|
Name |
Accession |
Description |
Interval |
E-value |
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
191-724 |
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: 644.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 191 ELQEALAEKEELKQRCQELDMQVTALQDEKNSLVSENEMMNEKLDQLDgSFDDPNTMVAKKYFHVQLQLEQLQEENYRLE 270
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLE-SGDDSGTPGGKKYLLLQKQLEQLQEENFRLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 271 AAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEVYRQKLQDLNDLRKQVKSLQE 350
Cdd:pfam05622 80 TARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLGDLRRQVKLLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 351 TNMMYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKE 430
Cdd:pfam05622 160 RNAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 431 TNEELRCSKAQQDHLNQADSSATKSY---ENLAAEIMPVEYREVFIRLQHENKMLRLQQEGTENERIEQLQEQLEQKHRK 507
Cdd:pfam05622 240 TNEELRCAQLQQAELSQADALLSPSSdpgDNLAAEIMPAEIREKLIRLQHENKMLRLGQEGSYRERLTELQQLLEDANRR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 508 MNELETEQRLSKERIGELQQQIEDLQKSLQEQgsKSEGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDISQN- 586
Cdd:pfam05622 320 KNELETQNRLANQRILELQQQVEELQKALQEQ--GSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNl 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 587 AQKISELEAALQKKDEDMKAMEERYKMYLEKARNVIKTLDPKLNPAS-AEIMLLRKQLAEKDRRIEILESECKVAKF-RD 664
Cdd:pfam05622 398 AQKIDELQEALRKKDEDMKAMEERYKKYVEKAKSVIKTLDPKQNPASpPEIQALKNQLLEKDKKIEHLERDFEKSKLqRE 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 665 YEEKLIVSAWYNKSLAFQKLGMESRLVSGASackdsvaaaPARSFLAQQRHITSTRRNLS 724
Cdd:pfam05622 478 QEEKLIVTAWYNMGMALHRKAIEERLAGLSS---------PGQSFLARQRQATNARRGLS 528
|
|
| HkD_Hook1 |
cd22225 |
Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a ... |
27-168 |
1.92e-89 |
|
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: 276.73 E-value: 1.92e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 27 LQTFKTASPCQDVKQLTNGVTMAQVLHQIDVAWFSESWLSRIKDDVGDNWRIKASNLKKVLHGITSYYHEFLGQQISEEL 106
Cdd:cd22225 9 LQTFNTAAPCQTVQDLTSGVAMAQVLHQIDSSWFDESWLSRIKEDVGDNWRIKMSNLKKILQGIVDYYHEFLDQQISEFL 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958776293 107 IPDLNQITESSDPVELGRLLQLILGCAVNCEKKQEHIKNIMTLEESVQHVVMTAIQELMSKE 168
Cdd:cd22225 89 LPDLNRIAEHSDPVELGRLLQLILGCAVNCEKKQEHIQNIMTLEESVQHVVMTAIQELMSKE 150
|
|
| HOOK_N |
pfam19047 |
HOOK domain; This domain is found at the N-terminus of HOOK proteins. |
27-168 |
1.52e-81 |
|
HOOK domain; This domain is found at the N-terminus of HOOK proteins.
Pssm-ID: 465958 Cd Length: 151 Bit Score: 256.18 E-value: 1.52e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 27 LQTFKTASPCQDVKQLTNGVTMAQVLHQIDVAWFSESWLSRIKDDVGDNWRIKASNLKKVLHGITSYYHEFLGQQISEEL 106
Cdd:pfam19047 10 LQTFNVPAPCATVEDLTDGVAMAQVLHQIDPSWFTEAWLSRIKEDVGDNWRLKVSNLKKILQSVVDYYQDVLGQQISDFL 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958776293 107 IPDLNQITESSDPVELGRLLQLILGCAVNCEKKQEHIKNIMTLEESVQHVVMTAIQELMSKE 168
Cdd:pfam19047 90 LPDVNLIGEHSDPAELGRLLQLILGCAVNCEKKQEYIQQIMTLEESVQHVVMTAIQELMSKD 151
|
|
| HkD_Hook |
cd22222 |
Hook domain found in Hook family of microtubule-binding proteins; The Hook family includes ... |
27-166 |
1.28e-77 |
|
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: 245.62 E-value: 1.28e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 27 LQTFKTASPCQDVKQLTNGVTMAQVLHQIDVAWFSESWLSRIKDDVGDNWRIKASNLKKVLHGITSYYHEFLGQQISEEL 106
Cdd:cd22222 8 LQTFNLIAPHATAEDLSDGVAIAQVLNQIDPEYFSDSWLSKIKPDVGDNWRLKVSNLKKILKGIVDYYSEVLGQQISGFT 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 107 IPDLNQITESSDPVELGRLLQLILGCAVNCEKKQEHIKNIMTLEESVQHVVMTAIQELMS 166
Cdd:cd22222 88 MPDVNAIAEKEDPKELGRLLQLVLGCAVNCERKEEYIQAIMGLEESVQHVVMEAIQELMS 147
|
|
| HkD_Hook3 |
cd22226 |
Hook domain found in protein Hook 3 (Hook3) and similar proteins; Hook3 is an adaptor protein ... |
27-167 |
9.17e-65 |
|
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: 211.75 E-value: 9.17e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 27 LQTFKTASPCQDVKQLTNGVTMAQVLHQIDVAWFSESWLSRIKDDVGDNWRIKASNLKKVLHGITSYYHEFLGQQISEEL 106
Cdd:cd22226 13 IQTFNVDAPCQTVEDLTSGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEILGQQINDFT 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958776293 107 IPDLNQITESSDPVELGRLLQLILGCAVNCEKKQEHIKNIMTLEESVQHVVMTAIQELMSK 167
Cdd:cd22226 93 LPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMSK 153
|
|
| HkD_Hook2 |
cd22227 |
Hook domain found in protein Hook 2 (Hook2) and similar proteins; Hook2 is a ... |
27-167 |
1.03e-62 |
|
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: 206.26 E-value: 1.03e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 27 LQTFKTASPCQDVKQLTNGVTMAQVLHQIDVAWFSESWLSRIKDDVGDNWRIKASNLKKVLHGITSYYHEFLGQQISEEL 106
Cdd:cd22227 10 LQTFQVPSPCSSYQDLTSGVAIAQVLNRIDPSWFNEAWLGRIKEDTGDNWRLKVSNLKKILQSLLEYYQDVLGHQVSEDH 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958776293 107 IPDLNQITESSDPVELGRLLQLILGCAVNCEKKQEHIKNIMTLEESVQHVVMTAIQELMSK 167
Cdd:cd22227 90 LPDVNLIGEFSDDTELGKLLQLVLGCAISCEKKQEHIQQIMTLEESVQHVVMEAIQELLTK 150
|
|
| HkD_SF |
cd22211 |
Hook domain-containing proteins superfamily; The Hook domain superfamily includes Hook adaptor ... |
27-166 |
6.53e-46 |
|
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: 160.13 E-value: 6.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 27 LQTFKTASPCQDVKQLTNGVTMAQVLHQIDVAWFSESWLSriKDDVGDNWRIKASNLKKVLHGITSYYHEFLGQQISEEL 106
Cdd:cd22211 8 INTFPLSSPVESLDDLSDGVVLAEILSQIDPSYFDSEWLE--SRDSSDNWVLKLNNLKKLYRSLSKYYREVLGQQLSDLP 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 107 IPDLNQITESSDPVELGRLLQLILGCAVNCEKKQEHIKNIMTLEESVQHVVMTAIQELMS 166
Cdd:cd22211 86 LPDLSAIARDGDEEEIVKLLELVLGAAVQCENKEEYIARIQQLDESTQAELMLIIQEVLE 145
|
|
| HkD_HkRP |
cd22223 |
Hook domain found in the Hook-related protein (HkRP) family; The HkRP family includes Daple, ... |
27-164 |
6.15e-23 |
|
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: 95.35 E-value: 6.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 27 LQTFKTASPCQ-DVKQLTNGVTMAQVLHQIDVAWFSESWLSRIKDDVgdNWRIKasNLKKVLHGITSYYHEFLGQQISEE 105
Cdd:cd22223 10 AKTFADDGSAElSYTDLVDGVFLNNVMLQIDPRPFSEVSNRNVDDDV--NARIQ--NLDLLLRNIKSFYQEVLQQLIVMK 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958776293 106 LiPDLNQITESSDP----VELGRLLQLILGCAVNCEKKQEHIKNIMTLEESVQHVVMTAIQEL 164
Cdd:cd22223 86 L-PDILTIGREPESeqslEELEKLLLLLLGCAVQCERKEEFIERIKNLDLEVQHALVACIQEV 147
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
276-623 |
8.50e-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: 72.01 E-value: 8.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 276 YRVHCEELEKQLIEFQHRNDELTSLAEEtraLKDEIDVLRATSDKANKLESTVEVYRQKLQDL--NDLRKQVKSLQETNM 353
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDRLEDILNE---LERQLKSLERQAEKAERYKELKAELRELELALlvLRLEELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 354 MYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLlkeKERLIEQRDTLKETNE 433
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIL---RERLANLERQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 434 ELRCSKAQQDHLNQADSSATKSYENLAAEImpVEYREVFIRLQHENKMLrlqqegteNERIEQLQEQLEQKHRKMNELET 513
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEELKEEL--ESLEAELEELEAELEEL--------ESRLEELEEQLETLRSKVAQLEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 514 EQRLSKERIGELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDISQNAQKISEL 593
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEA 473
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1958776293 594 EAALQKKDED----------MKAMEERYKMYLEKARNVIK 623
Cdd:TIGR02168 474 EQALDAAERElaqlqarldsLERLQENLEGFSEGVKALLK 513
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
296-656 |
3.62e-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: 3.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 296 ELTSLAEETRALKDEIDVLRATSDkaNKLESTVEVYRQKLQDL-NDLRKQVKSLQETNMMYMHNTVSLEEELKK-ANAAR 373
Cdd:pfam15921 232 EISYLKGRIFPVEDQLEALKSESQ--NKIELLLQQHQDRIEQLiSEHEVEITGLTEKASSARSQANSIQSQLEIiQEQAR 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 374 AQLETYKRQVQDLHTKLSSeskradtLAFEMKRLEEKHETLLKEKERlieqrdTLKETNEELRCSKAQQDHLNQADSSAT 453
Cdd:pfam15921 310 NQNSMYMRQLSDLESTVSQ-------LRSELREAKRMYEDKIEELEK------QLVLANSELTEARTERDQFSQESGNLD 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 454 KSYENLAAEImpvEYREVFIRLQHENKMLRLQQEGTENERIEQLQEQLEQKHRKMNELETeqrLSKERIGELQQQIEDLQ 533
Cdd:pfam15921 377 DQLQKLLADL---HKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEA---LLKAMKSECQGQMERQM 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 534 KSLQEQGSKSEGESSskLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDISQNAQKISELEAALQKKDEDMKAMEERYKM 613
Cdd:pfam15921 451 AAIQGKNESLEKVSS--LTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDL 528
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1958776293 614 YLEKARNvIKTLDPKLNPASAEIMLLRKQLAEKDRRIEILESE 656
Cdd:pfam15921 529 KLQELQH-LKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQ 570
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
173-656 |
5.50e-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: 5.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 173 PASDAVGELEQQLKRALEELQEAlaEKEELKQRCQELDMQVTALQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAKky 252
Cdd:pfam15921 242 PVEDQLEALKSESQNKIELLLQQ--HQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMR-- 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 253 fHVQLQLEQLQEENYRLEAAKDDYRVHCEELEKQLI----EFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLES-- 326
Cdd:pfam15921 318 -QLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVlansELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSle 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 327 ----------------TVEVYRQKLQD-------LNDLRKQVKSLQETNM-MYMHNTVSLEEELKKANAARAQLETYK-- 380
Cdd:pfam15921 397 keqnkrlwdrdtgnsiTIDHLRRELDDrnmevqrLEALLKAMKSECQGQMeRQMAAIQGKNESLEKVSSLTAQLESTKem 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 381 --RQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKETNEELRCSKAQQDHLNQADSSATKSYEN 458
Cdd:pfam15921 477 lrKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQ 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 459 LAAEIMPVEyrevFIRLQHENKMLRLQQEGTENERIE----QLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQK 534
Cdd:pfam15921 557 MAEKDKVIE----ILRQQIENMTQLVGQHGRTAGAMQvekaQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLEL 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 535 SlqeqgsksegesssklKQKL-EAHMEKLTEVHEELQKKQELIEDLQP---DISQNAQKISELEAALQKKDEDMKAMEER 610
Cdd:pfam15921 633 E----------------KVKLvNAGSERLRAVKDIKQERDQLLNEVKTsrnELNSLSEDYEVLKRNFRNKSEEMETTTNK 696
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1958776293 611 YKMYL-------EKARNVIKTLDPKLNPASAEIMLLRKQLAEKDRRIEILESE 656
Cdd:pfam15921 697 LKMQLksaqselEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSK 749
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
159-656 |
8.60e-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: 8.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 159 TAIQELMSKEIVSSPASDAVGELEQqLKRALEELQEAL----AEKEELKQRCQELDMQVTALQDEKNSLVSENEMMNEKL 234
Cdd:TIGR02168 420 QQEIEELLKKLEEAELKELQAELEE-LEEELEELQEELerleEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 235 DQLDGSFDDPNTMVAKKY----FHVQLQLEQLQEENYR------LEAAKDDYRVHCEELEKQLIEFQHRNdeltslaEET 304
Cdd:TIGR02168 499 ENLEGFSEGVKALLKNQSglsgILGVLSELISVDEGYEaaieaaLGGRLQAVVVENLNAAKKAIAFLKQN-------ELG 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 305 RALKDEIDVLRATSDKANKLEStVEVYRQKLQDLNDLRKQVKSLQeTNMMYMHNTVSLEEELKKANAARAQLETYKRQVQ 384
Cdd:TIGR02168 572 RVTFLPLDSIKGTEIQGNDREI-LKNIEGFLGVAKDLVKFDPKLR-KALSYLLGGVLVVDDLDNALELAKKLRPGYRIVT 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 385 DLHTKLS--------SESKRADTLA--FEMKRLEEKHETLLKE----KERLIEQRDTLKETNEELRCSKAQQDHLNQADS 450
Cdd:TIGR02168 650 LDGDLVRpggvitggSAKTNSSILErrREIEELEEKIEELEEKiaelEKALAELRKELEELEEELEQLRKELEELSRQIS 729
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 451 SATKSYENLAAEIMPVEYRevFIRLQHENKMLRlQQEGTENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIE 530
Cdd:TIGR02168 730 ALRKDLARLEAEVEQLEER--IAQLSKELTELE-AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD 806
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 531 DLQKSLQEQGSK--SEGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDISQNAQKISELEAALQKKDEDMKAME 608
Cdd:TIGR02168 807 ELRAELTLLNEEaaNLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1958776293 609 ERYKMY---LEKARNVIKTLDPKLNPASAEIMLLRKQLAEKDRRIEILESE 656
Cdd:TIGR02168 887 EALALLrseLEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR 937
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
176-646 |
9.16e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.53 E-value: 9.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 176 DAVGELEQQLKraleELQEALAEKEELKQRCQEldmqvtaLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAKKyfhv 255
Cdd:PRK02224 206 ERLNGLESELA----ELDEEIERYEEQREQARE-------TRDEADEVLEEHEERREELETLEAEIEDLRETIAET---- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 256 qlqleqlqeenyrlEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRAT-SDKANKLESTVEVYRQK 334
Cdd:PRK02224 271 --------------EREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREElEDRDEELRDRLEECRVA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 335 LQDLND----LRKQVKSLQETNMMYMHNTVSLEEELKkanAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEK 410
Cdd:PRK02224 337 AQAHNEeaesLREDADDLEERAEELREEAAELESELE---EAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDF 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 411 HETLLKEKERLIEQRDTLKETNEELRCSKAQQDHLNQADSSATKSYENLAAEIMPV--EYREVFIRLQHENKMLRLQQEG 488
Cdd:PRK02224 414 LEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETieEDRERVEELEAELEDLEEEVEE 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 489 TEN--ERIEQLQEQLEQKHRKMNELET-EQRLS--KERIGELQQQIEDLQKSLQEqgsksegessskLKQKLEAHMEKLT 563
Cdd:PRK02224 494 VEErlERAEDLVEAEDRIERLEERREDlEELIAerRETIEEKRERAEELRERAAE------------LEAEAEEKREAAA 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 564 EVHEELQKKQELIEDLQPDISQNAQKISELEA----------------ALQKKDEDMKAMEERYKMYLEKARNVIKTLDP 627
Cdd:PRK02224 562 EAEEEAEEAREEVAELNSKLAELKERIESLERirtllaaiadaedeieRLREKREALAELNDERRERLAEKRERKRELEA 641
|
490
....*....|....*....
