---------ERIRQEEIAMEISRMREL-ERLQMERQQ---KNERVRQELEAARKVKILEEERQRKIQQQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 448 TKSYENLAAEIMPVEYREV-FIRLQHENKMLRLQQEGTENE-RIEQLQEQLEQKHRKMNELETEQRlSKERIGELQQQIe 525
Cdd:pfam17380 419 KVEMEQIRAEQEEARQREVrRLEEERAREMERVRLEEQERQqQVERLRQQEEERKRKKLELEKEKR-DRKRAEEQRRKI- 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 526 dLQKSLQEQgsksegesssklKQKLEAHMEKLTEVHEELQKKQELI--EDLQPDISQNAQKISELEAALQKKDEDMKAME 603
Cdd:pfam17380 497 -LEKELEER------------KQAMIEEERKRKLLEKEMEERQKAIyeEERRREAEEERRKQQEMEERRRIQEQMRKATE 563
|
250
....*....|....*...
gi 157818007 604 ERYKM-YLEKARNVIKTL 620
Cdd:pfam17380 564 ERSRLeAMEREREMMRQI 581
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
382-663 |
1.77e-05 |
|
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: 48.20 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 382 HTKLSSESKRADTLA-FEMKRLEEKHETLLKEKERlieqRDTLKETneelrcSKAQQDHLNQaDSSATKSYENLAAEimp 460
Cdd:pfam17380 280 HQKAVSERQQQEKFEkMEQERLRQEKEEKAREVER----RRKLEEA------EKARQAEMDR-QAAIYAEQERMAME--- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 461 veyrevfirlqHENKMLRLQQE--GTENERIEQLQEQLE-QKHRKMNELETEQRLSKERIG---ELQQQIEDLQKSLQEQ 534
Cdd:pfam17380 346 -----------RERELERIRQEerKRELERIRQEEIAMEiSRMRELERLQMERQQKNERVRqelEAARKVKILEEERQRK 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 535 GSKSEGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDISQNAQKISELEAALQKKDEDMKAMEERYKMYLEKAR 614
Cdd:pfam17380 415 IQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRR 494
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 157818007 615 NVIKTldpklnpasaEIMLLRKQLAEKDRRIEILESECKVAKFRDYEEK 663
Cdd:pfam17380 495 KILEK----------ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEE 533
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
478-651 |
2.06e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 478 RLQQEGTENERIEQLQEQLEQKHRKMNELEteqrlskERIGELQQQIEDLQKSLQEQGSKSEgesssklKQKLEAHMEKL 557
Cdd:COG4717 79 ELKEAEEKEEEYAELQEELEELEEELEELE-------AELEELREELEKLEKLLQLLPLYQE-------LEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 558 TEVHEELQKKQELIEDLQPDISQNAQKISELEAALQKKDEDMKAMEERykmYLEKARNVIKTLDPKLNPASAEIMLLRKQ 637
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE---ELQDLAEELEELQQRLAELEEELEEAQEE 221
|
170
....*....|....
gi 157818007 638 LAEKDRRIEILESE 651
Cdd:COG4717 222 LEELEEELEQLENE 235
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
311-557 |
2.56e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 311 ATSDKANKLESTVEVYRQKLQDLNDLRKQVKSLQEtnmmymhntvSLEEELKKANAARAQLEtykRQVQDLHTKLSSESK 390
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEK----------ALLKQLAALERRIAALA---RRIRALEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 391 RADTLAFEMKRLEEKHETLLKEKERLI------EQRDTLK-----ETNEELRCSKAQQDHLNQADSSATKSYENLAAEIm 459
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKEELAELLralyrlGRQPPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 460 pveyREVFIRLQHENKMLRLQQEGTENERiEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQGSKSE 539
Cdd:COG4942 163 ----AALRAELEAERAELEALLAELEEER-AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
250
....*....|....*...
gi 157818007 540 GESSSKLKQKLEAHMEKL 557
Cdd:COG4942 238 AAAERTPAAGFAALKGKL 255
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
180-640 |
3.28e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.32 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 180 LKRALEELQEALAEKEELKQRCQELDMQVTALQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAKKYFHVQLQLEQLqe 259
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKI-- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 260 enyrleaakddyrvhcEELEKQLIEFQHRNDELTSLAEE--TRALKDEIDvlratsDKANKLESTVEVYRQKLQDLNDLR 337
Cdd:TIGR04523 284 ----------------KELEKQLNQLKSEISDLNNQKEQdwNKELKSELK------NQEKKLEEIQNQISQNNKIISQLN 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 338 KQVKSLQETNMMYMHNTVSLEEELKKANAA-----------RAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKH 406
Cdd:TIGR04523 342 EQISQLKKELTNSESENSEKQRELEEKQNEieklkkenqsyKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEK 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 407 ETLLKEKERLIEQRDTLKETNEELRCSKAQQDhLNQADSSATKSYENLAAEIMPVEYREVFIRLQHENKMLRL--QQEGT 484
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNNSEIKDLTNQDSVKE-LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSkeKELKK 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 485 ENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEEL 564
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSL 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 565 QKKQ----ELIEDLQPDISQNAQKISELEAALQKKDEDMKAMEERYkmylEKARNVIKTLDPKLNPASAEIMLLRKQLAE 640
Cdd:TIGR04523 581 KKKQeekqELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKEN----EKLSSIIKNIKSKKNKLKQEVKQIKETIKE 656
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
486-651 |
3.97e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 486 NERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEqgsksegessskLKQKLEAHMEKLTEVHEELQ 565
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA------------LARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 566 KKQELIEDLQPDISQNAQKISELEAALQK-----------KDEDMKAMEERYkMYLEKARNVIKTLDPKLNPASAEIMLL 634
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLRALYRlgrqpplalllSPEDFLDAVRRL-QYLKYLAPARREQAEELRADLAELAAL 165
|
170
....*....|....*..
gi 157818007 635 RKQLAEKDRRIEILESE 651
Cdd:COG4942 166 RAELEAERAELEALLAE 182
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
480-651 |
4.32e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 4.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 480 QQEGTENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQGSKSEGESSSKLKQK---------- 549
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGgsvsyldvll 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 550 ----LEAHMEKLTEVHEELQKKQELIEDLQPDISQNAQKISELEAALQKKDEDMKAMEERYKMY---LEKARNVIKTLDP 622
Cdd:COG3883 110 gsesFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELeaqQAEQEALLAQLSA 189
|
170 180
....*....|....*....|....*....
