|
Name |
Accession |
Description |
Interval |
E-value |
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
186-534 |
7.34e-157 |
|
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: 458.77 E-value: 7.34e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 186 ELQEAIAEKEELKQRCQELDMQVTTLQDEKNSLVSENEMMNEKLDQLDgSFDDPNTMVAKKYFHVQLQLEQLQEENYRLE 265
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLE-SGDDSGTPGGKKYLLLQKQLEQLQEENFRLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 266 AAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEVYRQKLQDLNDLRKQVKSLQE 345
Cdd:pfam05622 80 TARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLGDLRRQVKLLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 346 TNMMYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKE 425
Cdd:pfam05622 160 RNAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 426 TNEELRCSKAQQDHLNQADASATKSY---ENLAAEIMPVEYREVFIRLQHENKMLRLQQEGTENERIEQLQEQLEQKHRK 502
Cdd:pfam05622 240 TNEELRCAQLQQAELSQADALLSPSSdpgDNLAAEIMPAEIREKLIRLQHENKMLRLGQEGSYRERLTELQQLLEDANRR 319
|
330 340 350
....*....|....*....|....*....|..
gi 568929948 503 MNELETEQRLSKERIGELQQQIEDLQKSLQEQ 534
Cdd:pfam05622 320 KNELETQNRLANQRILELQQQVEELQKALQEQ 351
|
|
| HkD_Hook1 |
cd22225 |
Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a ... |
14-163 |
3.98e-98 |
|
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: 294.45 E-value: 3.98e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 14 LCDSLIIWLQTFKTASPCQDVKQLTNGVTMAQVLHQIDVAWFSESWLSRIKDDVGDNWRIKASNLKKVLHGITSYYHEFL 93
Cdd:cd22225 1 LCDSLIIWLQTFNTAAPCQTVQDLTSGVAMAQVLHQIDSSWFDESWLSRIKEDVGDNWRIKMSNLKKILQGIVDYYHEFL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 94 GQQISEELIPDLNQITECADPVELGRLLQLILGCAVNCEKKQEHIKNIMTLEESVQHVVMTAIQELMSKE 163
Cdd:cd22225 81 DQQISEFLLPDLNRIAEHSDPVELGRLLQLILGCAVNCEKKQEHIQNIMTLEESVQHVVMTAIQELMSKE 150
|
|
| HOOK_N |
pfam19047 |
HOOK domain; This domain is found at the N-terminus of HOOK proteins. |
14-163 |
7.86e-88 |
|
HOOK domain; This domain is found at the N-terminus of HOOK proteins.
Pssm-ID: 465958 Cd Length: 151 Bit Score: 267.74 E-value: 7.86e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 14 LCDSLIIWLQTFKTASPCQDVKQLTNGVTMAQVLHQIDVAWFSESWLSRIKDDVGDNWRIKASNLKKVLHGITSYYHEFL 93
Cdd:pfam19047 2 LCDSLLTWLQTFNVPAPCATVEDLTDGVAMAQVLHQIDPSWFTEAWLSRIKEDVGDNWRLKVSNLKKILQSVVDYYQDVL 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 94 GQQISEELIPDLNQITECADPVELGRLLQLILGCAVNCEKKQEHIKNIMTLEESVQHVVMTAIQELMSKE 163
Cdd:pfam19047 82 GQQISDFLLPDVNLIGEHSDPAELGRLLQLILGCAVNCEKKQEYIQQIMTLEESVQHVVMTAIQELMSKD 151
|
|
| HkD_Hook |
cd22222 |
Hook domain found in Hook family of microtubule-binding proteins; The Hook family includes ... |
15-161 |
1.78e-84 |
|
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: 259.10 E-value: 1.78e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 15 CDSLIIWLQTFKTASPCQDVKQLTNGVTMAQVLHQIDVAWFSESWLSRIKDDVGDNWRIKASNLKKVLHGITSYYHEFLG 94
Cdd:cd22222 1 CDSLLQWLQTFNLIAPHATAEDLSDGVAIAQVLNQIDPEYFSDSWLSKIKPDVGDNWRLKVSNLKKILKGIVDYYSEVLG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568929948 95 QQISEELIPDLNQITECADPVELGRLLQLILGCAVNCEKKQEHIKNIMTLEESVQHVVMTAIQELMS 161
Cdd:cd22222 81 QQISGFTMPDVNAIAEKEDPKELGRLLQLVLGCAVNCERKEEYIQAIMGLEESVQHVVMEAIQELMS 147
|
|
| HkD_Hook3 |
cd22226 |
Hook domain found in protein Hook 3 (Hook3) and similar proteins; Hook3 is an adaptor protein ... |
14-162 |
8.90e-70 |
|