gi 1958776293 628 KLNPASAEIMLLRKQLAEK 646
Cdd:PRK02224 642 EFDEARIEEAREDKERAEE 660
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
174-656 |
9.89e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.53 E-value: 9.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 174 ASDA---VGELEQQLKRALEELQEALAEKEElkqrcQELDMQVTALQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAK 250
Cdd:PRK02224 171 ASDArlgVERVLSDQRGSLDQLKAQIEEKEE-----KDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 251 kyfHVQLQLEQLqeenyRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEEtraLKDEIDVLRATSDKANKLESTVEV 330
Cdd:PRK02224 246 ---HEERREELE-----TLEAEIEDLRETIAETEREREELAEEVRDLRERLEE---LEEERDDLLAEAGLDDADAEAVEA 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 331 YRQKLQD--------LNDLRKQVKSLQETNMMYMHNTVSLEEELKKA-----------NAARAQLETYKRQVQDLHTKLS 391
Cdd:PRK02224 315 RREELEDrdeelrdrLEECRVAAQAHNEEAESLREDADDLEERAEELreeaaeleselEEAREAVEDRREEIEELEEEIE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 392 SESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKETNEELRCSKAQQDHLNQADSSATKSYENLAAEIMPV--EYR 469
Cdd:PRK02224 395 ELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETieEDR 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 470 EVFIRLQHENKMLRLQQEGTEN--ERIEQLQEQLEQKHRKMNELET-EQRLS--KERIGELQQQIEDLQKSLQEqgskse 544
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVEErlERAEDLVEAEDRIERLEERREDlEELIAerRETIEEKRERAEELRERAAE------ 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 545 gessskLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDISQNAQ------KISELEAALQKKDEDMKAMEERYKMYLEKA 618
Cdd:PRK02224 549 ------LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKEriesleRIRTLLAAIADAEDEIERLREKREALAELN 622
|
490 500 510
....*....|....*....|....*....|....*...
gi 1958776293 619 RnviktldpklnpasaeimLLRKQLAEKDRRIEILESE 656
Cdd:PRK02224 623 D------------------ERRERLAEKRERKRELEAE 642
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
373-656 |
1.38e-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: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 373 RAQLETYKRQVQD--LHTKLSSESKRADTLAF---------EMKRLEEKHETLLKEKERLIEQRDTLKETNEELRcskAQ 441
Cdd:COG1196 199 ERQLEPLERQAEKaeRYRELKEELKELEAELLllklreleaELEELEAELEELEAELEELEAELAELEAELEELR---LE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 442 QDHLNQADSSATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGTENERIEQLQEQLEQkhrKMNELETEQRLSKER 521
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE---ELEELEEELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 522 IGELQQQIEDLQKSLQEQgSKSEGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQpdisQNAQKISELEAALQKKD 601
Cdd:COG1196 353 LEEAEAELAEAEEALLEA-EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE----ALLERLERLEEELEELE 427
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1958776293 602 EDMKAMEERykmyLEKARNVIKTLDPKLNPASAEIMLLRKQLAEKDRRIEILESE 656
Cdd:COG1196 428 EALAELEEE----EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
|
| HkD_Daple |
cd22228 |
Hook domain found in Daple (Dvl-associating protein with a high frequency of leucine residues) ... |
41-164 |
1.82e-11 |
|
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: 62.63 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 41 QLTNGVTMAQVLHQIDVAWFSEswlsRIKDDVGDNWRIKASNLKKVLHGITSYYHEFLGQQISEELiPDLNQIteSSDPV 120
Cdd:cd22228 29 DLVDGVFLNKIMLQIDPRPTNQ----RVNKHVNNDVNLRIQNLTILVRHIKTYYQEVLQQLIVMNL-PNVLMI--GKDPL 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1958776293 121 ------ELGRLLQLILGCAVNCEKKQEHIKNIMTLEESVQHVVMTAIQEL 164
Cdd:cd22228 102 sgksmeEIKKMLLLVLGCAVQCERKEEFIERIKQLDIETQAAIVSHIQEV 151
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
281-598 |
2.33e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 281 EELEKQLiefqhrnDELT---SLAEETRALKDEIDVLRA--TSDKANKLESTVEVYRQKLQDL-NDLRKQVKSLQETNMM 354
Cdd:COG1196 196 GELERQL-------EPLErqaEKAERYRELKEELKELEAelLLLKLRELEAELEELEAELEELeAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 355 YMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKETNEE 434
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 435 LrcsKAQQDHLNQADSSATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGTENERIEQLQEQLEQkhrKMNELETE 514
Cdd:COG1196 349 A---EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE---RLERLEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 515 QRLSKERIGELQQQIEDLQKSLQEQgskseGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDISQNAQKISELE 594
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEA-----AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
....
gi 1958776293 595 AALQ 598
Cdd:COG1196 498 EAEA 501
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
358-656 |
2.74e-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: 67.40 E-value: 2.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 358 NTVSLEEELKKAnaaRAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKETNEELRc 437
Cdd:TIGR02169 668 FSRSEPAELQRL---RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELE- 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 438 skAQQDHLNQAdssatksYENLAAEIMPVEyrevfirlqhenkmlrlqqegtenERIEQLQEQLEQKHRKMNELEteQRL 517
Cdd:TIGR02169 744 --EDLSSLEQE-------IENVKSELKELE------------------------ARIEELEEDLHKLEEALNDLE--ARL 788
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 518 SKERIGELQQQIEDLQKSLQEQGSKSEGessskLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDISQNAQKI------- 590
Cdd:TIGR02169 789 SHSRIPEIQAELSKLEEEVSRIEARLRE-----IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIenlngkk 863
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958776293 591 SELEAALQKKDEDMKAMEERY---KMYLEKARNVIKTLDPKLNPASAEIMLLRKQLAEKDRRIEILESE 656
Cdd:TIGR02169 864 EELEEELEELEAALRDLESRLgdlKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
268-609 |
9.23e-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: 9.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 268 RLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDV-LRATSDKANKLESTVEVYRQKLQDLNDLRKQV- 345
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqISALRKDLARLEAEVEQLEERIAQLSKELTELe 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 346 KSLQETNMMYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQR 425
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 426 DTLKETNEELRcskAQQDHLNQADSSATKSYENLAAEimpveyrevfirLQHEnkmlrLQQEGTENERIEQLQEQLEQKH 505
Cdd:TIGR02168 841 EDLEEQIEELS---EDIESLAAEIEELEELIEELESE------------LEAL-----LNERASLEEALALLRSELEELS 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 506 RKMNELETEQRLSKERIGELQQQIEDLQKSLQEqgsksegessskLKQKLEAHMEKLTEVHE-ELQKKQELIEDLQPDIS 584
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLEG------------LEVRIDNLQERLSEEYSlTLEEAEALENKIEDDEE 968
|
330 340
....*....|....*....|....*.
gi 1958776293 585 QNAQKISELEAALQKKDE-DMKAMEE 609
Cdd:TIGR02168 969 EARRRLKRLENKIKELGPvNLAAIEE 994
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
180-537 |
1.53e-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: 64.69 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 180 ELEQQLKRALEELQEALAEKEELKQRCQELDMQVTALQDEKNSLVSENEMMNEKLDQLDGsfddpntmvakkyfhvqlql 259
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK-------------------- 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 260 eqlqeenyRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANK-LESTVEVYRQKLQDL 338
Cdd:TIGR02168 755 --------ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAeLTLLNEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 339 NDLRKQVKSLQETNMMYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMK-RLEEKHETLLKE 417
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRsELEELSEELREL 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 418 KERLIEQRDTLKETNE-----ELRCSKAQQDHLNQADsSATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQE----G 488
Cdd:TIGR02168 907 ESKRSELRRELEELREklaqlELRLEGLEVRIDNLQE-RLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKikelG 985
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1958776293 489 TENER-IEQLQEQleqkhrkmneleteqrlsKERIGELQQQIEDLQKSLQ 537
Cdd:TIGR02168 986 PVNLAaIEEYEEL------------------KERYDFLTAQKEDLTEAKE 1017
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
314-645 |
2.78e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.92 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 314 LRATSDKANKLESTVEVYRQKLQDLNDLRKQVKSLqetnmmymhntvsLEEELKKANAARAQLETYKRQVQDLhtklsse 393
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKE-------------LEELSRQISALRKDLARLEAEVEQL------- 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 394 SKRADTLAFEMKRLEEKHETLLkekERLIEQRDTLKETNEELRCSKAQQDHLNQADSSATKSYENLAAEIMpvEYREVFI 473
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELE---ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT--LLNEEAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 474 RLQHENKMLRLQQEGTEnERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQGSKSegesssklkQ 553
Cdd:TIGR02168 821 NLRERLESLERRIAATE-RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL---------A 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 554 KLEAHMEKL-TEVHEELQKKQELIEDLQPDISQNAQKISELEAALQKKDEDMKAMEERYKMYLEKARNVIKTLDPKLNPA 632
Cdd:TIGR02168 891 LLRSELEELsEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEA 970
|
330
....*....|...
gi 1958776293 633 SAEIMLLRKQLAE 645
Cdd:TIGR02168 971 RRRLKRLENKIKE 983
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
137-669 |
6.58e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.77 E-value: 6.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 137 EKKQEHIKNIMTLEESVQHVVMTAIQELMSKEIVSSPASDAVGELEQQLKRALEELQEALAEKE---ELKQRCQELDMQV 213
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEeieELEKELESLEGSK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 214 TALQDEKNSLVSENEMMNEKLDQLDGSFDDPNTM--VAKKYFHVQLQLEQLQEENYRLEAAKDDYRVHCEELEKQLIEFQ 291
Cdd:PRK03918 255 RKLEEKIRELEERIEELKKEIEELEEKVKELKELkeKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 292 HRNDELTSLAEETRALKDEIDVLRatsdkanKLESTVEVYRQKLQDLNDLRKQVKSLQETNMMYMHNTVS-----LEEEL 366
Cdd:PRK03918 335 EKEERLEELKKKLKELEKRLEELE-------ERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEkakeeIEEEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 367 KKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRlEEKHETLLKEKERLIEQRDTLKETNEELRCSKAQQDHLN 446
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTE-EHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELE 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 447 QADSSATK--SYENLAAEIMPVEYR-EVFIRLQHENKMLRLQQEGTENERIEQLQEQLEQKHRKMNELETEQRLSKERIG 523
Cdd:PRK03918 487 KVLKKESEliKLKELAEQLKELEEKlKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLD 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 524 ELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHME--KLTEVHEELQKKQELIEDLQPDISQNAQKISELEAALQKKD 601
Cdd:PRK03918 567 ELEEELAELLKELEELGFESVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELR 646
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958776293 602 EDMKAMEERY-KMYLEKARNVIKTLDPKLNPASAEIMLLRKQLAEKDRRIEILESEckVAKFRDYEEKL 669
Cdd:PRK03918 647 KELEELEKKYsEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE--LEEREKAKKEL 713
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
295-621 |
7.08e-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: 62.78 E-value: 7.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 295 DELTSLAEETRALKDEIDVLRatsDKANKLESTVEVYRQKLQDLNdlrKQVKSLQEtnmmymhntvSLEEELKKANAARA 374
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQ---SELRRIENRLDELSQELSDAS---RKIGEIEK----------EIEQLEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 375 QLETYKRQVQDLHTKLSSESKRADTLAfemKRLEEKHETLLKEKERL--IEQRDT----------LKETNEELRCSKAQQ 442
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELE---ARIEELEEDLHKLEEALndLEARLShsripeiqaeLSKLEEEVSRIEARL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 443 DHLNQADSSATKSYENLAAEImpvEYREVFIRLQHENKMLRLQQEGTENERIEQLQEQLEQKHRKMNELETEQRLSKERI 522
Cdd:TIGR02169 815 REIEQKLNRLTLEKEYLEKEI---QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 523 GELQQQIEDLQKSLQEQGSK--SEGESSSKLKQKLEAHMEKLTE--------------------VHEELQKKQELIEDLQ 580
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQieKKRKRLSELKAKLEALEEELSEiedpkgedeeipeeelsledVQAELQRVEEEIRALE 971
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1958776293 581 P-------DISQNAQKISELEAALQKKDEDMKAMEERYKMYLEKARNV 621
Cdd:TIGR02169 972 PvnmlaiqEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
174-669 |
8.08e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 8.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 174 ASDAVGELEQQLKRALEELQEALAEKEELKQRCQELDMQVTALQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMvAKKYF 253
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL-KEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 254 HVQLQLEQLQEENYRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSL---AEETRALKDE----IDVLRATSDKANKLES 326
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELkekAEEYIKLSEFyeeyLDELREIEKRLSRLEE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 327 TVEVYRQKLQDLNDLRKQVKSLQETNMMYMHNTVSLEEELKKANAARAQLEtykrQVQDLHTKLSSES-----KRADTLA 401
Cdd:PRK03918 322 EINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE----ELERLKKRLTGLTpekleKELEELE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 402 FEMKRLEEKHETLLKEKERLIEQRDTLKETNEELRCSKAQ---------QDHLNQADSSATKSYENLAAEI--------- 463
Cdd:PRK03918 398 KAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgreltEEHRKELLEEYTAELKRIEKELkeieekerk 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 464 MPVEYREVFIRLQHENKMLRLQQEGtenERIEQLQEQLEQ-KHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEqgsk 542
Cdd:PRK03918 478 LRKELRELEKVLKKESELIKLKELA---EQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEK---- 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 543 segesSSKLKQKLEAHMEKLTEVHEELQK-KQELIEDLQPDISQNAQKISELEAALQKKDEDMKAMEErykmyLEKARNV 621
Cdd:PRK03918 551 -----LEELKKKLAELEKKLDELEEELAElLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKE-----LEREEKE 620
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1958776293 622 IKTLDPKLNPASAEIMLLRKQLAEKDRRIEILESECKVAKFRDYEEKL 669
Cdd:PRK03918 621 LKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEY 668
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
408-656 |
8.56e-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: 8.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 408 EEKHETLLKekerLIEQRDTLKETNEELRCSKAQQDHLnQADSSATKSYENLAAEIMPVEYREVFIRL-QHENKMLRLQQ 486
Cdd:TIGR02168 172 ERRKETERK----LERTRENLDRLEDILNELERQLKSL-ERQAEKAERYKELKAELRELELALLVLRLeELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 487 EGTENER--------IEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQGSKSEGessskLKQKLEAH 558
Cdd:TIGR02168 247 ELKEAEEeleeltaeLQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN-----LERQLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 559 MEKLTEVHEELQKKQELIEDLQPDISQNAQKISELEAALQKKDEDMKAMEERykmylekarnvIKTLDPKLNPASAEIML 638
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR-----------LEELEEQLETLRSKVAQ 390
|
250
....*....|....*...