gi 157818007 623 KLNPASAEIMLLRKQLAEKDRRIEILESE 651
Cdd:COG3883 190 EEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
420-665 |
4.90e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.55 E-value: 4.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 420 RDTLKETNEELRCSKAQQDHLNQadssATKSYENLAAEimpveyrevfirlqhenkmlrlqQEGTENERIEQLQEQLEQK 499
Cdd:PHA02562 173 KDKIRELNQQIQTLDMKIDHIQQ----QIKTYNKNIEE-----------------------QRKKNGENIARKQNKYDEL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 500 HRKMNELETEQRLSKERIGELQQQIEDLQKSLQEqgsksegesSSKLKQKLEAHMEKLTEVHEELQKKQEL------IED 573
Cdd:PHA02562 226 VEEAKTIKAEIEELTDELLNLVMDIEDPSAALNK---------LNTAAAKIKSKIEQFQKVIKMYEKGGVCptctqqISE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 574 LQPDISQNAQKISELEAALQKKDEDMKAMEERYKMYLEkARNVIKTLDPKLNPASAEIMLLRKQLAEKDRRIEILESECK 653
Cdd:PHA02562 297 GPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNE-QSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFV 375
|
250
....*....|....*..
gi 157818007 654 -----VAKFRDYEEKLI 665
Cdd:PHA02562 376 dnaeeLAKLQDELDKIV 392
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
399-591 |
6.45e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 6.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 399 MKRLEEKHETLLKEKERL-IEQRDTLKETNEELRCSKAQQDHLNQAD---SSATKSYENLAAEIMPVEYREVFIRLQHEN 474
Cdd:COG4717 48 LERLEKEADELFKPQGRKpELNLKELKELEEELKEAEEKEEEYAELQeelEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 475 KMLRLQQEGTENER--IEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQgsksEGESSSKLKQKLEA 552
Cdd:COG4717 128 LPLYQELEALEAELaeLPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA----TEEELQDLAEELEE 203
|
170 180 190
....*....|....*....|....*....|....*....
gi 157818007 553 HMEKLTEVHEELQKKQELIEDLQPDISQNAQKISELEAA 591
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
354-615 |
7.85e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.29 E-value: 7.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 354 TVSLEEELKKANAARAQLETYKR-------QVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKET 426
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEkrdelneELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 427 NEELRCSKAQQDHLNQADSSATKSYENLAAEIMPVEYRevfirlqHENKMLRLQQEGTENERIEQLQEQLE------QKH 500
Cdd:COG1340 87 LNELREELDELRKELAELNKAGGSIDKLRKEIERLEWR-------QQTEVLSPEEEKELVEKIKELEKELEkakkalEKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 501 RKMNELETEQRLSKERIGELQQQIEDLQKSLQEqgsksEGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDISQ 580
Cdd:COG1340 160 EKLKELRAELKELRKEAEEIHKKIKELAEEAQE-----LHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIE 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 157818007 581 NAQKISELEAALQ---------KKDEDMKAMEERYKMYLEKARN 615
Cdd:COG1340 235 LQKELRELRKELKklrkkqralKREKEKEELEEKAEEIFEKLKK 278
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
291-607 |
1.01e-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: 46.10 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 291 ELTSLAEETRALKDEIDVLRATSdkaNKLESTVEVYRQKLQDLNDLRKQVKSLQETNMMymHNTVSLEEELKKANAARAQ 370
Cdd:COG3096 837 ELAALRQRRSELERELAQHRAQE---QQLRQQLDQLKEQLQLLNKLLPQANLLADETLA--DRLEELREELDAAQEAQAF 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 371 LETYKRQVQDLHTKLSSeskradtlafeMKRLEEKHETLLKEKERLIEQRDTLKETNEELRCSKAQQDHLNQADSSAtks 450
Cdd:COG3096 912 IQQHGKALAQLEPLVAV-----------LQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSYEDAVG--- 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 451 yenlaaeiMPVEYREVFIRLQHenKMLRLQQEGTE-NERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQK 529
Cdd:COG3096 978 --------LLGENSDLNEKLRA--RLEQAEEARREaREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGV 1047
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157818007 530 SLQEQGSKSegesssklkqkleAHMEKlTEVHEELqkkqeliedlqpdiSQNAQKISELEAALQKKDEDMKAMEERYK 607
Cdd:COG3096 1048 QADAEAEER-------------ARIRR-DELHEEL--------------SQNRSRRSQLEKQLTRCEAEMDSLQKRLR 1097
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
176-646 |
1.86e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 176 LEQQLKRALEELQEALAEKEELKQRCQELDMQVTALQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAKKYFHVQLQLE 255
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSM 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 256 QLQEENYRLEAAKDDYRVHCEELEK---QLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEVYRQKLQD 332
Cdd:PRK01156 268 ELEKNNYYKELEERHMKIINDPVYKnrnYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSR 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 333 LNDLRKQVKSLQETNMMYMHNTVSLEEELKKanaaraqLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKE 412
Cdd:PRK01156 348 YDDLNNQILELEGYEMDYNSYLKSIESLKKK-------IEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQD 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 413 KE----RLIEQRDTLKETNEELRCSKAQQDHLNQADSSATKSYENLAAEIMPvEYREVFIRLQHENKMLRLQQEGTENER 488
Cdd:PRK01156 421 ISskvsSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIIN-HYNEKKSRLEEKIREIEIEVKDIDEKI 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 489 IEQLQEQLEQKHRKMNELETEQRLSKERIGELqQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEELQKKQ 568
Cdd:PRK01156 500 VDLKKRKEYLESEEINKSINEYNKIESARADL-EDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVIS 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 569 EL-IEDLQPDISQNAQKISELEAALQKKDEDMKAMEERYKMYLEKARNVIKTLDPKLNPASA----------EIMLLRKQ 637
Cdd:PRK01156 579 LIdIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQEnkilieklrgKIDNYKKQ 658
|
....*....
gi 157818007 638 LAEKDRRIE 646
Cdd:PRK01156 659 IAEIDSIIP 667
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
298-533 |
1.97e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 298 ETRALKDEIDVLRATSDKANKLESTVEVYRQKLQDLNDLRKQVKSLQEtnmmymhntvsLEEELKKANAARAQLETYKRQ 377
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALEDAREQIELLEPIRELAERYAA-----------ARERLAELEYLRAALRLWFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 378 vqdlhtklssesKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKETNEELRcskaqqdhlNQADSSATKSYENLAAE 457
Cdd:COG4913 288 ------------RRLELLEAELEELRAELARLEAELERLEARLDALREELDELE---------AQIRGNGGDRLEQLERE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 458 I--MPVEYREV---FIRLQHENKMLRLQQEGTE---NERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQK 529
Cdd:COG4913 347 IerLERELEERerrRARLEALLAALGLPLPASAeefAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
....