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: 221.38 E-value: 8.90e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 14 LCDSLIIWLQTFKTASPCQDVKQLTNGVTMAQVLHQIDVAWFSESWLSRIKDDVGDNWRIKASNLKKVLHGITSYYHEFL 93
Cdd:cd22226 5 LCESLLTWIQTFNVDAPCQTVEDLTSGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEIL 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568929948 94 GQQISEELIPDLNQITECADPVELGRLLQLILGCAVNCEKKQEHIKNIMTLEESVQHVVMTAIQELMSK 162
Cdd:cd22226 85 GQQINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMSK 153
|
|
| HkD_Hook2 |
cd22227 |
Hook domain found in protein Hook 2 (Hook2) and similar proteins; Hook2 is a ... |
14-162 |
8.15e-69 |
|
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: 218.59 E-value: 8.15e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 14 LCDSLIIWLQTFKTASPCQDVKQLTNGVTMAQVLHQIDVAWFSESWLSRIKDDVGDNWRIKASNLKKVLHGITSYYHEFL 93
Cdd:cd22227 2 LCDSLLTWLQTFQVPSPCSSYQDLTSGVAIAQVLNRIDPSWFNEAWLGRIKEDTGDNWRLKVSNLKKILQSLLEYYQDVL 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568929948 94 GQQISEELIPDLNQITECADPVELGRLLQLILGCAVNCEKKQEHIKNIMTLEESVQHVVMTAIQELMSK 162
Cdd:cd22227 82 GHQVSEDHLPDVNLIGEFSDDTELGKLLQLVLGCAISCEKKQEHIQQIMTLEESVQHVVMEAIQELLTK 150
|
|
| HkD_SF |
cd22211 |
Hook domain-containing proteins superfamily; The Hook domain superfamily includes Hook adaptor ... |
16-161 |
2.52e-49 |
|
Hook domain-containing proteins superfamily; The Hook domain superfamily includes Hook adaptor proteins, Hook-related proteins and nuclear mitotic apparatus protein (NuMA). They share an N-terminal conserved globular Hook domain, which folds as a variant of the helical calponin homology (CH) domain with an extended alpha-helix. The Hook domain is responsible for the binding of microtubule. The Hook family includes microtubule-binding proteins, Hook1-3. Hook1 is required for spermatid differentiation. Hook2 contributes to the establishment and maintenance of centrosome function. Hook3 is an adaptor protein for microtubule-dependent intracellular vesicle and protein trafficking, and is involved in Golgi and endosome transport. Hook proteins are components of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex. The Hook-related protein (HkRP) family includes Daple, Girdin and Gipie. Daple, also called Dvl-associating protein with a high frequency of leucine residues, or coiled-coil domain-containing protein 88C(CCDC88C), or Hook-related protein 2 (HkRP2), is a novel non-receptor nucleotide exchange factor (GEF) required for activation of guanine nucleotide-binding proteins (G-proteins) during non-canonical Wnt signaling. Girdin, also called Akt phosphorylation enhancer (APE), or coiled-coil domain-containing protein 88A (CCDC88A), or G alpha-interacting vesicle-associated protein (GIV), or Girders of actin filament, or Hook-related protein 1 (HkRP1), is a bifunctional modulator of guanine nucleotide-binding proteins (G proteins). Gipie, also called GRP78-interacting protein induced by ER stress, or coiled-coil domain-containing protein 88B(CCDC88B), or brain leucine zipper domain-containing protein, or Hook-related protein 3 (HkRP3), is a novel actin cytoskeleton-binding protein and Akt substrate that regulates cell migratory responses in various biological contexts. NuMA, also called nuclear mitotic apparatus protein 1, or nuclear matrix protein-22 (NMP-22), or SP-H antigen, is a microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignment and the segregation of chromosomes during mitotic cell division.