gi 1958776293 639 LRKQLAEKDRRIEILESE 656
Cdd:TIGR02168 391 LELQIASLNNEIERLEAR 408
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
415-668 |
8.91e-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: 8.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 415 LKEKERLIEQRDTLKETNEELRCSKAQQDHLNQADSSATKSYENLAAEIMpveyrevfiRLQHENKMLrLQQEGTENERI 494
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIG---------EIEKEIEQL-EQEEEKLKERL 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 495 EQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQGSKSEGESSsklkQKLEAHMEKLTEVHEELQKKQE 574
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI----PEIQAELSKLEEEVSRIEARLR 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 575 LIE----DLQPDISQNAQKISELE----------AALQKKDEDMKAMEERYKMYLEKARNVIKTLDPKLNPASAEIMLLR 640
Cdd:TIGR02169 816 EIEqklnRLTLEKEYLEKEIQELQeqridlkeqiKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE 895
|
250 260
....*....|....*....|....*...
gi 1958776293 641 KQLAEKDRRIEILESECKVAKFRDYEEK 668
Cdd:TIGR02169 896 AQLRELERKIEELEAQIEKKRKRLSELK 923
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
183-625 |
1.14e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.98 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 183 QQLKRALEELQEALA----EKEELKQRCQELDMQVTALQDEKNSLVSENEMMNEKLDQLDGSFDDpntmVAKKYFHVQLQ 258
Cdd:PRK02224 254 ETLEAEIEDLRETIAeterEREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREE----LEDRDEELRDR 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 259 LEQLQEENYRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETR-----------ALKDEIDVLRATSDKANKLEST 327
Cdd:PRK02224 330 LEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAReavedrreeieELEEEIEELRERFGDAPVDLGN 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 328 VEVYRQKLQ-DLNDLRKQVKSLqETNMMYMHNTVSLEEELKKA----------------------NAARAQLETYKRQVQ 384
Cdd:PRK02224 410 AEDFLEELReERDELREREAEL-EATLRTARERVEEAEALLEAgkcpecgqpvegsphvetieedRERVEELEAELEDLE 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 385 DLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKETNEELRCSKAQQDHLN----QADSSATKSYENLA 460
Cdd:PRK02224 489 EEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEaeaeEKREAAAEAEEEAE 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 461 AEIMPV-----EYREVFIRLQHENKMLRLQQEGTENE-RIEQLQEQLEQKhrkmNELETEQRlskERIGELQQQIEDLQK 534
Cdd:PRK02224 569 EAREEVaelnsKLAELKERIESLERIRTLLAAIADAEdEIERLREKREAL----AELNDERR---ERLAEKRERKRELEA 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 535 SLQEqgsksegESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDISQNAQKISELEAAlqkkDEDMKAMEERyKMY 614
Cdd:PRK02224 642 EFDE-------ARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEEL----RERREALENR-VEA 709
|
490
....*....|.
gi 1958776293 615 LEKARNVIKTL 625
Cdd:PRK02224 710 LEALYDEAEEL 720
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
368-669 |
1.38e-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: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 368 KANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLE-------EKHET----LLKEKERLIEQRDT----LKETN 432
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAEryqallkEKREYegyeLLKEKEALERQKEAierqLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 433 EELRCSKAQQDHLNQADSSATKSYENLAAEIMPVEyrevfirlqhENKMLRLQQEGTENE-RIEQLQEQLEQKHRKMNEL 511
Cdd:TIGR02169 251 EELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG----------EEEQLRVKEKIGELEaEIASLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 512 ETEQRLSKERIGELQQQIEDLQKSLQEQGSKSE--GESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDISQNAQK 589
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDklTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 590 ISELEAALQKKDEDMKAMEERykmyLEKARNVIKTLDPKLNPASAEIMLLRKQLAEKDRRIEILeseckVAKFRDYEEKL 669
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEE----LADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL-----AADLSKYEQEL 471
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
419-655 |
1.39e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.85 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 419 ERLIEQRDTLKETNEELRCSKAQQDHLNQADSSATKsYENLAAEIMPVEYREVFIRLQHENKMLRLQQEgteneRIEQLQ 498
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLEPIRELAER-YAAARERLAELEYLRAALRLWFAQRRLELLEA-----ELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 499 EQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQ-KSLQEqgsksegessskLKQKLEAHMEKLTEVHEELQKKQELIE 577
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQ------------LEREIERLERELEERERRRARLEALLA 369
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958776293 578 DLQPDISQNAQKISELEAALQKKDEDMKAMEERykmylekarnviktLDPKLNPASAEIMLLRKQLAEKDRRIEILES 655
Cdd:COG4913 370 ALGLPLPASAEEFAALRAEAAALLEALEEELEA--------------LEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
284-598 |
2.26e-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: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 284 EKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKAN-KLESTVEVYRQKLQDLNDLRKQVKSLQETNMMYMHNTV-S 361
Cdd:TIGR02169 219 EKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTeEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIgE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 362 LEEELKKAnaaRAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKETNEELRCSKAQ 441
Cdd:TIGR02169 299 LEAEIASL---ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 442 QDHLNQADSSATKSYenlaaeimpveyREVFIRLQHENKMLRLQQEgtenerieQLQEQLEQKHRKMNELETEQRLSKER 521
Cdd:TIGR02169 376 VDKEFAETRDELKDY------------REKLEKLKREINELKRELD--------RLQEELQRLSEELADLNAAIAGIEAK 435
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958776293 522 IGELQQQIEDLQKSLQEQgsksegesssklKQKLEAHMEKLTEVHEELQKKQELIEDLQPDISQNAQKISELEAALQ 598
Cdd:TIGR02169 436 INELEEEKEDKALEIKKQ------------EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAR 500
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
180-667 |
2.60e-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: 2.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 180 ELEQQLKRALEELQEALAEKEELKQRCQELDMQVTALQDEKNSLVSENEMMNEKLDqldgsfddpntmvakkyfHVQLQL 259
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA------------------RLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 260 EQLQEENYRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEID--VLRATSDKANKLESTVEVYRQKLQD 337
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEeaLLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 338 LNDLRKQVKSLQETNMMYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKE 417
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 418 KERLIEQRDTLKETNEELRCSK-AQQDHLNQADSSATKSYENLAAEIMPVEYREVFIRLQHENK---------MLRLQQE 487
Cdd:COG1196 472 AALLEAALAELLEELAEAAARLlLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAyeaaleaalAAALQNI 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 488 GTENERIEQLQEQLEQKHRK----------------MNELETEQRLSKERIGELQQQIEDLQKSLQEQGSKSEGESSSKL 551
Cdd:COG1196 552 VVEDDEVAAAAIEYLKAAKAgratflpldkiraraaLAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAR 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 552 KQKLEAHMEKLTEVHEELQKKQELIEDLQPDISQNAQKISELEAALQKKDEDMKAMEERYKMYLEKARNVIKTLDPKLNP 631
Cdd:COG1196 632 LEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711
|
490 500 510
....*....|....*....|....*....|....*.
gi 1958776293 632 ASAEIMLLRKQLAEKDRRIEILESECKVAKFRDYEE 667
Cdd:COG1196 712 AEEERLEEELEEEALEEQLEAEREELLEELLEEEEL 747
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
268-597 |
3.06e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 268 RLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATsdkanklestvevYRQKLQDLNDLRKQVKS 347
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE-------------EYELLAELARLEQDIAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 348 LQETNmmyMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAfemKRLEEKHETLLKEKERLIEQRDT 427
Cdd:COG1196 307 LEERR---RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE---AELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 428 LKETNEELRCSKAQQDHLNQADSSATKSYENLAAEImpveyrevfIRLQHENKMLRLQQEGTENERIEQLQEQLEQKHRK 507
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERL---------ERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 508 MNELETEQRLSKERIGELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEELQKKQELiEDLQPDISQNA 587
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL-RGLAGAVAVLI 530
|
330
....*....|
gi 1958776293 588 QKISELEAAL 597
Cdd:COG1196 531 GVEAAYEAAL 540
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
268-667 |
7.85e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.38 E-value: 7.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 268 RLEAAKDDYRVHCEELEKQLIEfQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEVYRQKLQDLNDLRKQVKS 347
Cdd:PTZ00121 1225 KAEAVKKAEEAKKDAEEAKKAE-EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKK 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 348 LQETNMMyMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDT 427
Cdd:PTZ00121 1304 ADEAKKK-AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA 1382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 428 LKETNEELRCS----------KAQQDHLNQADSSATKSYE--NLAAEIMPVEyrEVFIRLQHENKMLRLQQEGTENERIE 495
Cdd:PTZ00121 1383 AKKKAEEKKKAdeakkkaeedKKKADELKKAAAAKKKADEakKKAEEKKKAD--EAKKKAEEAKKADEAKKKAEEAKKAE 1460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 496 QLQEQLEQKhRKMNELETEQRlSKERIGELQQQIEDLQKSLQE-QGSKSEGESSSKLKQKLEAHMEKLTEVHEELQKKQE 574
Cdd:PTZ00121 1461 EAKKKAEEA-KKADEAKKKAE-EAKKADEAKKKAEEAKKKADEaKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADE 1538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 575 LIEDLQPDISQNAQKISELEAALQ-KKDEDMKAMEERYKMYLEKARNVIKTLDPKLNPASAEIMLLRKQLAEKDRRIEil 653
Cdd:PTZ00121 1539 AKKAEEKKKADELKKAEELKKAEEkKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE-- 1616
|
410
....*....|....
gi 1958776293 654 ESECKVAKFRDYEE 667
Cdd:PTZ00121 1617 EAKIKAEELKKAEE 1630
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
135-661 |
9.89e-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: 9.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 135 NCEKKQEHIKNIMTLEESVQHVVMTAIQELMSKEIVSSPASDAV----GELEQQLKRALEELQEALAEKEELKQRCQELD 210
Cdd:TIGR02168 299 RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELeeklEELKEELESLEAELEELEAELEELESRLEELE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 211 MQVTALQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAKkyfhvqLQLEQLQEENYRLEAAKDDYRVHCEELEKQLIEF 290
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER------LQQEIEELLKKLEEAELKELQAELEELEEELEEL 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 291 QHRND----ELTSLAEETRALKDEIDVLRATSDKANKLESTVEVYRQKLQDLNDLRKQVKSLQETNMMYMH---NTVSLE 363
Cdd:TIGR02168 453 QEELErleeALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGvlsELISVD 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 364 EELKKA-----------------NAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRD 426
Cdd:TIGR02168 533 EGYEAAieaalggrlqavvvenlNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDP 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 427 TLKETNEELRCSKAQQDHLNQADSSATKSYEN-----LAAEIMPVEYREVFIRLQHENKMLRLQQEGTENER-IEQLQEQ 500
Cdd:TIGR02168 613 KLRKALSYLLGGVLVVDDLDNALELAKKLRPGyrivtLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEkIEELEEK 692
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 501 LEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQgskseGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQ 580
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISAL-----RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 581 PDISQNAQKISELEAALQKKDEDMKAMEERYKMY---LEKARNVIKTLDPKLNPASAEIMLLRKQLAEKDRRIEILESEC 657
Cdd:TIGR02168 768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847
|
....