gi 157818007 530 SLQE 533
Cdd:COG4913 427 EIAS 430
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
263-534 |
2.28e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 263 RLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETraLKDEIDVLRATSDKANKLESTVevyRQKLQDLNDLRKQVKS 342
Cdd:PRK04863 855 DHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADET--LADRVEEIREQLDEAEEAKRFV---QQHGNALAQLEPIVSV 929
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 343 LQETNMMYmhntvsleEELKKA-NAARAQLETYKRQVQDLhtklSSESKRADTLAFE--MKRLEEKHETLLKEKERLIEQ 419
Cdd:PRK04863 930 LQSDPEQF--------EQLKQDyQQAQQTQRDAKQQAFAL----TEVVQRRAHFSYEdaAEMLAKNSDLNEKLRQRLEQA 997
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 420 RDTLKETNEELRCSKAQQDHLNQADSSATKSYENlaaeimpveYREVFIRLQHENKMLRLQ-QEGTEN---ERIEQLQEQ 495
Cdd:PRK04863 998 EQERTRAREQLRQAQAQLAQYNQVLASLKSSYDA---------KRQMLQELKQELQDLGVPaDSGAEErarARRDELHAR 1068
|
250 260 270
....*....|....*....|....*....|....*....
gi 157818007 496 LEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQ 534
Cdd:PRK04863 1069 LSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEM 1107
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
175-609 |
2.30e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 175 ELEQQLKRALEELQEALAEKEELKQRCQELDMQVTALQDEKnslvsENEMMNEKLDQLDGSFDdpntmvakkyfhvqlql 254
Cdd:COG4717 92 ELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ-----ELEALEAELAELPERLE----------------- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 255 eqlqeenyRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIdvLRATSDKANKLESTVEVYRQKLQD-- 332
Cdd:COG4717 150 --------ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE--LQDLAEELEELQQRLAELEEELEEaq 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 333 --LNDLRKQVKSLQETNMMY-MHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETL 409
Cdd:COG4717 220 eeLEELEEELEQLENELEAAaLEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 410 LKEKERLIEQRDTLKETNEELRCSKAQQDHLNQADSsaTKSYENLAAEImpVEYREVFIRLQHENKMLRLQQEGTENERI 489
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPDLS--PEELLELLDRI--EELQELLREAEELEEELQLEELEQEIAAL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 490 EQLQ-----EQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEEL 564
Cdd:COG4717 376 LAEAgvedeEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREEL 455
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 157818007 565 QKKQELIEDLQPDisqnaQKISELEAALQKKDEDMKAMEERYKMY 609
Cdd:COG4717 456 AELEAELEQLEED-----GELAELLQELEELKAELRELAEEWAAL 495
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
357-552 |
2.51e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 357 LEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKE----KERLIEQRDTLKETNEELRC 432
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeaEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 433 SKAQQDHLNQADSSatksyENLAAEIMPVEYREVFIRlqHENKMLRLQQEgtENERIEQLQEQLEQKHRKMNELETEQRL 512
Cdd:COG3883 98 SGGSVSYLDVLLGS-----ESFSDFLDRLSALSKIAD--ADADLLEELKA--DKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 157818007 513 SKERIGELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEA 552
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
290-614 |
2.53e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 290 DELTSLAEETRALKDEI------DVLRATSDKANKLESTVEVYRQKLQDLNDLRK--QVKSLQETNMMymhnTVSLEEEl 361
Cdd:COG3206 71 SGLSSLSASDSPLETQIeilksrPVLERVVDKLNLDEDPLGEEASREAAIERLRKnlTVEPVKGSNVI----EISYTSP- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 362 kkaNAARAQ------LETYKRQVQDLhtKLSSESKRADTLAFEMKRLEEKhetlLKEKERLIEQrdtLKETNEELRcSKA 435
Cdd:COG3206 146 ---DPELAAavanalAEAYLEQNLEL--RREEARKALEFLEEQLPELRKE----LEEAEAALEE---FRQKNGLVD-LSE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 436 QQDHLNQADSSATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQqEGTENERIEQLQEQLEQKHRKMNELEteQRLSKE 515
Cdd:COG3206 213 EAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALP-ELLQSPVIQQLRAQLAELEAELAELS--ARYTPN 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 516 --RIGELQQQIEDLQKSLQEQGSKsegessskLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDISQNAQKISELEaalq 593
Cdd:COG3206 290 hpDVIALRAQIAALRAQLQQEAQR--------ILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLE---- 357
|
330 340
....*....|....*....|.
gi 157818007 594 kkdEDMKAMEERYKMYLEKAR 614
Cdd:COG3206 358 ---REVEVARELYESLLQRLE 375
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
295-505 |
3.52e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 295 LAEETRALKDEIDVLRATSDKANKLESTVEVYR---QKLQDLNDLRKQVKSLQETnmmymhnTVSLEEELKKANAARAQL 371
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERRealQRLAEYSWDEIDVASAERE-------IAELEAELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 372 ETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLketneELRCSKAQQDHLNQAdssatksy 451
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA-----EDLARLELRALLEER-------- 754
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 157818007 452 enLAAEIMPVEYREVFIRLQHENKmlrlqqegTENERIEQLQEQLEQKHRKMNE 505
Cdd:COG4913 755 --FAAALGDAVERELRENLEERID--------ALRARLNRAEEELERAMRAFNR 798
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
169-533 |
3.80e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 169 ASDAVGELEQQL---KRALEELQEAL----AEKEELKQRCQELDMQVTALQDEKNsLVSENEMMNEKLDQLDGSFDDPNT 241
Cdd:PRK04863 284 HLEEALELRRELytsRRQLAAEQYRLvemaRELAELNEAESDLEQDYQAASDHLN-LVQTALRQQEKIERYQADLEELEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 242 MVAKKYFHVQLQLEQLQEENYRLEAAKDDYrvhcEELEKQLIEFQHRNDELtslaeETRALK--------DEIDVLRATS 313
Cdd:PRK04863 363 RLEEQNEVVEEADEQQEENEARAEAAEEEV----DELKSQLADYQQALDVQ-----QTRAIQyqqavqalERAKQLCGLP 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 314 D-KANKLESTVEVYRQKLQDLNDLRKQvkslqetnmmymhntvsLEEELKKANAARAQLEtykrQVQDLHTKLSSESKRA 392
Cdd:PRK04863 434 DlTADNAEDWLEEFQAKEQEATEELLS-----------------LEQKLSVAQAAHSQFE----QAYQLVRKIAGEVSRS 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 393 DtlAFEMKR-LEEKHETLLKEKERLIEQRDTLKEtneelrcskAQQDHLNQADSsatksyenlaaeimpveyrevfIRLQ 471
Cdd:PRK04863 493 E--AWDVAReLLRRLREQRHLAEQLQQLRMRLSE---------LEQRLRQQQRA----------------------ERLL 539
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157818007 472 HENKMlRLQQEGTENERIEQLQEQLEQKhrkMNELETEQRLSKERIGELQQQIEDLQKSLQE 533
Cdd:PRK04863 540 AEFCK-RLGKNLDDEDELEQLQEELEAR---LESLSESVSEARERRMALRQQLEQLQARIQR 597
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
169-533 |
4.03e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 169 ASDAVGELEQQLKRALEELQEALAEKEELKQRCQELDMQVTALQdeknslvsenemmnekldqldgsfddpntmvakkyf 248
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ------------------------------------ 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 249 hvqlqleqlqeenyrleaakddyrvhceelekQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEVYRQ 328