Pssm-ID: 411792 Cd Length: 145 Bit Score: 167.07 E-value: 2.52e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 16 DSLIIWLQTFKTASPCQDVKQLTNGVTMAQVLHQIDVAWFSESWLSriKDDVGDNWRIKASNLKKVLHGITSYYHEFLGQ 95
Cdd:cd22211 2 AALLAWINTFPLSSPVESLDDLSDGVVLAEILSQIDPSYFDSEWLE--SRDSSDNWVLKLNNLKKLYRSLSKYYREVLGQ 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568929948 96 QISEELIPDLNQITECADPVELGRLLQLILGCAVNCEKKQEHIKNIMTLEESVQHVVMTAIQELMS 161
Cdd:cd22211 80 QLSDLPLPDLSAIARDGDEEEIVKLLELVLGAAVQCENKEEYIARIQQLDESTQAELMLIIQEVLE 145
|
|
| HkD_HkRP |
cd22223 |
Hook domain found in the Hook-related protein (HkRP) family; The HkRP family includes Daple, ... |
14-159 |
2.23e-25 |
|
Hook domain found in the Hook-related protein (HkRP) family; The HkRP family includes Daple, Girdin and Gipie. Daple, also called Dvl-associating protein with a high frequency of leucine residues, or coiled-coil domain-containing protein 88C (CCDC88C), or Hook-related protein 2 (HkRP2), is a novel non-receptor nucleotide exchange factor (GEF) required for activation of guanine nucleotide-binding proteins (G-proteins) during non-canonical Wnt signaling. Girdin, also called Akt phosphorylation enhancer (APE), or coiled-coil domain-containing protein 88A (CCDC88A), or G alpha-interacting vesicle-associated protein (GIV), or Girders of actin filament, or Hook-related protein 1 (HkRP1), is a bifunctional modulator of guanine nucleotide-binding proteins (G proteins). It acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein G(i) alpha subunits. It also acts as a guanine nucleotide dissociation inhibitor for guanine nucleotide-binding protein G(s) subunit alpha GNAS. In addition, Girdin plays an essential role in cell migration. Gipie, also called GRP78-interacting protein induced by ER stress, or coiled-coil domain-containing protein 88B (CCDC88B), or brain leucine zipper domain-containing protein, or Hook-related protein 3 (HkRP3), is a novel actin cytoskeleton-binding protein and Akt substrate that regulates cell migratory responses in various biological contexts. It acts as a positive regulator of T-cell maturation and inflammatory function. As a microtubule-binding protein, Gipie regulates lytic granule clustering and NK cell killing. All family members contain a conserved globular Hook domain which folds as a variant of the helical calponin homology (CH) domain.
Pssm-ID: 411794 Cd Length: 149 Bit Score: 101.90 E-value: 2.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 14 LCDSLIIWLQTFKTASPCQ-DVKQLTNGVTMAQVLHQIDVAWFSESWLSRIKDDVgdNWRIKasNLKKVLHGITSYYHEF 92
Cdd:cd22223 2 LSSPLVTWAKTFADDGSAElSYTDLVDGVFLNNVMLQIDPRPFSEVSNRNVDDDV--NARIQ--NLDLLLRNIKSFYQEV 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568929948 93 LGQQISEELiPDLNQIteCADP------VELGRLLQLILGCAVNCEKKQEHIKNIMTLEESVQHVVMTAIQEL 159
Cdd:cd22223 78 LQQLIVMKL-PDILTI--GREPeseqslEELEKLLLLLLGCAVQCERKEEFIERIKNLDLEVQHALVACIQEV 147
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
158-532 |
7.24e-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: 71.63 E-value: 7.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 158 ELMSKEIVISPASDTVGELEQQLKRALEELQEAIaekEELKQRCQELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFD 237
Cdd:TIGR02168 653 DLVRPGGVITGGSAKTNSSILERRREIEELEEKI---EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIS 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 238 DPNTMVAKKYFHVQLQLEQLQEENYRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKAN 317
Cdd:TIGR02168 730 ALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 318 K-LESTVEVYRQKLQDLNDLRKQVKSLQETNMMYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLA 396
Cdd:TIGR02168 810 AeLTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 397 FEMK-RLEEKHETLLKEKERLIEQRDTLKETNE-----ELRCSKAQQDHLNQADAsATKSYENLAAEIMPVEYREVFIRL 470
Cdd:TIGR02168 890 ALLRsELEELSEELRELESKRSELRRELEELREklaqlELRLEGLEVRIDNLQER-LSEEYSLTLEEAEALENKIEDDEE 968
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568929948 471 QHENKMLRLQQE----GTENER-IEQLQEQleqkhrkmneleteqrlsKERIGELQQQIEDLQKSLQ 532
Cdd:TIGR02168 969 EARRRLKRLENKikelGPVNLAaIEEYEEL------------------KERYDFLTAQKEDLTEAKE 1017
|
|
| HkD_Daple |
cd22228 |
Hook domain found in Daple (Dvl-associating protein with a high frequency of leucine residues) ... |
18-159 |
3.36e-12 |
|
Hook domain found in Daple (Dvl-associating protein with a high frequency of leucine residues) and similar proteins; Protein Daple, also called coiled-coil domain-containing protein 88C (CCDC88C), or Hook-related protein 2 (HkRP2), is a novel non-receptor nucleotide exchange factor (GEF) required for activation of guanine nucleotide-binding proteins (G-proteins) during non-canonical Wnt signaling.