gi 1958776293 658 KVAK 661
Cdd:TIGR02168 848 EELS 851
|
|
| HkD_Gipie |
cd22230 |
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar ... |
41-164 |
1.21e-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: 54.84 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 41 QLTNGVTMAQVLHQIDVAwfSESWLSRIKDDVGDNWRIKasNLKKVLHGITSYYHEFLGQQIseeLIPDLNQITESSDPV 120
Cdd:cd22230 46 RLSNGDLLNRVMGIIDPS--PRGGPRMRGDDGPAAHRVQ--NLHILWGRLRDFYQEELQQLI---LSPPPDLQVMGRDPF 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1958776293 121 ------ELGRLLQLILGCAVNCEKKQEHIKNIMTLEESVQHVVMTAIQEL 164
Cdd:cd22230 119 teeavqELEKLLRLLLGAAVQCERRELFIRHIQGLDLDVQAELAEAIQEV 168
|
|
| HkD_Girdin |
cd22229 |
Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation ... |
32-164 |
1.51e-08 |
|
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: 54.41 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 32 TASPCQDVKQLTNGVTMAQVLHQIDvawfSESWLSRIKDDVGDNWRIKASNLKKVLHGITSYYHEFLGQQISEELiPDL- 110
Cdd:cd22229 23 NGTPLDEYVALVDGVFLNEVMLQIN----PKSSNQRVNKKVNNDASLRIQNLSILVKQIKLYYQETLQQLIMMSL-PNVl 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958776293 111 ----NQITESSDPvELGRLLQLILGCAVNCEKKQEHIKNIMTLEESVQHVVMTAIQEL 164
Cdd:cd22229 98 vlgrNPLSEQGTE-EMKKLLLLLLGCAVQCERKEEFIERIQTLDFDTKAAVAAHIQEV 154
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
183-530 |
2.59e-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: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 183 QQLKRALEELQEALA--EKEELKQRCQELDMQVTALQDEKNSLVSENEMMNEKLDQLDGSFddpntmvakkyfhvqlqle 260
Cdd:TIGR02168 216 KELKAELRELELALLvlRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEV------------------- 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 261 qlqeenyrleaakddyrvhcEELEKQLIEFQHRNDELTSLAEEtraLKDEIDVLRATSDKANKLESTVEVYRQKL-QDLN 339
Cdd:TIGR02168 277 --------------------SELEEEIEELQKELYALANEISR---LEQQKQILRERLANLERQLEELEAQLEELeSKLD 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 340 DLRKQVKSLQETNMMYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSE----SKRADTLAFEMKRLEEKHETLL 415
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKvaqlELQIASLNNEIERLEARLERLE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 416 KEKERLIEQRDTLKETNEELRCSKAQQ--DHLNQADSSATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGTENER 493
Cdd:TIGR02168 414 DRRERLQQEIEELLKKLEEAELKELQAelEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
|
330 340 350
....*....|....*....|....*....|....*..
gi 1958776293 494 IEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIE 530
Cdd:TIGR02168 494 LERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIS 530
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
485-670 |
4.10e-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: 55.93 E-value: 4.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 485 QQEGTENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQGSKSEGESSSKLK------------ 552
Cdd:COG4942 48 KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRlgrqpplallls 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 553 -----------QKLEAHMEKLTEVHEELQKKQELIEDLQPDISQNAQKISELEAALQKKDEDMKAMEERYKMYLEKARNV 621
Cdd:COG4942 128 pedfldavrrlQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958776293 622 IKTLDPKLNPASAEIMLLRKQLAEKDRRIEILESECKVAKFRDYEEKLI 670
Cdd:COG4942 208 LAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
174-667 |
5.79e-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: 56.27 E-value: 5.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 174 ASDAVGELEQQLKRALEELQEALAEKEELKQRCQELDMQVTALQDEKNSLVSENEMMNEKLDQL----DGSFDDPNTMVA 249
Cdd:pfam05483 266 SRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLteekEAQMEELNKAKA 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 250 KKYFHVQLQLEQLQEENYRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVE 329
Cdd:pfam05483 346 AHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKK 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 330 VYRQKLQDLNDLRKQVKSLQETNMMYMHNtvsLEEELkkaNAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLee 409
Cdd:pfam05483 426 QFEKIAEELKGKEQELIFLLQAREKEIHD---LEIQL---TAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKL-- 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 410 khetllkekerLIEQRDTLKETNEELRCSKAQQDHLNqadsSATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGT 489
Cdd:pfam05483 498 -----------LLENKELTQEASDMTLELKKHQEDII----NCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGD 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 490 ENE-RIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEqgsksegessskLKQKLEAHMEKLTEVHEE 568
Cdd:pfam05483 563 EVKcKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEE------------LHQENKALKKKGSAENKQ 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 569 LQKKQELIEDLQPDISQNAQKISELEAALQKKDEDMKAMEERYKMYLEKARNVI-------KTLDPKLNPASAEIM-LLR 640
Cdd:pfam05483 631 LNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIAdeavklqKEIDKRCQHKIAEMVaLME 710
|
490 500
....*....|....*....|....*..
gi 1958776293 641 KQLAEKDRRIEILESECKVAKFRDYEE 667
Cdd:pfam05483 711 KHKHQYDKIIEERDSELGLYKNKEQEQ 737
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
174-645 |
7.09e-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: 7.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 174 ASDAVGELEQQLKRALEELQEALAEKEELKQRCQELDMQVTALQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAKKYF 253
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 254 HVQLQLEQLQEENYRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANK-LESTVEVYR 332
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEaLEEAAEEEA 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 333 QKLQDLNDLRKQVKSLQETNMMYMHNTVSLEEELKKANAARAQLETYKRQVQD-----LHTKLSSESKRADTLAFEMKRL 407
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGflegvKAALLLAGLRGLAGAVAVLIGV 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 408 EEKHETLLKEKERLIEQRDTLKETNEELRCSKAQQDH---------LNQADSSATKSYENLAAEIMPVEYREVFIRLQHE 478
Cdd:COG1196 533 EAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAkagratflpLDKIRARAALAAALARGAIGAAVDLVASDLREAD 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 479 NKMLRLQQEGTENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAH 558
Cdd:COG1196 613 ARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE 692
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 559 MEKLTEVHEELQKKQELIEDLQPDISQNAQKISELEAALQKKDEDMKAMEERYKMYLEKARnVIKTLDPKLNPASAEIML 638
Cdd:COG1196 693 LELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEAL-EELPEPPDLEELERELER 771
|
....*..
gi 1958776293 639 LRKQLAE 645
Cdd:COG1196 772 LEREIEA 778
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
186-619 |
8.98e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 8.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 186 KRALEEL----QEALAEKEELKQRCQELDMQVTALQDEKNSLVSENEMMNEKLDQldgsfDDPNTMVAKKYFHVQLQLEQ 261
Cdd:PTZ00121 1314 AKKADEAkkkaEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEA-----AEKKKEEAKKKADAAKKKAE 1388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 262 LQEENYRLEAAKDDYRVHCEELEKQLIEfQHRNDELTSLAEETRAlKDEIDVLRATSDKANKLESTVEVYRqKLQDLNDL 341
Cdd:PTZ00121 1389 EKKKADEAKKKAEEDKKKADELKKAAAA-KKKADEAKKKAEEKKK-ADEAKKKAEEAKKADEAKKKAEEAK-KAEEAKKK 1465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 342 RKQVKSLQETNmmymhntvSLEEELKKANAARAQLETYKRQVQDLHtKLSSESKRADTL--------AFEMKRLEEKHET 413
Cdd:PTZ00121 1466 AEEAKKADEAK--------KKAEEAKKADEAKKKAEEAKKKADEAK-KAAEAKKKADEAkkaeeakkADEAKKAEEAKKA 1536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 414 LLKEKERLIEQRDTLKETnEELRCS----KAQQDHLNQADSSATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGT 489
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKA-EELKKAeekkKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 490 ENERI--EQLQEQLEQKHRkmneleTEQRLSKERigELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAhmEKLTEVHE 567
Cdd:PTZ00121 1616 EEAKIkaEELKKAEEEKKK------VEQLKKKEA--EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA--EEAKKAEE 1685
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1958776293 568 ELQKKQELIEDlQPDISQNAQKISELEAALQKKDEDMKAMEERYKMYLEKAR 619
Cdd:PTZ00121 1686 DEKKAAEALKK-EAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAK 1736
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
267-669 |
1.78e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 267 YRLEAAKDDYRVHCEELEKQLIEFQHRNDELT------SLAEETRALKDEIDVLratSDKANKLESTVEVYRQKLQDLND 340
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEkllqllPLYQELEALEAELAEL---PERLEELEERLEELRELEEELEE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 341 LRKQVKSLQEtnmmymhntvSLEEELKK-ANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKE 419
Cdd:COG4717 168 LEAELAELQE----------ELEELLEQlSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 420 RLiEQRDTLKETNEELRCSKAQQDHLNQADSSATKSYE--NLAAEIMPVEYREVFIRLQHENKMLRLQQEGTENERIEQL 497
Cdd:COG4717 238 AA-ALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiaGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 498 QEQLEQKHRKmnELETEQRLSKERIGELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKL-TEVHEELQKKQELI 576
Cdd:COG4717 317 EEEELEELLA--ALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAgVEDEEELRAALEQA 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 577 EDLQpdisQNAQKISELEAALQKKDEDMKAMEERYKmyLEKARNVIKTLDPKLNPASAEIMLLRKQLAEKDRRIEILESE 656
Cdd:COG4717 395 EEYQ----ELKEELEELEEQLEELLGELEELLEALD--EEELEEELEELEEELEELEEELEELREELAELEAELEQLEED 468
|
410
....*....|...
gi 1958776293 657 CKVAKFRDYEEKL 669
Cdd:COG4717 469 GELAELLQELEEL 481
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
270-668 |
2.75e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 270 EAAKDDYRVHCEELEKQlIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEVYRqKLQDLNDLRKQVKSLQ 349
Cdd:PTZ00121 1370 EKKKEEAKKKADAAKKK-AEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK-KADEAKKKAEEAKKAD 1447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 350 ETNmmymhntvSLEEELKKANAARAQLETyKRQVQDLHTKlSSESKRADTLAFEMKRLEEKHETLlKEKERLIEQRDTLK 429
Cdd:PTZ00121 1448 EAK--------KKAEEAKKAEEAKKKAEE-AKKADEAKKK-AEEAKKADEAKKKAEEAKKKADEA-KKAAEAKKKADEAK 1516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 430 ETNEELRCSKAQQDHLNQADSSATKSYENLAAEimpveyrevfirlqhENKMLRLQQEGTENERIEQLQEQLEQKHRKMN 509
Cdd:PTZ00121 1517 KAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD---------------ELKKAEELKKAEEKKKAEEAKKAEEDKNMALR 1581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 510 ELETEQRLSKERIGELQQ--------QIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTE---VHEELQKKQELIED 578
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKlyeeekkmKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEekkKAEELKKAEEENKI 1661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 579 LQPDISQNAQKISELEAALQKKDEDMKAMEERYKMYLEKARNVIKtldpklnpasaeimlLRKQLAEKDRRIEILESECK 658
Cdd:PTZ00121 1662 KAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE---------------LKKKEAEEKKKAEELKKAEE 1726
|
410
....*....|
gi 1958776293 659 VAKFRDYEEK 668
Cdd:PTZ00121 1727 ENKIKAEEAK 1736
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
180-614 |
4.04e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 180 ELEQQLKRALEELQEALAEKEELKQRCQELDMqVTALQDEKNSLvsENEMMNEKLDQLDGSFDDpntmVAKKYFHVQLQL 259
Cdd:PRK03918 335 EKEERLEELKKKLKELEKRLEELEERHELYEE-AKAKKEELERL--KKRLTGLTPEKLEKELEE----LEKAKEEIEEEI 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 260 EQLQEENYRLEAAKDDYRVHCEELEK---------QLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEV 330
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKKakgkcpvcgRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEK 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 331 YRQKLQDLNDLRKQVKSLQEtnmmymhntvsLEEELKKANAAraQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEk 410
Cdd:PRK03918 488 VLKKESELIKLKELAEQLKE-----------LEEKLKKYNLE--ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE- 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 411 hetLLKEKERLIEQRDTLKETNEELrcskaqqdhLNQADSSATKSYENLAAEIMPVE--YREvFIRLQHENKMLRlqqeg 488
Cdd:PRK03918 554 ---LKKKLAELEKKLDELEEELAEL---------LKELEELGFESVEELEERLKELEpfYNE-YLELKDAEKELE----- 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 489 TENERIEQLQEQLEQKHRKMNELETeqrlskeRIGELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEE 568
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETEK-------RLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKR 688
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1958776293 569 LQKKQELIEDLQPDISQNAQKISELEaALQKKDEDMKAMEERYKMY 614
Cdd:PRK03918 689 REEIKKTLEKLKEELEEREKAKKELE-KLEKALERVEELREKVKKY 733
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
137-626 |
2.38e-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: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 137 EKKQEHIKNIMTLEESVQHVVMTAIQELMSKEIvsspASDAVGELEQQLKRALEELQEALAEKEELKQRCQELDMQVTAL 216
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEE----LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 217 QDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAKKYFHVQLQLEQLQEENYRLEAAKDDYRVHCEELEKQLIEFQHRNDE 296
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 297 LTSLAEETRALKDEIDVLRATS-DKANKLESTVEVYRQKLQDLNDLRKQVKSLQETNMMYMHNTVSLEEELKKAN----- 370
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLaELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGlrgla 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 371 ---------------------AARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLK 429
Cdd:COG1196 524 gavavligveaayeaaleaalAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDL 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 430 ETNEELRCSKAQQDHLNQA--DSSATKSYENLAAEIMPVEYREVFIRL----QHENKMLRLQQEGTENERIEQLQEQLEQ 503
Cdd:COG1196 604 VASDLREADARYYVLGDTLlgRTLVAARLEAALRRAVTLAGRLREVTLegegGSAGGSLTGGSRRELLAALLEAEAELEE 683
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 504 KHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEvHEELQKKQELIEDLQPDI 583
Cdd:COG1196 684 LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE-EELLEEEALEELPEPPDL 762
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 584 SQNAQKISELEAALQKK-------DEDMKAMEERYKMY------LEKARN----VIKTLD 626
Cdd:COG1196 763 EELERELERLEREIEALgpvnllaIEEYEELEERYDFLseqredLEEAREtleeAIEEID 822
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
408-600 |
2.77e-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: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 408 EEKHETLLKEKERLIEQRDTLKETNEELRcskAQQDHLNQADSSatksYENLAaeimpvEYREVFIRL-QHENKMLRLQQ 486
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALE---AELDALQERREA----LQRLA------EYSWDEIDVaSAEREIAELEA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 487 EGTE----NERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQ---KSLQEQGSKSEGESSSKLKQKLEAHm 559
Cdd:COG4913 676 ELERldasSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEeelDELQDRLEAAEDLARLELRALLEER- 754
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958776293 560 eklteVHEELQKK--QELIEDLQPDISQNAQKISELEAALQKK 600
Cdd:COG4913 755 -----FAAALGDAveRELRENLEERIDALRARLNRAEEELERA 792
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
297-674 |
4.03e-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: 50.49 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 297 LTSLAEETRALKDEIDVLRATSDKANKLESTVEVYRQKLQDLNDLRKQVKSLQETNMMYMHNTVS----LEEELKKANAA 372
Cdd:pfam05483 246 LIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMStqkaLEEDLQIATKT 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 373 RAQL-ETYKRQVQDLHTKLSSESKRADTLAFEMKRLEekhETLLKEKERLIEQRDTLKETNEELRCSKAQQDHLNQADSS 451
Cdd:pfam05483 326 ICQLtEEKEAQMEELNKAKAAHSFVVTEFEATTCSLE---ELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNN 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 452 ATKSYENLAAEIMPVEyrevfiRLQHENKMLRLQQE---GTENERIEQLQeqleQKHRKMNELETEQRLSKERIGELQQQ 528
Cdd:pfam05483 403 KEVELEELKKILAEDE------KLLDEKKQFEKIAEelkGKEQELIFLLQ----AREKEIHDLEIQLTAIKTSEEHYLKE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 529 IEDLQKSLQEQGSKSEGESSSKLKQKLEAH--MEKLTEVHEELQKKQELI-------EDLQPDISQNAQKISELEAALQK 599
Cdd:pfam05483 473 VEDLKTELEKEKLKNIELTAHCDKLLLENKelTQEASDMTLELKKHQEDIinckkqeERMLKQIENLEEKEMNLRDELES 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 600 KDEDMKAMEERYKMYLEKARNVIKTLDPKLNPASAEIML-------LRKQLAEKDRRIEILESECKVAKFRDYEEKLIVS 672
Cdd:pfam05483 553 VREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKIlenkcnnLKKQIENKNKNIEELHQENKALKKKGSAENKQLN 632
|
..