Cdd:COG4913 652 --------------------------------RLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEA 699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 329 KLQDLNDLRKQvkslqetnmmymhntvsLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHET 408
Cdd:COG4913 700 ELEELEEELDE-----------------LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDA 762
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 409 LLKE-KERLIEQRDTLKETNEELRcskaqqDHLNQADSSATKSYENLAAEIMPV-----EYREVFIRLQ------HENKM 476
Cdd:COG4913 763 VERElRENLEERIDALRARLNRAE------EELERAMRAFNREWPAETADLDADleslpEYLALLDRLEedglpeYEERF 836
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 157818007 477 LRLQQEgTENERIEQLQEQLEQKHRkmneleteqrlskerigELQQQIEDLQKSLQE 533
Cdd:COG4913 837 KELLNE-NSIEFVADLLSKLRRAIR-----------------EIKERIDPLNDSLKR 875
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
475-664 |
4.31e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.66 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 475 KMLRLQQEGTENERIEQLQEQLEQKHR-------KMNELETEQRL---------SKERIGELQQQIEDLQKSLQEQgsks 538
Cdd:PRK00409 453 KALMYNREGVENASVEFDEETLRPTYRlligipgKSNAFEIAKRLglpeniieeAKKLIGEDKEKLNELIASLEEL---- 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 539 egesssklKQKLEahmEKLTEVHEELQKKQELIEDLQpdisqnaQKISELEaalQKKDEDMKAMEERYKMYLEKAR---- 614
Cdd:PRK00409 529 --------ERELE---QKAEEAEALLKEAEKLKEELE-------EKKEKLQ---EEEDKLLEEAEKEAQQAIKEAKkead 587
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 157818007 615 NVIKTLDPKLNPASAEIMllRKQLAEKDRRI----EILESECKVAKFRDYEEKL 664
Cdd:PRK00409 588 EIIKELRQLQKGGYASVK--AHELIEARKRLnkanEKKEKKKKKQKEKQEELKV 639
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
154-506 |
5.43e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 5.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 154 TAIQELMSKEIVSSPASDAVGELEQQLKRALEELQEALAE----KEELKQ---RCQELDMQVTALQDEKNSLVSENEMMN 226
Cdd:TIGR02169 692 SLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEeeklKERLEEleeDLSSLEQEIENVKSELKELEARIEELE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 227 EKLDQLDGSFDDPNTMVAKKYF-HVQLQLEQLQEENYRLEAAKDDYRVhceELEKQLIEFQHRNDELTSLAEETRALKDE 305
Cdd:TIGR02169 772 EDLHKLEEALNDLEARLSHSRIpEIQAELSKLEEEVSRIEARLREIEQ---KLNRLTLEKEYLEKEIQELQEQRIDLKEQ 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 306 IDVLRATSDKAN----KLESTVEVYRQKLQDLN----DLRKQVKSLQEtnmmymhntvSLEEELKKANAARAQLETYKRQ 377
Cdd:TIGR02169 849 IKSIEKEIENLNgkkeELEEELEELEAALRDLEsrlgDLKKERDELEA----------QLRELERKIEELEAQIEKKRKR 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 378 VQDLHTKLSSESKRADTLAFEMKRLEE------KHETLLKEKERLIEQRDTLKETNeelrcSKAQQDhlnqadssatksY 451
Cdd:TIGR02169 919 LSELKAKLEALEEELSEIEDPKGEDEEipeeelSLEDVQAELQRVEEEIRALEPVN-----MLAIQE------------Y 981
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 157818007 452 ENLAAEIMpvEYREVFIRLQHENKMLRLQQEGTENERIEQLQEQLEQKHRKMNEL 506
Cdd:TIGR02169 982 EEVLKRLD--ELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFEAINENFNEI 1034
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
302-582 |
7.46e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.04 E-value: 7.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 302 LKDEIDVLRATSDKANKLESTVEVYRQKLQDLNDLRKQVKSLQETNMMYMHNTVSLEEEL-KKANAARAQLETYKRQVQD 380
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLaKEEEELKSELLKLERRKVD 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 381 LHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKETNEELRcskAQQDHLNQADSSATKSYENLAaeimp 460
Cdd:pfam02463 312 DEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELE---KLQEKLEQLEEELLAKKKLES----- 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 461 vEYREVFIRLQHENKMLRLQQEGTENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQGSKSEG 540
Cdd:pfam02463 384 -ERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK 462
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 157818007 541 ESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDISQNA 582
Cdd:pfam02463 463 DELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESK 504
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
168-619 |
9.72e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.65 E-value: 9.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 168 PASDAVGELEQQLKRALEELQEALAEKEELKQRCQELDMQVTALQDEKNSLVSENEMMNEKLDQLD--GSFDDPNTMVAK 245
Cdd:TIGR00618 297 AHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEvaTSIREISCQQHT 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 246 KYFHVQLQLEQLQEENYRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAeetRALKDEIDVLRATSDKANKLESTVEV 325
Cdd:TIGR00618 377 LTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLA---HAKKQQELQQRYAELCAAAITCTAQC 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 326 YRQKLQDLNDLRKQVKSLQEtNMMYMHNTVSLEEELKKANAARAQ-LETYKRQVQDLHTKLSSESKRADTLAFEMKRLEE 404
Cdd:TIGR00618 454 EKLEKIHLQESAQSLKEREQ-QLQTKEQIHLQETRKKAVVLARLLeLQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQR 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 405 KHETLLKEKERLIEQRDTLKETNEELRCSKAQQDHLNQADSSATKSYENLAAEIMPVEYREVFIR-LQHENKMLRLQQEG 483
Cdd:TIGR00618 533 GEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQdLTEKLSEAEDMLAC 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 484 TENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQE------QGSKSEGESSSKLKQKLEAHMEKL 557
Cdd:TIGR00618 613 EQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREhalsirVLPKELLASRQLALQKMQSEKEQL 692
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157818007 558 TEVHEELQKKQELIEDLQPDISQNAQKISELEAALQKKDEDMKAMEERYKMYLEKARNVIKT 619
Cdd:TIGR00618 693 TYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQART 754
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
520-665 |
1.51e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.77 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 520 LQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDISQNAQKISELEAALQKKDEdm 599
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARS-- 455
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157818007 600 kamEERYKMyleKARNVIKTLDpklnpasAEIMLLRKQLAEKDRRIEILESecKVAKFRDYEEKLI 665
Cdd:COG2433 456 ---EERREI---RKDREISRLD-------REIERLERELEEERERIEELKR--KLERLKELWKLEH 506
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
428-534 |
1.59e-03 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 41.90 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 428 EELRcsKAQQDHLNQAdssATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGTENERIEQLQEQLEQKHRKMNELE 507
Cdd:pfam13779 516 QELR--EALDDYMQAL---AEQAQQNPQDLQQPDDPNAQEMTQQDLQRMLDRIEELARSGRRAEAQQMLSQLQQMLENLQ 590
|
90 100
....*....|....*....|....*....