Pssm-ID: 411799 Cd Length: 153 Bit Score: 64.56 E-value: 3.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 18 LIIWLQTFKTASPCQDVK-----QLTNGVTMAQVLHQIDVAWFSEswlsRIKDDVGDNWRIKASNLKKVLHGITSYYHEF 92
Cdd:cd22228 6 LVTWVKTFGPLGFGSEDKlsmymDLVDGVFLNKIMLQIDPRPTNQ----RVNKHVNNDVNLRIQNLTILVRHIKTYYQEV 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568929948 93 LGQQISEELiPDLNQITEcaDPV------ELGRLLQLILGCAVNCEKKQEHIKNIMTLEESVQHVVMTAIQEL 159
Cdd:cd22228 82 LQQLIVMNL-PNVLMIGK--DPLsgksmeEIKKMLLLVLGCAVQCERKEEFIERIKQLDIETQAAIVSHIQEV 151
|
|
| HkD_Girdin |
cd22229 |
Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation ... |
18-159 |
2.11e-10 |
|
Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation enhancer (APE), or coiled-coil domain-containing protein 88A (CCDC88A), or G alpha-interacting vesicle-associated protein (GIV), or Girders of actin filament, or Hook-related protein 1 (HkRP1), is a bifunctional modulator of guanine nucleotide-binding proteins (G proteins). It acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein G(i) alpha subunits. It also acts as a guanine nucleotide dissociation inhibitor for guanine nucleotide-binding protein G(s) subunit alpha GNAS. In addition, Girdin plays an essential role in cell migration.
Pssm-ID: 411800 Cd Length: 156 Bit Score: 59.42 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 18 LIIWLQTF-----KTASPCQDVKQLTNGVTMAQVLHQIDvawfSESWLSRIKDDVGDNWRIKASNLKKVLHGITSYYHEF 92
Cdd:cd22229 9 LVTWVKTFgplatGNGTPLDEYVALVDGVFLNEVMLQIN----PKSSNQRVNKKVNNDASLRIQNLSILVKQIKLYYQET 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568929948 93 LGQQISEELiPDL-----NQITECADPvELGRLLQLILGCAVNCEKKQEHIKNIMTLEESVQHVVMTAIQEL 159
Cdd:cd22229 85 LQQLIMMSL-PNVlvlgrNPLSEQGTE-EMKKLLLLLLGCAVQCERKEEFIERIQTLDFDTKAAVAAHIQEV 154
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
263-533 |
1.32e-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: 61.23 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 263 RLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDV-LRATSDKANKLESTVEVYRQKLQDLNDLRKQV- 340
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqISALRKDLARLEAEVEQLEERIAQLSKELTELe 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 341 KSLQETNMMYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQR 420
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 421 DTLKETNEELRcskAQQDHLNQADASATKSYENLAAEimpveyrevfirLQHEnkmlrLQQEGTENERIEQLQEQLEQKH 500
Cdd:TIGR02168 841 EDLEEQIEELS---EDIESLAAEIEELEELIEELESE------------LEAL-----LNERASLEEALALLRSELEELS 900
|
250 260 270
....*....|....*....|....*....|...