gi 1958776293 673 AW 674
Cdd:pfam05483 633 AY 634
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
362-609 |
7.06e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 7.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 362 LEEELKKANAARAQLETYKRQVQ----------------DLHTKLSS-ESKRADTLAfEMKRLEEKHETLLKEKERLIEQ 424
Cdd:PRK02224 164 LEEYRERASDARLGVERVLSDQRgsldqlkaqieekeekDLHERLNGlESELAELDE-EIERYEEQREQARETRDEADEV 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 425 RDTLKETNEELRCSKAQQDHLNQADSSATKSYENLAAEIMpvEYREVFIRLQHENKMLR--LQQEGTENERIEQLQEQLE 502
Cdd:PRK02224 243 LEEHEERREELETLEAEIEDLRETIAETEREREELAEEVR--DLRERLEELEEERDDLLaeAGLDDADAEAVEARREELE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 503 QKHRKMNELETEQRLS------------------KERIGELQQQIEDLQKSLQ--EQGSKSEGESSSKLKQKLEAHMEKL 562
Cdd:PRK02224 321 DRDEELRDRLEECRVAaqahneeaeslredaddlEERAEELREEAAELESELEeaREAVEDRREEIEELEEEIEELRERF 400
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1958776293 563 TEVHEELQKKQELIEDLQPDISQNAQKISELEAALQKKDEDMKAMEE 609
Cdd:PRK02224 401 GDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA 447
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
481-581 |
8.67e-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: 8.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 481 MLRLQQEGTENErIEQLQEQLEQKHRKMNELETEQRL-SKERIGELQQQIEDLQKSLQE-----QGSKSEGESSSKLKQK 554
Cdd:COG0542 401 RVRMEIDSKPEE-LDELERRLEQLEIEKEALKKEQDEaSFERLAELRDELAELEEELEAlkarwEAEKELIEEIQELKEE 479
|
90 100
....*....|....*....|....*..
gi 1958776293 555 LEAHMEKLTEVHEELQKKQELIEDLQP 581
Cdd:COG0542 480 LEQRYGKIPELEKELAELEEELAELAP 506
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
373-625 |
1.09e-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: 48.97 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 373 RAQLETYKRQVqdlhtklssESKRADTLAFEMKRLEEKhETLLKEKERlieQRDTLKETNEELRCSKAQQDHLNQADSSA 452
Cdd:pfam17380 352 RIRQEERKREL---------ERIRQEEIAMEISRMREL-ERLQMERQQ---KNERVRQELEAARKVKILEEERQRKIQQQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 453 TKSYENLAAEIMPVEYREV-FIRLQHENKMLRLQQEGTENE-RIEQLQEQLEQKHRKMNELETEQRlSKERIGELQQQIe 530
Cdd:pfam17380 419 KVEMEQIRAEQEEARQREVrRLEEERAREMERVRLEEQERQqQVERLRQQEEERKRKKLELEKEKR-DRKRAEEQRRKI- 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 531 dLQKSLQEQgsksegesssklKQKLEAHMEKLTEVHEELQKKQELI--EDLQPDISQNAQKISELEAALQKKDEDMKAME 608
Cdd:pfam17380 497 -LEKELEER------------KQAMIEEERKRKLLEKEMEERQKAIyeEERRREAEEERRKQQEMEERRRIQEQMRKATE 563
|
250
....*....|....*...
gi 1958776293 609 ERYKM-YLEKARNVIKTL 625
Cdd:pfam17380 564 ERSRLeAMEREREMMRQI 581
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
332-589 |
1.12e-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: 48.22 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 332 RQKLQDLNDLRKQVKSLQETnmmymhntvsLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKH 411
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKE----------LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 412 ETLlkeKERLIEQRDTLKEtneelRCSKAQQDHLNQADSSATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEgten 491
Cdd:COG4942 93 AEL---RAELEAQKEELAE-----LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA---- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 492 eRIEQLQEQLEQKHRKMNELETEQrlsKERIGELQQQIEDLQKSLQEqgsksegessskLKQKLEAHMEKLTEVHEELQK 571
Cdd:COG4942 161 -ELAALRAELEAERAELEALLAEL---EEERAALEALKAERQKLLAR------------LEKELAELAAELAELQQEAEE 224
|
250
....*....|....*...
gi 1958776293 572 KQELIEDLQPDISQNAQK 589
Cdd:COG4942 225 LEALIARLEAEAAAAAER 242
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
387-668 |
1.30e-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: 48.58 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 387 HTKLSSESKRADTLA-FEMKRLEEKHETLLKEKERlieqRDTLKETneelrcSKAQQDHLNQaDSSATKSYENLAAEimp 465
Cdd:pfam17380 280 HQKAVSERQQQEKFEkMEQERLRQEKEEKAREVER----RRKLEEA------EKARQAEMDR-QAAIYAEQERMAME--- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 466 veyrevfirlqHENKMLRLQQE--GTENERIEQLQEQLE-QKHRKMNELETEQRLSKERIG---ELQQQIEDLQKSLQEQ 539
Cdd:pfam17380 346 -----------RERELERIRQEerKRELERIRQEEIAMEiSRMRELERLQMERQQKNERVRqelEAARKVKILEEERQRK 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 540 GSKSEGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDISQNAQKISELEAALQKKDEDMKAMEERYKMYLEKAR 619
Cdd:pfam17380 415 IQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRR 494
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1958776293 620 NVIKTldpklnpasaEIMLLRKQLAEKDRRIEILESECKVAKFRDYEEK 668
Cdd:pfam17380 495 KILEK----------ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEE 533
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
278-538 |
1.60e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 48.39 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 278 VHCEELEKQLIEFQHRndELTSLAEEtraLKDEIDVLRATSDKANKLESTVEVYrqKLQDLNDLRKQVKSlqetnmmymh 357
Cdd:PRK05771 31 VHIEDLKEELSNERLR--KLRSLLTK---LSEALDKLRSYLPKLNPLREEKKKV--SVKSLEELIKDVEE---------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 358 NTVSLEEELKKANAARAQLETYKRqvqdlhtKLSSESKRADTL-AFEmkrLEEKhetLLKEKERLIEQRDTLKETNEELr 436
Cdd:PRK05771 94 ELEKIEKEIKELEEEISELENEIK-------ELEQEIERLEPWgNFD---LDLS---LLLGFKYVSVFVGTVPEDKLEE- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 437 cSKAQQDHLNQADSSATKSYENLAAeIMPVEYREVFIRL--QHENKMLRLQQEGTENERIEQLQEQLEQKHRKMNELete 514
Cdd:PRK05771 160 -LKLESDVENVEYISTDKGYVYVVV-VVLKELSDEVEEElkKLGFERLELEEEGTPSELIREIKEELEEIEKERESL--- 234
|
250 260
....*....|....*....|....
gi 1958776293 515 qrlsKERIGELQQQIEDLQKSLQE 538
Cdd:PRK05771 235 ----LEELKELAKKYLEELLALYE 254
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
187-623 |
1.64e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 187 RALEELQEALAEKEELKQRCQELDMQVTALQDEKNSLVSENEMMNEKLDQLDgsfddpntmvakkyfhvqlqleqLQEEN 266
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE-----------------------KLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 267 YRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTvevyrQKLQDLNDLRKQVK 346
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSL-----ATEEELQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 347 SLQETNMMYMHNTVSLEEELKKANAARAQLET------YKRQVQDLHTKLSSESKRAdTLAFEMKRLEEKHETLLK---- 416
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENeleaaaLEERLKEARLLLLIAAALL-ALLGLGGSLLSLILTIAGvlfl 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 417 -------EKERLIEQRDTLKETNEELRCSKAQQDhLNQADSSATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGT 489
Cdd:COG4717 282 vlgllalLFLLLAREKASLGKEAEELQALPALEE-LEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 490 ENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQGSKSEGESSSKLKQkleahmEKLTEVHEEL 569
Cdd:COG4717 361 EELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEA------LDEEELEEEL 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958776293 570 QKKQELIEDLQPDISQNAQKISELEAALQK--KDEDMKAMEERYKMYLEKARNVIK 623
Cdd:COG4717 435 EELEEELEELEEELEELREELAELEAELEQleEDGELAELLQELEELKAELRELAE 490
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
483-656 |
2.23e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 483 RLQQEGTENERIEQLQEQLEQKHRKMNELEteqrlskERIGELQQQIEDLQKSLQEQGSKSEgesssklKQKLEAHMEKL 562
Cdd:COG4717 79 ELKEAEEKEEEYAELQEELEELEEELEELE-------AELEELREELEKLEKLLQLLPLYQE-------LEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 563 TEVHEELQKKQELIEDLQPDISQNAQKISELEAALQKKDEDMKAMEERykmYLEKARNVIKTLDPKLNPASAEIMLLRKQ 642
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE---ELQDLAEELEELQQRLAELEEELEEAQEE 221
|
170
....*....|....
gi 1958776293 643 LAEKDRRIEILESE 656
Cdd:COG4717 222 LEELEEELEQLENE 235
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
316-562 |
3.16e-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: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 316 ATSDKANKLESTVEVYRQKLQDLNDLRKQVKSLQEtnmmymhntvSLEEELKKANAARAQLEtykRQVQDLHTKLSSESK 395
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEK----------ALLKQLAALERRIAALA---RRIRALEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 396 RADTLAFEMKRLEEKHETLLKEKERLI------EQRDTLK-----ETNEELRCSKAQQDHLNQADSSATKSYENLAAEIm 464
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKEELAELLralyrlGRQPPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 465 pveyREVFIRLQHENKMLRLQQEGTENERiEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQGSKSE 544
Cdd:COG4942 163 ----AALRAELEAERAELEALLAELEEER-AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
250
....*....|....*...
gi 1958776293 545 GESSSKLKQKLEAHMEKL 562
Cdd:COG4942 238 AAAERTPAAGFAALKGKL 255
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
185-645 |
3.20e-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: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 185 LKRALEELQEALAEKEELKQRCQELDMQVTALQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAKKYFHVQLQLEQLqe 264
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKI-- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 265 enyrleaakddyrvhcEELEKQLIEFQHRNDELTSLAEE--TRALKDEIDvlratsDKANKLESTVEVYRQKLQDLNDLR 342
Cdd:TIGR04523 284 ----------------KELEKQLNQLKSEISDLNNQKEQdwNKELKSELK------NQEKKLEEIQNQISQNNKIISQLN 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 343 KQVKSLQETNMMYMHNTVSLEEELKKANAA-----------RAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKH 411
Cdd:TIGR04523 342 EQISQLKKELTNSESENSEKQRELEEKQNEieklkkenqsyKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEK 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 412 ETLLKEKERLIEQRDTLKETNEELRCSKAQQDhLNQADSSATKSYENLAAEIMPVEYREVFIRLQHENKMLRL--QQEGT 489
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNNSEIKDLTNQDSVKE-LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSkeKELKK 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 490 ENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEEL 569
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSL 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 570 QKKQ----ELIEDLQPDISQNAQKISELEAALQKKDEDMKAMEERYkmylEKARNVIKTLDPKLNPASAEIMLLRKQLAE 645
Cdd:TIGR04523 581 KKKQeekqELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKEN----EKLSSIIKNIKSKKNKLKQEVKQIKETIKE 656
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
425-670 |
4.86e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.55 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 425 RDTLKETNEELRCSKAQQDHLNQadssATKSYENLAAEimpveyrevfirlqhenkmlrlqQEGTENERIEQLQEQLEQK 504
Cdd:PHA02562 173 KDKIRELNQQIQTLDMKIDHIQQ----QIKTYNKNIEE-----------------------QRKKNGENIARKQNKYDEL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 505 HRKMNELETEQRLSKERIGELQQQIEDLQKSLQEqgsksegesSSKLKQKLEAHMEKLTEVHEELQKKQEL------IED 578
Cdd:PHA02562 226 VEEAKTIKAEIEELTDELLNLVMDIEDPSAALNK---------LNTAAAKIKSKIEQFQKVIKMYEKGGVCptctqqISE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 579 LQPDISQNAQKISELEAALQKKDEDMKAMEERYKMYLEkARNVIKTLDPKLNPASAEIMLLRKQLAEKDRRIEILESECK 658
Cdd:PHA02562 297 GPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNE-QSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFV 375
|
250
....*....|....*..
gi 1958776293 659 -----VAKFRDYEEKLI 670
Cdd:PHA02562 376 dnaeeLAKLQDELDKIV 392
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
491-656 |
4.94e-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: 46.30 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 491 NERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEqgsksegessskLKQKLEAHMEKLTEVHEELQ 570
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA------------LARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 571 KKQELIEDLQPDISQNAQKISELEAALQK-----------KDEDMKAMEERYkMYLEKARNVIKTLDPKLNPASAEIMLL 639
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLRALYRlgrqpplalllSPEDFLDAVRRL-QYLKYLAPARREQAEELRADLAELAAL 165
|
170
....*....|....*..
gi 1958776293 640 RKQLAEKDRRIEILESE 656
Cdd:COG4942 166 RAELEAERAELEALLAE 182
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
485-656 |
4.96e-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: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 485 QQEGTENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQGSKSEGESSSKLKQK---------- 554
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGgsvsyldvll 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 555 ----LEAHMEKLTEVHEELQKKQELIEDLQPDISQNAQKISELEAALQKKDEDMKAMEERYKMY---LEKARNVIKTLDP 627
Cdd:COG3883 110 gsesFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELeaqQAEQEALLAQLSA 189
|
170 180
....*....|....*....|....*....