gi 157818007 508 TEQR--LSKERIGELQQQIEDLQKSLQEQ 534
Cdd:pfam13779 591 AGQPqqQQQQGQSEMQQAMDELGDLLREQ 619
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
171-659 |
1.69e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 41.65 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 171 DAVGELEQQLKRALEELQEALAEKEELKQRCQELDMQvtalqdeknslVSENEMMNEKLDQLDGSFDDPNTMVAKKYFHV 250
Cdd:pfam05557 111 NELSELRRQIQRAELELQSTNSELEELQERLDLLKAK-----------ASEAEQLRQNLEKQQSSLAEAEQRIKELEFEI 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 251 QLQLEQLQEenyrLEAAKDDYrVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRA-------TSDKANKLESTV 323
Cdd:pfam05557 180 QSQEQDSEI----VKNSKSEL-ARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRklereekYREEAATLELEK 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 324 EVYRQKLQ-----------DLN---DLRKQVKSLQETNMMYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSES 389
Cdd:pfam05557 255 EKLEQELQswvklaqdtglNLRspeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKL 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 390 KRADTLAfemKRLEEKHETLLKEkerlieqRDTLKETNEELrcskaqQDHLNQADSSATKSYENLAAEIMPVEYREVFIR 469
Cdd:pfam05557 335 KRHKALV---RRLQRRVLLLTKE-------RDGYRAILESY------DKELTMSNYSPQLLERIEEAEDMTQKMQAHNEE 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 470 LQHenKMLRLQQEGTENERIEQLQEQlEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQGSKsegesssklKQK 549
Cdd:pfam05557 399 MEA--QLSVAEEELGGYKQQAQTLER-ELQALRQQESLADPSYSKEEVDSLRRKLETLELERQRLREQ---------KNE 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 550 LEAHMEKLTEVHEELQKKQELIEDLQPDISQNAQKISELEAALQKKDEDMKAMEERYKMYLEKARNVIKTldpKLNPASA 629
Cdd:pfam05557 467 LEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPET---TSTMNFK 543
|
490 500 510
....*....|....*....|....*....|..
gi 157818007 630 EIMLLRKQLAEKDRRIEILESECKVA--KFRD 659
Cdd:pfam05557 544 EVLDLRKELESAELKNQRLKEVFQAKiqEFRD 575
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
400-653 |
2.24e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 400 KRLEEKHETLLKEKERLIEQRDTLKETNEELRCSKAQQDHLNQADSSATKSYENLAAEIMPVEYREVFIRLQHENKMLRL 479
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 480 QQEGTENERIEQLQEQLEQKHRKMNELETEQRLSKErIGELQQQIEDLQKSLQEqgSKSEGESSSKLKQKLEAHMEKLTE 559
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEE--YLDELREIEKRLSRLEEEINGIEE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 560 VHEELQKKQELIEDLQPDISQNAQKISELEAALQKKDEDMKAMEERYKMYLEKARNVIKTLDPKLNPASAEIMLLRKQLA 639
Cdd:PRK03918 329 RIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEIS 408
|
250
....*....|....
gi 157818007 640 EKDRRIEILESECK 653
Cdd:PRK03918 409 KITARIGELKKEIK 422
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
468-624 |
2.33e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 468 IRLQH-ENKMLRLQQE-GTENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQ---KSLQEQGSKSE--- 539
Cdd:COG1579 10 LDLQElDSELDRLEHRlKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEariKKYEEQLGNVRnnk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 540 -----GESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDISQNAQKISELEAALqkkDEDMKAMEERYKMYLEKAR 614
Cdd:COG1579 90 eyealQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL---DEELAELEAELEELEAERE 166
|
170
....*....|
gi 157818007 615 NVIKTLDPKL 624
Cdd:COG1579 167 ELAAKIPPEL 176
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
263-457 |
2.79e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 263 RLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIdvlRATSDKANKLESTVEVYRQKLQDLN-DLRKQVK 341
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI---RALEQELAALEAELAELEKEIAELRaELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 342 SLQE-TNMMYMHNTVSLEEELKKANAARAQLetykRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQR 420
Cdd:COG4942 105 ELAElLRALYRLGRQPPLALLLSPEDFLDAV----RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 157818007 421 DTLKETNEELRCSKAQQDHLNQADSSATKSYENLAAE 457
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
155-533 |
3.39e-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: 41.11 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 155 AIQELMSKEIVSSPASDAVGELEQQLKRALEELQEALAEKEELKQRCQELDMQVTAlQDEKNSLVSENEMMNEKLDQLDG 234
Cdd:pfam02463 650 KGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKE-QREKEELKKLKLEAEELLADRVQ 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 235 SFDDPNTMVAKKYFHVQLQLEQLQEENYRLEAAKDDYRVHCEELEKQLIEFQHRNdeltslaEETRALKDEIDVLRATSD 314
Cdd:pfam02463 729 EAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKT-------EKLKVEEEKEEKLKAQEE 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 315 KANKLESTVEVYRQKLQDLNDLRKQVKSLQETNMMYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADT 394
Cdd:pfam02463 802 ELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEE 881
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 395 LAF--EMKRLEEKHETLLKEKERLIEQRDTLKETNEELRCSKAQQDHLNQADSSATKSYEnLAAEIMPVEYREVFIRLQH 472
Cdd:pfam02463 882 QKLkdELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELL-LEEADEKEKEENNKEEEEE 960
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157818007 473 ENKMLRLQQEGTENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQE 533
Cdd:pfam02463 961 RNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
400-665 |
3.54e-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: 40.73 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 400 KRLEEKHETLLKEKERLIEQRDTLKETNEELRCSKAQqdhlnqaDSSATKSYENLAAEIMPVEYREVFIRLQH-ENKMLR 478
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQ-------AKKALEYYQLKEKLELEEEYLLYLDYLKLnEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 479 LQQEGTENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQiEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLT 558
Cdd:pfam02463 242 LQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEE-ELKLLAKEEEELKSELLKLERRKVDDEEKLKESE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 559 EVHEELQKKQELiedLQPDISQNAQKISELEAALQKKDEDMKAMEERYKMYLEKARNVIKTLDPKLNPASAEIMLLRKQL 638
Cdd:pfam02463 321 KEKKKAEKELKK---EKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEEL 397
|
250 260
....*....|....*....|....*..