gi 568929948 501 RKMNELETEQRLSKERIGELQQQIEDLQKSLQE 533
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLEG 933
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
276-534 |
2.15e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 276 EELEKQLiefqhrnDELT---SLAEETRALKDEIDVLRA--TSDKANKLESTVEVYRQKLQDL-NDLRKQVKSLQETNMM 349
Cdd:COG1196 196 GELERQL-------EPLErqaEKAERYRELKEELKELEAelLLLKLRELEAELEELEAELEELeAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 350 YMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKETNEE 429
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 430 LrcsKAQQDHLNQADASATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGTENERIEQLQEQLEQkhrKMNELETE 509
Cdd:COG1196 349 A---EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE---RLERLEEE 422
|
250 260
....*....|....*....|....*
gi 568929948 510 QRLSKERIGELQQQIEDLQKSLQEQ 534
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEA 447
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
170-532 |
3.01e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 170 SDTVGELEQQLKRaLEElQEAIAEK-EELKQRCQELDMQVTTLQDEKnsLVSENEMMNEKLDQLDGSFDDPNTMVAKKYF 248
Cdd:COG1196 192 EDILGELERQLEP-LER-QAEKAERyRELKEELKELEAELLLLKLRE--LEAELEELEAELEELEAELEELEAELAELEA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 249 HVQLQLEQLQEENYRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRAtsdkanKLESTVEVYRQ 328
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE------ELEELEEELEE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 329 KLQDLNDLRKQVKSLQEtnmmymhntvSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHET 408
Cdd:COG1196 342 LEEELEEAEEELEEAEA----------ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 409 LLKEKERLIEQRDTLKETNEELRcskAQQDHLNQADASATKSYENLAAEIMpveyrevfirlqhENKMLRLQQEGTENER 488
Cdd:COG1196 412 LLERLERLEEELEELEEALAELE---EEEEEEEEALEEAAEEEAELEEEEE-------------ALLELLAELLEEAALL 475
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 568929948 489 IEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQ 532
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
|
| HkD_Gipie |
cd22230 |
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar ... |
36-159 |
3.95e-09 |
|
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar proteins; Gipie, also called coiled-coil domain-containing protein 88B (CCDC88B), or brain leucine zipper domain-containing protein, or Hook-related protein 3 (HkRP3), is a novel actin cytoskeleton-binding protein and Akt substrate that regulates cell migratory responses in various biological contexts. It acts as a positive regulator of T-cell maturation and inflammatory function. As a microtubule-binding protein, Gipie regulates lytic granule clustering and NK cell killing.
Pssm-ID: 411801 Cd Length: 170 Bit Score: 55.99 E-value: 3.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 36 QLTNGVTMAQVLHQIDVAwfSESWLSRIKDDVGDNWRIKasNLKKVLHGITSYYHEFLGQQISEELiPDL-----NQITE 110
Cdd:cd22230 46 RLSNGDLLNRVMGIIDPS--PRGGPRMRGDDGPAAHRVQ--NLHILWGRLRDFYQEELQQLILSPP-PDLqvmgrDPFTE 120
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 568929948 111 CAdPVELGRLLQLILGCAVNCEKKQEHIKNIMTLEESVQHVVMTAIQEL 159
Cdd:cd22230 121 EA-VQELEKLLRLLLGAAVQCERRELFIRHIQGLDLDVQAELAEAIQEV 168
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
169-430 |
7.96e-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: 58.53 E-value: 7.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 169 ASDTVGELEQQLKRALEELQEAIAEKEELKQRCQELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAKKYF 248
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 249 HVQLQLEQLQEENYRLEAAK----------DDYRVHCEELEKQLIEFQhrnDELTSLAEETRALKDEIDVLRATsdkANK 318
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSedieslaaeiEELEELIEELESELEALL---NERASLEEALALLRSELEELSEE---LRE 905
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 319 LESTVEVYRQKLQDLNDLRKQVK-SLQETNMMYMHNT--------VSLEEELKKANAARAQLETYKRQVQDLHTKLSsES 389
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLElRLEGLEVRIDNLQerlseeysLTLEEAEALENKIEDDEEEARRRLKRLENKIK-EL 984
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 568929948 390 KRADTLAF-EMKRLEEKHETLLKEKERLIEQRDTLKETNEEL 430
Cdd:TIGR02168 985 GPVNLAAIeEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
178-525 |
8.38e-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: 58.53 E-value: 8.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 178 QQLKRALEELQEAIA--EKEELKQRCQELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFddpntmvakkyfhvqlqle 255
Cdd:TIGR02168 216 KELKAELRELELALLvlRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEV------------------- 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 256 qlqeenyrleaakddyrvhcEELEKQLIEFQHRNDELTSLAEEtraLKDEIDVLRATSDKANKLESTVEVYRQKL-QDLN 334
Cdd:TIGR02168 277 --------------------SELEEEIEELQKELYALANEISR---LEQQKQILRERLANLERQLEELEAQLEELeSKLD 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 335 DLRKQVKSLQETNMMYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSE----SKRADTLAFEMKRLEEKHETLL 410
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKvaqlELQIASLNNEIERLEARLERLE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 411 KEKERLIEQRDTLKETNEELRCSKAQQ--DHLNQADASATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGTENER 488
Cdd:TIGR02168 414 DRRERLQQEIEELLKKLEEAELKELQAelEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
|
330 340 350
....*....|....*....|....*....|....*..