gi 1958776293 628 KLNPASAEIMLLRKQLAEKDRRIEILESE 656
Cdd:COG3883 190 EEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
404-596 |
6.98e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 6.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 404 MKRLEEKHETLLKEKERL-IEQRDTLKETNEELRCSKAQQDHLNQAD---SSATKSYENLAAEIMPVEYREVFIRLQHEN 479
Cdd:COG4717 48 LERLEKEADELFKPQGRKpELNLKELKELEEELKEAEEKEEEYAELQeelEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 480 KMLRLQQEGTENER--IEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQgsksEGESSSKLKQKLEA 557
Cdd:COG4717 128 LPLYQELEALEAELaeLPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA----TEEELQDLAEELEE 203
|
170 180 190
....*....|....*....|....*....|....*....
gi 1958776293 558 HMEKLTEVHEELQKKQELIEDLQPDISQNAQKISELEAA 596
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
359-620 |
7.05e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.29 E-value: 7.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 359 TVSLEEELKKANAARAQLETYKR-------QVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKET 431
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEkrdelneELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 432 NEELRCSKAQQDHLNQADSSATKSYENLAAEIMPVEYRevfirlqHENKMLRLQQEGTENERIEQLQEQLE------QKH 505
Cdd:COG1340 87 LNELREELDELRKELAELNKAGGSIDKLRKEIERLEWR-------QQTEVLSPEEEKELVEKIKELEKELEkakkalEKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 506 RKMNELETEQRLSKERIGELQQQIEDLQKSLQEqgsksEGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDISQ 585
Cdd:COG1340 160 EKLKELRAELKELRKEAEEIHKKIKELAEEAQE-----LHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIE 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1958776293 586 NAQKISELEAALQ---------KKDEDMKAMEERYKMYLEKARN 620
Cdd:COG1340 235 LQKELRELRKELKklrkkqralKREKEKEELEEKAEEIFEKLKK 278
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
296-612 |
1.08e-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: 45.71 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 296 ELTSLAEETRALKDEIDVLRATSdkaNKLESTVEVYRQKLQDLNDLRKQVKSLQETNMMymHNTVSLEEELKKANAARAQ 375
Cdd:COG3096 837 ELAALRQRRSELERELAQHRAQE---QQLRQQLDQLKEQLQLLNKLLPQANLLADETLA--DRLEELREELDAAQEAQAF 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 376 LETYKRQVQDLHTKLSSeskradtlafeMKRLEEKHETLLKEKERLIEQRDTLKETNEELRCSKAQQDHLNQADSSAtks 455
Cdd:COG3096 912 IQQHGKALAQLEPLVAV-----------LQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSYEDAVG--- 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 456 yenlaaeiMPVEYREVFIRLQHenKMLRLQQEGTE-NERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQK 534
Cdd:COG3096 978 --------LLGENSDLNEKLRA--RLEQAEEARREaREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGV 1047
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958776293 535 SLQEQGSKSegesssklkqkleAHMEKlTEVHEELqkkqeliedlqpdiSQNAQKISELEAALQKKDEDMKAMEERYK 612
Cdd:COG3096 1048 QADAEAEER-------------ARIRR-DELHEEL--------------SQNRSRRSQLEKQLTRCEAEMDSLQKRLR 1097
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
181-651 |
1.52e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.28 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 181 LEQQLKRALEELQEALAEKEELKQRCQELDMQVTALQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAKKYFHVQLQLE 260
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSM 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 261 QLQEENYRLEAAKDDYRVHCEELEK---QLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEVYRQKLQD 337
Cdd:PRK01156 268 ELEKNNYYKELEERHMKIINDPVYKnrnYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSR 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 338 LNDLRKQVKSLQETNMMYMHNTVSLEEELKKanaaraqLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKE 417
Cdd:PRK01156 348 YDDLNNQILELEGYEMDYNSYLKSIESLKKK-------IEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQD 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 418 KE----RLIEQRDTLKETNEELRCSKAQQDHLNQADSSATKSYENLAAEIMPvEYREVFIRLQHENKMLRLQQEGTENER 493
Cdd:PRK01156 421 ISskvsSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIIN-HYNEKKSRLEEKIREIEIEVKDIDEKI 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 494 IEQLQEQLEQKHRKMNELETEQRLSKERIGELqQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEELQKKQ 573
Cdd:PRK01156 500 VDLKKRKEYLESEEINKSINEYNKIESARADL-EDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVIS 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 574 EL-IEDLQPDISQNAQKISELEAALQKKDEDMKAMEERYKMYLEKARNVIKTLDPKLNPASA----------EIMLLRKQ 642
Cdd:PRK01156 579 LIdIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQEnkilieklrgKIDNYKKQ 658
|
....*....
gi 1958776293 643 LAEKDRRIE 651
Cdd:PRK01156 659 IAEIDSIIP 667
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
303-538 |
1.86e-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: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 303 ETRALKDEIDVLRATSDKANKLESTVEVYRQKLQDLNDLRKQVKSLQEtnmmymhntvsLEEELKKANAARAQLETYKRQ 382
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALEDAREQIELLEPIRELAERYAA-----------ARERLAELEYLRAALRLWFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 383 vqdlhtklssesKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKETNEELRcskaqqdhlNQADSSATKSYENLAAE 462
Cdd:COG4913 288 ------------RRLELLEAELEELRAELARLEAELERLEARLDALREELDELE---------AQIRGNGGDRLEQLERE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 463 I--MPVEYREV---FIRLQHENKMLRLQQEGTE---NERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQK 534
Cdd:COG4913 347 IerLERELEERerrRARLEALLAALGLPLPASAeefAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
....
gi 1958776293 535 SLQE 538
Cdd:COG4913 427 EIAS 430
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
268-539 |
2.43e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 268 RLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETraLKDEIDVLRATSDKANKLESTVevyRQKLQDLNDLRKQVKS 347
Cdd:PRK04863 855 DHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADET--LADRVEEIREQLDEAEEAKRFV---QQHGNALAQLEPIVSV 929
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 348 LQETNMMYmhntvsleEELKKA-NAARAQLETYKRQVQDLhtklSSESKRADTLAFE--MKRLEEKHETLLKEKERLIEQ 424
Cdd:PRK04863 930 LQSDPEQF--------EQLKQDyQQAQQTQRDAKQQAFAL----TEVVQRRAHFSYEdaAEMLAKNSDLNEKLRQRLEQA 997
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 425 RDTLKETNEELRCSKAQQDHLNQADSSATKSYENlaaeimpveYREVFIRLQHENKMLRLQ-QEGTEN---ERIEQLQEQ 500
Cdd:PRK04863 998 EQERTRAREQLRQAQAQLAQYNQVLASLKSSYDA---------KRQMLQELKQELQDLGVPaDSGAEErarARRDELHAR 1068
|
250 260 270
....*....|....*....|....*....|....*....
gi 1958776293 501 LEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQ 539
Cdd:PRK04863 1069 LSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEM 1107
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
180-614 |
2.54e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 180 ELEQQLKRALEELQEALAEKEELKQRCQELDMQVTALQDEKnslvsENEMMNEKLDQLDGSFDdpntmvakkyfhvqlql 259
Cdd:COG4717 92 ELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ-----ELEALEAELAELPERLE----------------- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 260 eqlqeenyRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIdvLRATSDKANKLESTVEVYRQKLQD-- 337
Cdd:COG4717 150 --------ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE--LQDLAEELEELQQRLAELEEELEEaq 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 338 --LNDLRKQVKSLQETNMMY-MHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETL 414
Cdd:COG4717 220 eeLEELEEELEQLENELEAAaLEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 415 LKEKERLIEQRDTLKETNEELRCSKAQQDHLNQADSsaTKSYENLAAEImpVEYREVFIRLQHENKMLRLQQEGTENERI 494
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPDLS--PEELLELLDRI--EELQELLREAEELEEELQLEELEQEIAAL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 495 EQLQ-----EQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEEL 569
Cdd:COG4717 376 LAEAgvedeEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREEL 455
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1958776293 570 QKKQELIEDLQPDisqnaQKISELEAALQKKDEDMKAMEERYKMY 614
Cdd:COG4717 456 AELEAELEQLEED-----GELAELLQELEELKAELRELAEEWAAL 495
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
362-557 |
2.84e-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: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 362 LEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKE----KERLIEQRDTLKETNEELRC 437
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeaEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 438 SKAQQDHLNQADSSatksyENLAAEIMPVEYREVFIRlqHENKMLRLQQEgtENERIEQLQEQLEQKHRKMNELETEQRL 517
Cdd:COG3883 98 SGGSVSYLDVLLGS-----ESFSDFLDRLSALSKIAD--ADADLLEELKA--DKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958776293 518 SKERIGELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEA 557
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
300-510 |
3.35e-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: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 300 LAEETRALKDEIDVLRATSDKANKLESTVEVYR---QKLQDLNDLRKQVKSLQETnmmymhnTVSLEEELKKANAARAQL 376
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERRealQRLAEYSWDEIDVASAERE-------IAELEAELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 377 ETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLketneELRCSKAQQDHLNQAdssatksy 456
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA-----EDLARLELRALLEER-------- 754
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958776293 457 enLAAEIMPVEYREVFIRLQHENKmlrlqqegTENERIEQLQEQLEQKHRKMNE 510
Cdd:COG4913 755 --FAAALGDAVERELRENLEERID--------ALRARLNRAEEELERAMRAFNR 798
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
174-538 |
3.74e-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: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 174 ASDAVGELEQQLKRALEELQEALAEKEELKQRCQELDMQVTALQdeknslvsenemmnekldqldgsfddpntmvakkyf 253
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ------------------------------------ 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 254 hvqlqleqlqeenyrleaakddyrvhceelekQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEVYRQ 333
Cdd:COG4913 652 --------------------------------RLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEA 699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 334 KLQDLNDLRKQvkslqetnmmymhntvsLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHET 413
Cdd:COG4913 700 ELEELEEELDE-----------------LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDA 762
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 414 LLKE-KERLIEQRDTLKETNEELRcskaqqDHLNQADSSATKSYENLAAEIMPV-----EYREVFIRLQ------HENKM 481
Cdd:COG4913 763 VERElRENLEERIDALRARLNRAE------EELERAMRAFNREWPAETADLDADleslpEYLALLDRLEedglpeYEERF 836
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958776293 482 LRLQQEgTENERIEQLQEQLEQKHRkmneleteqrlskerigELQQQIEDLQKSLQE 538
Cdd:COG4913 837 KELLNE-NSIEFVADLLSKLRRAIR-----------------EIKERIDPLNDSLKR 875
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
174-538 |
3.87e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 174 ASDAVGELEQQL---KRALEELQEAL----AEKEELKQRCQELDMQVTALQDEKNsLVSENEMMNEKLDQLDGSFDDPNT 246
Cdd:PRK04863 284 HLEEALELRRELytsRRQLAAEQYRLvemaRELAELNEAESDLEQDYQAASDHLN-LVQTALRQQEKIERYQADLEELEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 247 MVAKKYFHVQLQLEQLQEENYRLEAAKDDYrvhcEELEKQLIEFQHRNDELtslaeETRALK--------DEIDVLRATS 318
Cdd:PRK04863 363 RLEEQNEVVEEADEQQEENEARAEAAEEEV----DELKSQLADYQQALDVQ-----QTRAIQyqqavqalERAKQLCGLP 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 319 D-KANKLESTVEVYRQKLQDLNDLRKQvkslqetnmmymhntvsLEEELKKANAARAQLEtykrQVQDLHTKLSSESKRA 397
Cdd:PRK04863 434 DlTADNAEDWLEEFQAKEQEATEELLS-----------------LEQKLSVAQAAHSQFE----QAYQLVRKIAGEVSRS 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 398 DtlAFEMKR-LEEKHETLLKEKERLIEQRDTLKEtneelrcskAQQDHLNQADSsatksyenlaaeimpveyrevfIRLQ 476
Cdd:PRK04863 493 E--AWDVAReLLRRLREQRHLAEQLQQLRMRLSE---------LEQRLRQQQRA----------------------ERLL 539
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958776293 477 HENKMlRLQQEGTENERIEQLQEQLEQKhrkMNELETEQRLSKERIGELQQQIEDLQKSLQE 538
Cdd:PRK04863 540 AEFCK-RLGKNLDDEDELEQLQEELEAR---LESLSESVSEARERRMALRQQLEQLQARIQR 597
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
159-511 |
4.28e-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: 43.90 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 159 TAIQELMSKEIVSSPASDAVGELEQQLKRALEELQEALAE----KEELKQ---RCQELDMQVTALQDEKNSLVSENEMMN 231
Cdd:TIGR02169 692 SLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEeeklKERLEEleeDLSSLEQEIENVKSELKELEARIEELE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 232 EKLDQLDGSFDDPNTMVAKKYF-HVQLQLEQLQEENYRLEAAKDDYRVhceELEKQLIEFQHRNDELTSLAEETRALKDE 310
Cdd:TIGR02169 772 EDLHKLEEALNDLEARLSHSRIpEIQAELSKLEEEVSRIEARLREIEQ---KLNRLTLEKEYLEKEIQELQEQRIDLKEQ 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 311 IDVLRATSDKAN----KLESTVEVYRQKLQDLN----DLRKQVKSLQEtnmmymhntvSLEEELKKANAARAQLETYKRQ 382
Cdd:TIGR02169 849 IKSIEKEIENLNgkkeELEEELEELEAALRDLEsrlgDLKKERDELEA----------QLRELERKIEELEAQIEKKRKR 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 383 VQDLHTKLSSESKRADTLAFEMKRLEE------KHETLLKEKERLIEQRDTLKETNeelrcSKAQQDhlnqadssatksY 456
Cdd:TIGR02169 919 LSELKAKLEALEEELSEIEDPKGEDEEipeeelSLEDVQAELQRVEEEIRALEPVN-----MLAIQE------------Y 981
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1958776293 457 ENLAAEIMpvEYREVFIRLQHENKMLRLQQEGTENERIEQLQEQLEQKHRKMNEL 511
Cdd:TIGR02169 982 EEVLKRLD--ELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFEAINENFNEI 1034
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
480-669 |
4.69e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.66 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 480 KMLRLQQEGTENERIEQLQEQLEQKHR-------KMNELETEQRL---------SKERIGELQQQIEDLQKSLQEQgsks 543
Cdd:PRK00409 453 KALMYNREGVENASVEFDEETLRPTYRlligipgKSNAFEIAKRLglpeniieeAKKLIGEDKEKLNELIASLEEL---- 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 544 egesssklKQKLEahmEKLTEVHEELQKKQELIEDLQpdisqnaQKISELEaalQKKDEDMKAMEERYKMYLEKAR---- 619
Cdd:PRK00409 529 --------ERELE---QKAEEAEALLKEAEKLKEELE-------EKKEKLQ---EEEDKLLEEAEKEAQQAIKEAKkead 587
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958776293 620 NVIKTLDPKLNPASAEIMllRKQLAEKDRRI----EILESECKVAKFRDYEEKL 669
Cdd:PRK00409 588 EIIKELRQLQKGGYASVK--AHELIEARKRLnkanEKKEKKKKKQKEKQEELKV 639
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
295-619 |
7.14e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 295 DELTSLAEETRALKDEI------DVLRATSDKANKLESTVEVYRQKLQDLNDLRK--QVKSLQETNMMymhnTVSLEEEl 366
Cdd:COG3206 71 SGLSSLSASDSPLETQIeilksrPVLERVVDKLNLDEDPLGEEASREAAIERLRKnlTVEPVKGSNVI----EISYTSP- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 367 kkaNAARAQ------LETYKRQVQDLhtKLSSESKRADTLAFEMKRLEEKhetlLKEKERLIEQrdtLKETNEELRcSKA 440
Cdd:COG3206 146 ---DPELAAavanalAEAYLEQNLEL--RREEARKALEFLEEQLPELRKE----LEEAEAALEE---FRQKNGLVD-LSE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 441 QQDHLNQADSSATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQqEGTENERIEQLQEQLEQKHRKMNELEteQRLSKE 520
Cdd:COG3206 213 EAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALP-ELLQSPVIQQLRAQLAELEAELAELS--ARYTPN 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 521 --RIGELQQQIEDLQKSLQEQGSKsegessskLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDISQNAQKISELEaalq 598
Cdd:COG3206 290 hpDVIALRAQIAALRAQLQQEAQR--------ILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLE---- 357
|
330 340
....*....|....*....|.