gi 157818007 639 AEKDRRIEILESECKVAKFRDYEEKLI 665
Cdd:pfam02463 398 ELKSEEEKEAQLLLELARQLEDLLKEE 424
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
464-617 |
3.61e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 464 REVFIRLQHENKMLRLQQEGTENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKslQEQGSKSEGESS 543
Cdd:PRK12704 56 KEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQ--KQQELEKKEEEL 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157818007 544 SKLKQKLEAHMEKLTEVHEElQKKQELIEDLQPDISQNAQKIseleaalqkkdedMKAMEERYKMYLEK-ARNVI 617
Cdd:PRK12704 134 EELIEEQLQELERISGLTAE-EAKEILLEKVEEEARHEAAVL-------------IKEIEEEAKEEADKkAKEIL 194
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
176-463 |
3.83e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.66 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 176 LEQQLKRALEELQEALAEKEELKQRCQELDMQVtALQDEKNSLVSEN----EMMNEKLDQLDGSFDDPNTMVAKKYFHVQ 251
Cdd:PLN02939 147 LNQARLQALEDLEKILTEKEALQGKINILEMRL-SETDARIKLAAQEkihvEILEEQLEKLRNELLIRGATEGLCVHSLS 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 252 LQLEQLQEENYRLeaaKDDyrvhCEELEKQLIEFQHRNDELTSLAEEtRALKD------EIDVLRATSDKANKLESTVEV 325
Cdd:PLN02939 226 KELDVLKEENMLL---KDD----IQFLKAELIEVAETEERVFKLEKE-RSLLDaslrelESKFIVAQEDVSKLSPLQYDC 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 326 YRQKLQDLNDLRKQVKSLQETNMMYMHNTVSLEEELKKANAARAQLETYkrqvqdlhtKLSSEskRADTLAFEMKRLEEK 405
Cdd:PLN02939 298 WWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVS---------KFSSY--KVELLQQKLKLLEER 366
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 157818007 406 HEtllKEKERLIEQRDTLKETNEELrcskaqQDHLNQADSSATKSYENLAAEIMPVEY 463
Cdd:PLN02939 367 LQ---ASDHEIHSYIQLYQESIKEF------QDTLSKLKEESKKRSLEHPADDMPSEF 415
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
286-528 |
4.02e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 286 QHRNDELTSLAEETRALKDEIDVLRAtsdKANKLESTVEVYRQKlQDLNDLRKQVKSLQEtnmmymhNTVSLEEELKKAN 365
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRK---ELEEAEAALEEFRQK-NGLVDLSEEAKLLLQ-------QLSELESQLAEAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 366 AARAQLETYKRQVQdlhtKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKETNEELRCSKAQQDHLNQads 445
Cdd:COG3206 233 AELAEAEARLAALR----AQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRA--- 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 446 satksyeNLAAEImpveyREVFIRLQHENKMLRlQQEGTENERIEQLQEQLE---QKHRKMNELETEQRLSKERIGELQQ 522
Cdd:COG3206 306 -------QLQQEA-----QRILASLEAELEALQ-AREASLQAQLAQLEARLAelpELEAELRRLEREVEVARELYESLLQ 372
|
....*.
gi 157818007 523 QIEDLQ 528
Cdd:COG3206 373 RLEEAR 378
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
175-585 |
4.26e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 175 ELEQQLKRALEELQEALAEKEELKQRCQELDMQVTALQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAKKYFHVQLQL 254
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 255 EQLQEENYRLEAAKDDYRVHCEELEKQLIEFQhrndELTSLAEETRALKDEIDVLRATSDKANKLESTVEVYRQKLQDLN 334
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLE----NELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAG 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 335 DLRKQVKSLQETNMMYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKE 414
Cdd:COG4717 278 VLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 415 RLIEQRDTLketneelRCSKAQQDHLNQADSSATKSYENLAAEImpVEYREVFIRLQHENKMLRLQ----QEGTENERIE 490
Cdd:COG4717 358 ELEEELQLE-------ELEQEIAALLAEAGVEDEEELRAALEQA--EEYQELKEELEELEEQLEELlgelEELLEALDEE 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 491 QLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSlqeqgsksegESSSKLKQKLEAHMEKLTEVHEELQK---- 566
Cdd:COG4717 429 ELEEELEELEEELEELEEELEELREELAELEAELEQLEED----------GELAELLQELEELKAELRELAEEWAAlkla 498
|
410 420
....*....|....*....|....*.
gi 157818007 567 -------KQELIEDLQPDISQNAQKI 585
Cdd:COG4717 499 lelleeaREEYREERLPPVLERASEY 524
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
164-420 |
4.30e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 164 IVSSPASDAVGELEQQLKRALEELQEALAEKEElkqrcqeldmQVTALQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMV 243
Cdd:COG4942 9 LLLALAAAAQADAAAEAEAELEQLQQEIAELEK----------ELAALKKEEKALLKQLAALERRIAALARRIRALEQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 244 AKkyfhvqlQLEQLQEENYRLEAAKDDYRVHCEELEKQLIEFQ--HRNDELTSLAEETRALkDEIDVLRATSDKANKLES 321
Cdd:COG4942 79 AA-------LEAELAELEKEIAELRAELEAQKEELAELLRALYrlGRQPPLALLLSPEDFL-DAVRRLQYLKYLAPARRE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 322 TVEVYRQKLQDLNDLRKQVKSLQETnmmymhntvsLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKR 401
Cdd:COG4942 151 QAEELRADLAELAALRAELEAERAE----------LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
250
....*....|....*....
gi 157818007 402 LEEKHETLLKEKERLIEQR 420
Cdd:COG4942 221 EAEELEALIARLEAEAAAA 239
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
175-557 |
4.64e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.42 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 175 ELEQQLKRALEELQEALAEKEELKQRCQELDMQVTALQDEKNSLVSENEMMNEKLDQLdgsfddpNTMVAKKYFHVQLQL 254
Cdd:TIGR00606 699 DLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKV-------NRDIQRLKNDIEEQE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 255 EQLQEENYRLEAAKD---DYRVhCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEVYRQKLQ 331
Cdd:TIGR00606 772 TLLGTIMPEEESAKVcltDVTI-MERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 332 DLNDLRKQVKSLQETNMMYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLK 411
Cdd:TIGR00606 851 LIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS 930
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 412 EKER-----LIEQRDTLKETNEELRCSKAQQDHLNQADSSATKSYENLAAEIMpVEYREVFIRLQHENKMLRLQQEGTEN 486
Cdd:TIGR00606 931 SKETsnkkaQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVN-AQLEECEKHQEKINEDMRLMRQDIDT 1009
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157818007 487 ERIEQ--LQEQLEQKHR--KMNELETEQRLSKERIGELQ-QQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKL 557
Cdd:TIGR00606 1010 QKIQErwLQDNLTLRKRenELKEVEEELKQHLKEMGQMQvLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIK 1085
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
182-602 |
4.66e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.27 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 182 RALEELQEALAEKEELKQRCQELDMQVTAL---QDEKNSLVSENEMMNEKLDQ---------------LDGSFDDPNTMV 243
Cdd:PRK01156 329 KKLSVLQKDYNDYIKKKSRYDDLNNQILELegyEMDYNSYLKSIESLKKKIEEyskniermsafiseiLKIQEIDPDAIK 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 244 aKKYFHVQLQLEQLQEENYRLEAAKDDYRVHCEELEKQLIEFQHRNDEL---TSLAEETRAlkdeiDVLRATSDKANKLE 320
Cdd:PRK01156 409 -KELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPvcgTTLGEEKSN-----HIINHYNEKKSRLE 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 321 STVEVYRQKLQDLNDLRKQVKSLQEtnMMYMHNTVSLEEELKKANAARAQLETYK---RQVQDLHTKLSSESKRADTLAF 397
Cdd:PRK01156 483 EKIREIEIEVKDIDEKIVDLKKRKE--YLESEEINKSINEYNKIESARADLEDIKikiNELKDKHDKYEEIKNRYKSLKL 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 398 EMkrLEEKHETLLKekerLIEQRDTLketneELRCSKAQQDHLNQADSSATKSYENLAAEIMPVE-YREVFIRLQHEnkm 476
Cdd:PRK01156 561 ED--LDSKRTSWLN----ALAVISLI-----DIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKsYIDKSIREIEN--- 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 477 lrlqqegtENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQqIEDLQKSLQEQGSKSEGESSSKLKQkleahmek 556
Cdd:PRK01156 627 --------EANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDS-IIPDLKEITSRINDIEDNLKKSRKA-------- 689
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 157818007 557 LTEVHEELQKKQELIEDLQPDISQNAQKISELEAALQKKDEDMKAM 602
Cdd:PRK01156 690 LDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAI 735
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
281-607 |
4.93e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.19 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 281 QLIEFQHRNDELTSLAEETRALKDEIDVlratsdKANKLESTVEVYRqklqdlnDLRKQVKSLQETNMmymHNTVSLEEE 360
Cdd:pfam10174 210 HLREELHRRNQLQPDPAKTKALQTVIEM------KDTKISSLERNIR-------DLEDEVQMLKTNGL---LHTEDREEE 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 361 LKkanaaraQLETYKRQVQDLHTK---LSSESKRADTlafEMKRLEEKHETLLKEKERLIEQRDTLKE--TNEELRCSKA 435
Cdd:pfam10174 274 IK-------QMEVYKSHSKFMKNKidqLKQELSKKES---ELLALQTKLETLTNQNSDCKQHIEVLKEslTAKEQRAAIL 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 436 QQD------HLNQADSSATKSYENLaaEIMPVEYREVFIRLQHENKMLRLQQE--GTENERIEQLQEQLEQKHRKMNELE 507
Cdd:pfam10174 344 QTEvdalrlRLEEKESFLNKKTKQL--QDLTEEKSTLAGEIRDLKDMLDVKERkiNVLQKKIENLQEQLRDKDKQLAGLK 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 508 T-------------------EQRLS-KERIGE-LQQQIEDLQKSLQEQGSKSEGESSSkLKQKLEAHMEKLTEVHEELQK 566
Cdd:pfam10174 422 ErvkslqtdssntdtalttlEEALSeKERIIErLKEQREREDRERLEELESLKKENKD-LKEKVSALQPELTEKESSLID 500
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 157818007 567 KQELIEDLQPDISQNAQKISELEAALQKKDEDMKAMEERYK 607
Cdd:pfam10174 501 LKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLK 541
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
353-528 |
5.53e-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: 40.32 E-value: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 353 NTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKETNEELRc 432
Cdd:COG3096 513 RLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLR- 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 433 skAQQDHLnqadssATKSYENLAAeimpveyREVFIRLQhenkmlrlQQEGTENERIEQLQEQLEQKHRKMNELETEQRL 512
Cdd:COG3096 592 --ARIKEL------AARAPAWLAA-------QDALERLR--------EQSGEALADSQEVTAAMQQLLEREREATVERDE 648
|
170
....*....|....*.