gi 1958776293 599 kkdEDMKAMEERYKMYLEKAR 619
Cdd:COG3206 358 ---REVEVARELYESLLQRLE 375
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
307-587 |
7.85e-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: 7.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 307 LKDEIDVLRATSDKANKLESTVEVYRQKLQDLNDLRKQVKSLQETNMMYMHNTVSLEEEL-KKANAARAQLETYKRQVQD 385
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLaKEEEELKSELLKLERRKVD 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 386 LHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKETNEELRcskAQQDHLNQADSSATKSYENLAaeimp 465
Cdd:pfam02463 312 DEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELE---KLQEKLEQLEEELLAKKKLES----- 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 466 vEYREVFIRLQHENKMLRLQQEGTENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQGSKSEG 545
Cdd:pfam02463 384 -ERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK 462
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958776293 546 ESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDISQNA 587
Cdd:pfam02463 463 DELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESK 504
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
173-624 |
1.09e-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: 42.65 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 173 PASDAVGELEQQLKRALEELQEALAEKEELKQRCQELDMQVTALQDEKNSLVSENEMMNEKLDQLD--GSFDDPNTMVAK 250
Cdd:TIGR00618 297 AHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEvaTSIREISCQQHT 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 251 KYFHVQLQLEQLQEENYRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAeetRALKDEIDVLRATSDKANKLESTVEV 330
Cdd:TIGR00618 377 LTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLA---HAKKQQELQQRYAELCAAAITCTAQC 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 331 YRQKLQDLNDLRKQVKSLQEtNMMYMHNTVSLEEELKKANAARAQ-LETYKRQVQDLHTKLSSESKRADTLAFEMKRLEE 409
Cdd:TIGR00618 454 EKLEKIHLQESAQSLKEREQ-QLQTKEQIHLQETRKKAVVLARLLeLQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQR 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 410 KHETLLKEKERLIEQRDTLKETNEELRCSKAQQDHLNQADSSATKSYENLAAEIMPVEYREVFIR-LQHENKMLRLQQEG 488
Cdd:TIGR00618 533 GEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQdLTEKLSEAEDMLAC 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 489 TENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQE------QGSKSEGESSSKLKQKLEAHMEKL 562
Cdd:TIGR00618 613 EQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREhalsirVLPKELLASRQLALQKMQSEKEQL 692
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958776293 563 TEVHEELQKKQELIEDLQPDISQNAQKISELEAALQKKDEDMKAMEERYKMYLEKARNVIKT 624
Cdd:TIGR00618 693 TYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQART 754
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
525-670 |
1.47e-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: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 525 LQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDISQNAQKISELEAALQKKDEdm 604
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARS-- 455
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958776293 605 kamEERYKMyleKARNVIKTLDpklnpasAEIMLLRKQLAEKDRRIEILESecKVAKFRDYEEKLI 670
Cdd:COG2433 456 ---EERREI---RKDREISRLD-------REIERLERELEEERERIEELKR--KLERLKELWKLEH 506
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
433-539 |
1.71e-03 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 41.90 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 433 EELRcsKAQQDHLNQAdssATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGTENERIEQLQEQLEQKHRKMNELE 512
Cdd:pfam13779 516 QELR--EALDDYMQAL---AEQAQQNPQDLQQPDDPNAQEMTQQDLQRMLDRIEELARSGRRAEAQQMLSQLQQMLENLQ 590
|
90 100
....*....|....*....|....*....
gi 1958776293 513 TEQR--LSKERIGELQQQIEDLQKSLQEQ 539
Cdd:pfam13779 591 AGQPqqQQQQGQSEMQQAMDELGDLLREQ 619
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
176-664 |
1.88e-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: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 176 DAVGELEQQLKRALEELQEALAEKEELKQRCQELDMQvtalqdeknslVSENEMMNEKLDQLDGSFDDPNTMVAKKYFHV 255
Cdd:pfam05557 111 NELSELRRQIQRAELELQSTNSELEELQERLDLLKAK-----------ASEAEQLRQNLEKQQSSLAEAEQRIKELEFEI 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 256 QLQLEQLQEenyrLEAAKDDYrVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRA-------TSDKANKLESTV 328
Cdd:pfam05557 180 QSQEQDSEI----VKNSKSEL-ARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRklereekYREEAATLELEK 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 329 EVYRQKLQ-----------DLN---DLRKQVKSLQETNMMYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSES 394
Cdd:pfam05557 255 EKLEQELQswvklaqdtglNLRspeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKL 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 395 KRADTLAfemKRLEEKHETLLKEkerlieqRDTLKETNEELrcskaqQDHLNQADSSATKSYENLAAEIMPVEYREVFIR 474
Cdd:pfam05557 335 KRHKALV---RRLQRRVLLLTKE-------RDGYRAILESY------DKELTMSNYSPQLLERIEEAEDMTQKMQAHNEE 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 475 LQHenKMLRLQQEGTENERIEQLQEQlEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQGSKsegesssklKQK 554
Cdd:pfam05557 399 MEA--QLSVAEEELGGYKQQAQTLER-ELQALRQQESLADPSYSKEEVDSLRRKLETLELERQRLREQ---------KNE 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 555 LEAHMEKLTEVHEELQKKQELIEDLQPDISQNAQKISELEAALQKKDEDMKAMEERYKMYLEKARNVIKTldpKLNPASA 634
Cdd:pfam05557 467 LEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPET---TSTMNFK 543
|
490 500 510
....*....|....*....|....*....|..
gi 1958776293 635 EIMLLRKQLAEKDRRIEILESECKVA--KFRD 664
Cdd:pfam05557 544 EVLDLRKELESAELKNQRLKEVFQAKiqEFRD 575
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
473-629 |
2.03e-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: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 473 IRLQH-ENKMLRLQQE-GTENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQ---KSLQEQGSKSE--- 544
Cdd:COG1579 10 LDLQElDSELDRLEHRlKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEariKKYEEQLGNVRnnk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 545 -----GESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDISQNAQKISELEAALqkkDEDMKAMEERYKMYLEKAR 619
Cdd:COG1579 90 eyealQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL---DEELAELEAELEELEAERE 166
|
170
....*....|
gi 1958776293 620 NVIKTLDPKL 629
Cdd:COG1579 167 ELAAKIPPEL 176
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
469-622 |
3.20e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 469 REVFIRLQHENKMLRLQQEGTENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKslQEQGSKSEGESS 548
Cdd:PRK12704 56 KEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQ--KQQELEKKEEEL 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958776293 549 SKLKQKLEAHMEKLTEVHEElQKKQELIEDLQPDISQNAQKIseleaalqkkdedMKAMEERYKMYLEK-ARNVI 622
Cdd:PRK12704 134 EELIEEQLQELERISGLTAE-EAKEILLEKVEEEARHEAAVL-------------IKEIEEEAKEEADKkAKEIL 194
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
268-462 |
3.29e-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: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 268 RLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIdvlRATSDKANKLESTVEVYRQKLQDLN-DLRKQVK 346
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI---RALEQELAALEAELAELEKEIAELRaELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 347 SLQE-TNMMYMHNTVSLEEELKKANAARAQLetykRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQR 425
Cdd:COG4942 105 ELAElLRALYRLGRQPPLALLLSPEDFLDAV----RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 1958776293 426 DTLKETNEELRCSKAQQDHLNQADSSATKSYENLAAE 462
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 ... |
160-538 |
3.60e-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: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 160 AIQELMSKEIVSSPASDAVGELEQQLKRALEELQEALAEKEELKQRCQELDMQVTAlQDEKNSLVSENEMMNEKLDQLDG 239
Cdd:pfam02463 650 KGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKE-QREKEELKKLKLEAEELLADRVQ 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 240 SFDDPNTMVAKKYFHVQLQLEQLQEENYRLEAAKDDYRVHCEELEKQLIEFQHRNdeltslaEETRALKDEIDVLRATSD 319
Cdd:pfam02463 729 EAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKT-------EKLKVEEEKEEKLKAQEE 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 320 KANKLESTVEVYRQKLQDLNDLRKQVKSLQETNMMYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADT 399
Cdd:pfam02463 802 ELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEE 881
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 400 LAF--EMKRLEEKHETLLKEKERLIEQRDTLKETNEELRCSKAQQDHLNQADSSATKSYEnLAAEIMPVEYREVFIRLQH 477
Cdd:pfam02463 882 QKLkdELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELL-LEEADEKEKEENNKEEEEE 960
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958776293 478 ENKMLRLQQEGTENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQE 538
Cdd:pfam02463 961 RNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
181-468 |
3.67e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.66 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 181 LEQQLKRALEELQEALAEKEELKQRCQELDMQVtALQDEKNSLVSEN----EMMNEKLDQLDGSFDDPNTMVAKKYFHVQ 256
Cdd:PLN02939 147 LNQARLQALEDLEKILTEKEALQGKINILEMRL-SETDARIKLAAQEkihvEILEEQLEKLRNELLIRGATEGLCVHSLS 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 257 LQLEQLQEENYRLeaaKDDyrvhCEELEKQLIEFQHRNDELTSLAEEtRALKD------EIDVLRATSDKANKLESTVEV 330
Cdd:PLN02939 226 KELDVLKEENMLL---KDD----IQFLKAELIEVAETEERVFKLEKE-RSLLDaslrelESKFIVAQEDVSKLSPLQYDC 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 331 YRQKLQDLNDLRKQVKSLQETNMMYMHNTVSLEEELKKANAARAQLETYkrqvqdlhtKLSSEskRADTLAFEMKRLEEK 410
Cdd:PLN02939 298 WWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVS---------KFSSY--KVELLQQKLKLLEER 366
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958776293 411 HEtllKEKERLIEQRDTLKETNEELrcskaqQDHLNQADSSATKSYENLAAEIMPVEY 468
Cdd:PLN02939 367 LQ---ASDHEIHSYIQLYQESIKEF------QDTLSKLKEESKKRSLEHPADDMPSEF 415
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
187-607 |
3.80e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.66 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 187 RALEELQEALAEKEELKQRCQELDMQVTAL---QDEKNSLVSENEMMNEKLDQ---------------LDGSFDDPNTMV 248
Cdd:PRK01156 329 KKLSVLQKDYNDYIKKKSRYDDLNNQILELegyEMDYNSYLKSIESLKKKIEEyskniermsafiseiLKIQEIDPDAIK 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 249 aKKYFHVQLQLEQLQEENYRLEAAKDDYRVHCEELEKQLIEFQHRNDEL---TSLAEETRAlkdeiDVLRATSDKANKLE 325
Cdd:PRK01156 409 -KELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPvcgTTLGEEKSN-----HIINHYNEKKSRLE 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 326 STVEVYRQKLQDLNDLRKQVKSLQEtnMMYMHNTVSLEEELKKANAARAQLETYK---RQVQDLHTKLSSESKRADTLAF 402
Cdd:PRK01156 483 EKIREIEIEVKDIDEKIVDLKKRKE--YLESEEINKSINEYNKIESARADLEDIKikiNELKDKHDKYEEIKNRYKSLKL 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 403 EMkrLEEKHETLLKekerLIEQRDTLketneELRCSKAQQDHLNQADSSATKSYENLAAEIMPVE-YREVFIRLQHEnkm 481
Cdd:PRK01156 561 ED--LDSKRTSWLN----ALAVISLI-----DIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKsYIDKSIREIEN--- 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 482 lrlqqegtENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQqIEDLQKSLQEQGSKSEGESSSKLKQkleahmek 561
Cdd:PRK01156 627 --------EANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDS-IIPDLKEITSRINDIEDNLKKSRKA-------- 689
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1958776293 562 LTEVHEELQKKQELIEDLQPDISQNAQKISELEAALQKKDEDMKAM 607
Cdd:PRK01156 690 LDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAI 735
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
405-670 |
3.85e-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: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 405 KRLEEKHETLLKEKERLIEQRDTLKETNEELRCSKAQqdhlnqaDSSATKSYENLAAEIMPVEYREVFIRLQH-ENKMLR 483
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQ-------AKKALEYYQLKEKLELEEEYLLYLDYLKLnEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 484 LQQEGTENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQiEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLT 563
Cdd:pfam02463 242 LQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEE-ELKLLAKEEEELKSELLKLERRKVDDEEKLKESE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 564 EVHEELQKKQELiedLQPDISQNAQKISELEAALQKKDEDMKAMEERYKMYLEKARNVIKTLDPKLNPASAEIMLLRKQL 643
Cdd:pfam02463 321 KEKKKAEKELKK---EKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEEL 397
|
250 260
....*....|....*....|....*..