gi 157818007 513 SKERIGELQQQIEDLQ 528
Cdd:COG3096 649 LAARKQALESQIERLS 664
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
161-379 |
6.26e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 6.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 161 SKEIVSSPASDAVGELEQQLKRALEELQEALAEKEELKQRCQELDM---------QVTALQDEKNSLVSENEMMNEKLDQ 231
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLseeaklllqQLSELESQLAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 232 LDGSFDDPNTMVAkkyfhvqlqleqLQEENYRLEAAKDDYRvhceELEKQLIE----FQHRNDELTSLAEETRALKDEID 307
Cdd:COG3206 245 LRAQLGSGPDALP------------ELLQSPVIQQLRAQLA----ELEAELAElsarYTPNHPDVIALRAQIAALRAQLQ 308
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157818007 308 vlRATSDKANKLESTVEVYRQKLQDLNDLRKQvkslqetnmmymhntvsLEEELKKANAARAQLETYKRQVQ 379
Cdd:COG3206 309 --QEAQRILASLEAELEALQAREASLQAQLAQ-----------------LEARLAELPELEAELRRLEREVE 361
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
175-607 |
6.60e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.95 E-value: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 175 ELEQQLKRALEELQEALAEKEELKQRCQELDMQVTALQdEKNSLVSENEMMNEKLDQLDGSfdDPNTMVAKKYFHVQLQL 254
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIE-ELRAQEAVLEETQERINRARKA--APLAAHIKAVTQIEQQA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 255 EQLQEENYRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDV---LRATSDKANKLESTVEVYRQKLQ 331
Cdd:TIGR00618 310 QRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVatsIREISCQQHTLTQHIHTLQQQKT 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 332 DLNDLRKQVKSL--QETNMMYMHNTVSLEEELKKANAARA----QLETYKRQVQDLH-TKLSSESKRADTLAFEMKRLEE 404
Cdd:TIGR00618 390 TLTQKLQSLCKEldILQREQATIDTRTSAFRDLQGQLAHAkkqqELQQRYAELCAAAiTCTAQCEKLEKIHLQESAQSLK 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 405 KHETLLKEKERlIEQRDTLKETNEELRCSKAQQDHLNQADSSATKSYENLAAEIMPVEYREVfirLQHENKMLRLQQEG- 483
Cdd:TIGR00618 470 EREQQLQTKEQ-IHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRM---QRGEQTYAQLETSEe 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 484 -------TENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQgsksegesssklkqkLEAHMEK 556
Cdd:TIGR00618 546 dvyhqltSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKL---------------SEAEDML 610
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 157818007 557 LTEVHEELQKKQELIEDLQPDIS--QNAQKISELEAALQKKDEDMKAMEERYK 607
Cdd:TIGR00618 611 ACEQHALLRKLQPEQDLQDVRLHlqQCSQELALKLTALHALQLTLTQERVREH 663
|
|
| FapA |
pfam03961 |
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ... |
486-574 |
6.64e-03 |
|
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta solenoid domain of FapA and its homologs. Members of this family include FapA (flagellar assembly protein A) found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction. This entry shows similarity to pfam03775 suggesting a similar functional role.
Pssm-ID: 461111 [Multi-domain] Cd Length: 272 Bit Score: 39.21 E-value: 6.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 486 NERIEQLQEQLEQKhrkmneleteqrlsKERIGELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEELQ 565
Cdd:pfam03961 155 KEKLEELEKELEEL--------------EEELEKLKKRLKKLPKKARGQLPPEKREQLEKLLETKNKLSEELEELEEELK 220
|
....*....
gi 157818007 566 KKQELIEDL 574
Cdd:pfam03961 221 ELKEELESL 229
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
495-651 |
7.08e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 495 QLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQgskseGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDL 574
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNEL-----QAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 575 QPDISQNAQKISELEAALQKKD--------EDMKAMEERYKMYLEKARNVIKTLDPKLNPASAEIMLLRKQLAEKDRRIE 646
Cdd:COG3883 92 ARALYRSGGSVSYLDVLLGSESfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
....*
gi 157818007 647 ILESE 651
Cdd:COG3883 172 ELEAQ 176
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
327-599 |
8.41e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 39.65 E-value: 8.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 327 RQKLQDLNDLRKQVKSLQETNMMYMHNTVSLEEELKKANAaRAQ-----LETYKRQVQDLHTKLSSESKRADTLAFEMKR 401
Cdd:PRK10929 26 KQITQELEQAKAAKTPAQAEIVEALQSALNWLEERKGSLE-RAKqyqqvIDNFPKLSAELRQQLNNERDEPRSVPPNMST 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 402 LEEKHETL-----LKEKERLIEQ-RDTLKETNEELRCSKAQQDHLNQADSSATKsyenlaaeimpveyrevfirlqhenk 475
Cdd:PRK10929 105 DALEQEILqvssqLLEKSRQAQQeQDRAREISDSLSQLPQQQTEARRQLNEIER-------------------------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 476 mlRLQQEGTENERIEQLQE---QLEQKHRK--MNELETEQ-------RLSKERIGELQQQIEDLQKSLQEQGSKSEGESS 543
Cdd:PRK10929 159 --RLQTLGTPNTPLAQAQLtalQAESAALKalVDELELAQlsannrqELARLRSELAKKRSQQLDAYLQALRNQLNSQRQ 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 157818007 544 SKLKQKLEaHMEKLTEVheelqkkqelIEDLQPDISQNAQKISELEAALQKKDEDM 599
Cdd:PRK10929 237 REAERALE-STELLAEQ----------SGDLPKSIVAQFKINRELSQALNQQAQRM 281
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
269-607 |
9.10e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.56 E-value: 9.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 269 DDYRVHCEELEK----QLIEFQHRNDELTSLAEETRALKDE-IDVLRATSDKANKLESTVEVYRQKLQDLNDLRKQvksl 343
Cdd:PRK04863 746 DDSVFSVEELEKavvvKIADRQWRYSRFPEVPLFGRAAREKrIEQLRAEREELAERYATLSFDVQKLQRLHQAFSR---- 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 344 qetnMMYMHNTVSL----EEELKKANAARAQLEtykRQVQDLHTKLSSESKRADTLAFEMKRLEE--KHETLLKEK---E 414
Cdd:PRK04863 822 ----FIGSHLAVAFeadpEAELRQLNRRRVELE---RALADHESQEQQQRSQLEQAKEGLSALNRllPRLNLLADEtlaD 894
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 415 RLIEQRDTLKETNEELRCSKAQQDHLNQADSSATK------SYENLAAEIMPVEYR------------EVFIRLQHENKM 476
Cdd:PRK04863 895 RVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVlqsdpeQFEQLKQDYQQAQQTqrdakqqafaltEVVQRRAHFSYE 974
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 477 LRLQQEGTENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQeqgskSEGESSSKLKQKLEAHMEK 556
Cdd:PRK04863 975 DAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYD-----AKRQMLQELKQELQDLGVP 1049
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 157818007 557 LTEVHEELQKKQEliEDLQPDISQNAQKISELEAALQKKDEDMKAMEERYK 607
Cdd:PRK04863 1050 ADSGAEERARARR--DELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLR 1098
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
315-601 |
9.95e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.39 E-value: 9.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 315 KANKLESTVEVYRQKLQDLNDLRKQVKSLQETNMMYMHNTVSLEEELKKANAARAQLETYKRQ----VQDLHTKLSSESK 390
Cdd:pfam01576 10 KEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQEleeiLHELESRLEEEEE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 391 RADTLAFEMKRLEEKHETLLK--EKERLIEQRDTLKETNEELRCSKAQQDHLNQADSSATKSYENLAAEIMPVEYREVFI 468
Cdd:pfam01576 90 RSQQLQNEKKKMQQHIQDLEEqlDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818007 469 RLQHENKML---RLQQEGTenerIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQGSksegesssk 545
Cdd:pfam01576 170 EEEEKAKSLsklKNKHEAM----ISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRA--------- 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 157818007 546 lkqkleahmeKLTEVHEELQKKQELIEDLQPDISQNAQKISELEAALQKKDEDMKA 601
Cdd:pfam01576 237 ----------QLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLES 282
|
|
| |