gi 1958776293 644 AEKDRRIEILESECKVAKFRDYEEKLI 670
Cdd:pfam02463 398 ELKSEEEKEAQLLLELARQLEDLLKEE 424
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
180-562 |
4.15e-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: 40.80 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 180 ELEQQLKRALEELQEALAEKEELKQRCQELDMQVTALQDEKNSLVSENEMMNEKLDQLdgsfddpNTMVAKKYFHVQLQL 259
Cdd:TIGR00606 699 DLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKV-------NRDIQRLKNDIEEQE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 260 EQLQEENYRLEAAKD---DYRVhCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEVYRQKLQ 336
Cdd:TIGR00606 772 TLLGTIMPEEESAKVcltDVTI-MERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 337 DLNDLRKQVKSLQETNMMYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLK 416
Cdd:TIGR00606 851 LIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS 930
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 417 EKER-----LIEQRDTLKETNEELRCSKAQQDHLNQADSSATKSYENLAAEIMpVEYREVFIRLQHENKMLRLQQEGTEN 491
Cdd:TIGR00606 931 SKETsnkkaQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVN-AQLEECEKHQEKINEDMRLMRQDIDT 1009
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958776293 492 ERIEQ--LQEQLEQKHR--KMNELETEQRLSKERIGELQ-QQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKL 562
Cdd:TIGR00606 1010 QKIQErwLQDNLTLRKRenELKEVEEELKQHLKEMGQMQvLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIK 1085
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
180-590 |
4.60e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 180 ELEQQLKRALEELQEALAEKEELKQRCQELDMQVTALQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAKKYFHVQLQL 259
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 260 EQLQEENYRLEAAKDDYRVHCEELEKQLIEFQhrndELTSLAEETRALKDEIDVLRATSDKANKLESTVEVYRQKLQDLN 339
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLE----NELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAG 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 340 DLRKQVKSLQETNMMYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKE 419
Cdd:COG4717 278 VLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 420 RLIEQRDTlketneeLRCSKAQQDHLNQADSSATKSYENLAAEImpVEYREVFIRLQHENKMLRLQ----QEGTENERIE 495
Cdd:COG4717 358 ELEEELQL-------EELEQEIAALLAEAGVEDEEELRAALEQA--EEYQELKEELEELEEQLEELlgelEELLEALDEE 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 496 QLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSlqeqgsksegESSSKLKQKLEAHMEKLTEVHEELQK---- 571
Cdd:COG4717 429 ELEEELEELEEELEELEEELEELREELAELEAELEQLEED----------GELAELLQELEELKAELRELAEEWAAlkla 498
|
410 420
....*....|....*....|....*.
gi 1958776293 572 -------KQELIEDLQPDISQNAQKI 590
Cdd:COG4717 499 lelleeaREEYREERLPPVLERASEY 524
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
286-612 |
5.10e-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: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 286 QLIEFQHRNDELTSLAEETRALKDEIDVlratsdKANKLESTVEVYRqklqdlnDLRKQVKSLQETNMmymHNTVSLEEE 365
Cdd:pfam10174 210 HLREELHRRNQLQPDPAKTKALQTVIEM------KDTKISSLERNIR-------DLEDEVQMLKTNGL---LHTEDREEE 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 366 LKkanaaraQLETYKRQVQDLHTK---LSSESKRADTlafEMKRLEEKHETLLKEKERLIEQRDTLKE--TNEELRCSKA 440
Cdd:pfam10174 274 IK-------QMEVYKSHSKFMKNKidqLKQELSKKES---ELLALQTKLETLTNQNSDCKQHIEVLKEslTAKEQRAAIL 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 441 QQD------HLNQADSSATKSYENLaaEIMPVEYREVFIRLQHENKMLRLQQE--GTENERIEQLQEQLEQKHRKMNELE 512
Cdd:pfam10174 344 QTEvdalrlRLEEKESFLNKKTKQL--QDLTEEKSTLAGEIRDLKDMLDVKERkiNVLQKKIENLQEQLRDKDKQLAGLK 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 513 T-------------------EQRLS-KERIGE-LQQQIEDLQKSLQEQGSKSEGESSSkLKQKLEAHMEKLTEVHEELQK 571
Cdd:pfam10174 422 ErvkslqtdssntdtalttlEEALSeKERIIErLKEQREREDRERLEELESLKKENKD-LKEKVSALQPELTEKESSLID 500
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1958776293 572 KQELIEDLQPDISQNAQKISELEAALQKKDEDMKAMEERYK 612
Cdd:pfam10174 501 LKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLK 541
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
169-425 |
5.16e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.75 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 169 IVSSPASDAVGELEQQLKRALEELQEALAEKEElkqrcqeldmQVTALQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMV 248
Cdd:COG4942 9 LLLALAAAAQADAAAEAEAELEQLQQEIAELEK----------ELAALKKEEKALLKQLAALERRIAALARRIRALEQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 249 AKkyfhvqlQLEQLQEENYRLEAAKDDYRVHCEELEKQLIEFQ--HRNDELTSLAEETRALkDEIDVLRATSDKANKLES 326
Cdd:COG4942 79 AA-------LEAELAELEKEIAELRAELEAQKEELAELLRALYrlGRQPPLALLLSPEDFL-DAVRRLQYLKYLAPARRE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 327 TVEVYRQKLQDLNDLRKQVKSLQETnmmymhntvsLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKR 406
Cdd:COG4942 151 QAEELRADLAELAALRAELEAERAE----------LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
250
....*....|....*....
gi 1958776293 407 LEEKHETLLKEKERLIEQR 425
Cdd:COG4942 221 EAEELEALIARLEAEAAAA 239
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
358-533 |
5.87e-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: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 358 NTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKETNEELRc 437
Cdd:COG3096 513 RLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLR- 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 438 skAQQDHLnqadssATKSYENLAAeimpveyREVFIRLQhenkmlrlQQEGTENERIEQLQEQLEQKHRKMNELETEQRL 517
Cdd:COG3096 592 --ARIKEL------AARAPAWLAA-------QDALERLR--------EQSGEALADSQEVTAAMQQLLEREREATVERDE 648
|
170
....*....|....*.
gi 1958776293 518 SKERIGELQQQIEDLQ 533
Cdd:COG3096 649 LAARKQALESQIERLS 664
|
|
| FapA |
pfam03961 |
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ... |
491-579 |
6.40e-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: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 491 NERIEQLQEQLEQKhrkmneleteqrlsKERIGELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEELQ 570
Cdd:pfam03961 155 KEKLEELEKELEEL--------------EEELEKLKKRLKKLPKKARGQLPPEKREQLEKLLETKNKLSEELEELEEELK 220
|
....*....
gi 1958776293 571 KKQELIEDL 579
Cdd:pfam03961 221 ELKEELESL 229
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
270-578 |
6.83e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 270 EAAKDDYRVHCEELEKQliEFQHRNDELTSlAEETRALKDEIDVlratsDKANKLESTVEVYRQKLQDLNDLRKqvKSLQ 349
Cdd:PTZ00121 1526 EAKKAEEAKKADEAKKA--EEKKKADELKK-AEELKKAEEKKKA-----EEAKKAEEDKNMALRKAEEAKKAEE--ARIE 1595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 350 ETNMMYMHNTVSLEEELKKANAARAQLETYKR------QVQDLHTKLSSESKRADTLafemkRLEEKHETLLKEKERLIE 423
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKaeeekkKVEQLKKKEAEEKKKAEEL-----KKAEEENKIKAAEEAKKA 1670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 424 QRDtlKETNEELRcsKAQQDHLNQADSSATKSYENLAAEImpveyrevfIRLQHENKMLRLQQEGTENERIEQLQEQLEQ 503
Cdd:PTZ00121 1671 EED--KKKAEEAK--KAEEDEKKAAEALKKEAEEAKKAEE---------LKKKEAEEKKKAEELKKAEEENKIKAEEAKK 1737
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958776293 504 KHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEELQKKQELIED 578
Cdd:PTZ00121 1738 EAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
180-612 |
7.31e-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: 7.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 180 ELEQQLKRALEELQEALAEKEELKQRCQELDMQVTALQdEKNSLVSENEMMNEKLDQLDGSfdDPNTMVAKKYFHVQLQL 259
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIE-ELRAQEAVLEETQERINRARKA--APLAAHIKAVTQIEQQA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 260 EQLQEENYRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDV---LRATSDKANKLESTVEVYRQKLQ 336
Cdd:TIGR00618 310 QRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVatsIREISCQQHTLTQHIHTLQQQKT 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 337 DLNDLRKQVKSL--QETNMMYMHNTVSLEEELKKANAARA----QLETYKRQVQDLH-TKLSSESKRADTLAFEMKRLEE 409
Cdd:TIGR00618 390 TLTQKLQSLCKEldILQREQATIDTRTSAFRDLQGQLAHAkkqqELQQRYAELCAAAiTCTAQCEKLEKIHLQESAQSLK 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 410 KHETLLKEKERlIEQRDTLKETNEELRCSKAQQDHLNQADSSATKSYENLAAEIMPVEYREVfirLQHENKMLRLQQEG- 488
Cdd:TIGR00618 470 EREQQLQTKEQ-IHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRM---QRGEQTYAQLETSEe 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 489 -------TENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQgsksegesssklkqkLEAHMEK 561
Cdd:TIGR00618 546 dvyhqltSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKL---------------SEAEDML 610
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1958776293 562 LTEVHEELQKKQELIEDLQPDIS--QNAQKISELEAALQKKDEDMKAMEERYK 612
Cdd:TIGR00618 611 ACEQHALLRKLQPEQDLQDVRLHlqQCSQELALKLTALHALQLTLTQERVREH 663
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
500-656 |
7.79e-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: 7.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 500 QLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQgskseGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDL 579
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNEL-----QAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 580 QPDISQNAQKISELEAALQKKD--------EDMKAMEERYKMYLEKARNVIKTLDPKLNPASAEIMLLRKQLAEKDRRIE 651
Cdd:COG3883 92 ARALYRSGGSVSYLDVLLGSESfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
....*
gi 1958776293 652 ILESE 656
Cdd:COG3883 172 ELEAQ 176
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
291-533 |
8.38e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.61 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 291 QHRNDELTSLAEETRALKDEIDVLRAtsdKANKLESTVEVYRQKlQDLNDLRKQVKSLQEtnmmymhNTVSLEEELKKAN 370
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRK---ELEEAEAALEEFRQK-NGLVDLSEEAKLLLQ-------QLSELESQLAEAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 371 AARAQLETYKRQVQdlhtKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKETNEELRCSKAQQDHLNQads 450
Cdd:COG3206 233 AELAEAEARLAALR----AQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRA--- 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 451 satksyeNLAAEImpveyREVFIRLQHENKMLRlQQEGTENERIEQLQEQLE---QKHRKMNELETEQRLSKERIGELQQ 527
Cdd:COG3206 306 -------QLQQEA-----QRILASLEAELEALQ-AREASLQAQLAQLEARLAelpELEAELRRLEREVEVARELYESLLQ 372
|
....*.
gi 1958776293 528 QIEDLQ 533
Cdd:COG3206 373 RLEEAR 378
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
281-575 |
8.90e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 38.74 E-value: 8.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 281 EELEKQLIEFQHRNDELTSLAEETRALKDE-IDVLRATSDKANKLESTVEVYRQKLQDLNDLRK----QVKSLQEtnmmy 355
Cdd:COG1340 4 DELSSSLEELEEKIEELREEIEELKEKRDElNEELKELAEKRDELNAQVKELREEAQELREKRDelneKVKELKE----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 356 mhntvSLEEELKKANAARAQLETYKRQVQDLHTKLSSEskraDTLAFEMKRLEEKHET--LLKEKER-LIEQRDTLKETN 432
Cdd:COG1340 79 -----ERDELNEKLNELREELDELRKELAELNKAGGSI----DKLRKEIERLEWRQQTevLSPEEEKeLVEKIKELEKEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 433 EELRCSKAQQDHLNQADSSATKSYENLAAEIMPV-EYREvfIRLQHENKMLRLQQEgtenerIEQLQEQLEQKHRKMNEL 511
Cdd:COG1340 150 EKAKKALEKNEKLKELRAELKELRKEAEEIHKKIkELAE--EAQELHEEMIELYKE------ADELRKEADELHKEIVEA 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958776293 512 ETEQRLSKERIGELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEahmEKLTEVHEELQKKQEL 575
Cdd:COG1340 222 QEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELE---EKAEEIFEKLKKGEKL 282
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
320-606 |
9.37e-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: 9.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 320 KANKLESTVEVYRQKLQDLNDLRKQVKSLQETNMMYMHNTVSLEEELKKANAARAQLETYKRQ----VQDLHTKLSSESK 395
Cdd:pfam01576 10 KEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQEleeiLHELESRLEEEEE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 396 RADTLAFEMKRLEEKHETLLK--EKERLIEQRDTLKETNEELRCSKAQQDHLNQADSSATKSYENLAAEIMPVEYREVFI 473
Cdd:pfam01576 90 RSQQLQNEKKKMQQHIQDLEEqlDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 474 RLQHENKML---RLQQEGTenerIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQGSksegesssk 550
Cdd:pfam01576 170 EEEEKAKSLsklKNKHEAM----ISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRA--------- 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958776293 551 lkqkleahmeKLTEVHEELQKKQELIEDLQPDISQNAQKISELEAALQKKDEDMKA 606
Cdd:pfam01576 237 ----------QLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLES 282
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
363-612 |
9.75e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.56 E-value: 9.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 363 EEELKKANAARAQLEtykRQVQDLHTKLSSESKRADTLAFEMKRLEE--KHETLLKEK---ERLIEQRDTLKETNEELRC 437
Cdd:PRK04863 836 EAELRQLNRRRVELE---RALADHESQEQQQRSQLEQAKEGLSALNRllPRLNLLADEtlaDRVEEIREQLDEAEEAKRF 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 438 SKAQQDHLNQADSSATK------SYENLAAEIMPVEYR------------EVFIRLQHENKMLRLQQEGTENERIEQLQE 499
Cdd:PRK04863 913 VQQHGNALAQLEPIVSVlqsdpeQFEQLKQDYQQAQQTqrdakqqafaltEVVQRRAHFSYEDAAEMLAKNSDLNEKLRQ 992
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776293 500 QLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQeqgskSEGESSSKLKQKLEAHMEKLTEVHEELQKKQEliEDL 579
Cdd:PRK04863 993 RLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYD-----AKRQMLQELKQELQDLGVPADSGAEERARARR--DEL 1065
|
250 260 270
....*....|....*....|....*....|...
gi 1958776293 580 QPDISQNAQKISELEAALQKKDEDMKAMEERYK 612
Cdd:PRK04863 1066 HARLSANRSRRNQLEKQLTFCEAEMDNLTKKLR 1098
|
|
| |