gi 568929948 489 IEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIE 525
Cdd:TIGR02168 494 LERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIS 530
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
166-528 |
1.31e-08 |
|
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: 57.82 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 166 ISPASDTVGELEQQLKRALEELQEAiaEKEELKQRCQELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAK 245
Cdd:pfam15921 240 IFPVEDQLEALKSESQNKIELLLQQ--HQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 246 kyfHVQLQLEQLQEENYRLEAAKDDYRVHCEELEKQLI----EFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLES 321
Cdd:pfam15921 318 ---QLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVlansELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELS 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 322 ------------------TVEVYRQKLQD-------LNDLRKQVKSLQETNM-MYMHNTVSLEEELKKANAARAQLETYK 375
Cdd:pfam15921 395 lekeqnkrlwdrdtgnsiTIDHLRRELDDrnmevqrLEALLKAMKSECQGQMeRQMAAIQGKNESLEKVSSLTAQLESTK 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 376 RQVQDLHTKLSSESKRADTlafeMKRLEEKHETLLKEKERLIEQ--------RDTLKETNEELRCSKAQQDHLNQADASA 447
Cdd:pfam15921 475 EMLRKVVEELTAKKMTLES----SERTVSDLTASLQEKERAIEAtnaeitklRSRVDLKLQELQHLKNEGDHLRNVQTEC 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 448 TKSYENLAAEIMPVEyrevFIRLQHENKMLRLQQEGTENERIE----QLQEQLEQKHRKMNELETEQRLSKERIGELQQQ 523
Cdd:pfam15921 551 EALKLQMAEKDKVIE----ILRQQIENMTQLVGQHGRTAGAMQvekaQLEKEINDRRLELQEFKILKDKKDAKIRELEAR 626
|
....*
gi 568929948 524 IEDLQ 528
Cdd:pfam15921 627 VSDLE 631
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
271-534 |
2.86e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 271 YRVHCEELEKQLIEFQHRNDELTSLAEEtraLKDEIDVLRATSDKANKLESTVEVYRQKLQDL--NDLRKQVKSLQETNM 348
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDRLEDILNE---LERQLKSLERQAEKAERYKELKAELRELELALlvLRLEELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 349 MYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLieqRDTLKETNE 428
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL---ERQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 429 ELRCSKAQQDHLNQADASATKSYENLAAEImpVEYREVFIRLQHENKMLrlqqegteNERIEQLQEQLEQKHRKMNELET 508
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEELKEEL--ESLEAELEELEAELEEL--------ESRLEELEEQLETLRSKVAQLEL 393
|
250 260
....*....|....*....|....*.
gi 568929948 509 EQRLSKERIGELQQQIEDLQKSLQEQ 534
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRERL 419
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
173-534 |
1.64e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 173 VGELEQQLKRALEELQEAIAEKEElkqrcQELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAKkyfHVQL 252
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKEE-----KDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEE---HEER 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 253 QLEQLqeenyRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEEtraLKDEIDVLRATSDKANKLESTVEVYRQKLQD 332
Cdd:PRK02224 250 REELE-----TLEAEIEDLRETIAETEREREELAEEVRDLRERLEE---LEEERDDLLAEAGLDDADAEAVEARREELED 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 333 --------LNDLRKQVKSLQETNMMYMHNTVSLEEELKKA-----------NAARAQLETYKRQVQDLHTKLSSESKRAD 393
Cdd:PRK02224 322 rdeelrdrLEECRVAAQAHNEEAESLREDADDLEERAEELreeaaeleselEEAREAVEDRREEIEELEEEIEELRERFG 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 394 TLAFEMKRLEEKHETLLKEKERLIEQRDTLKETNEELRCSKAQQDHLNQADASATKSYENLAAEIMPV--EYREVFIRLQ 471
Cdd:PRK02224 402 DAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETieEDRERVEELE 481
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568929948 472 HENKMLRLQQEGTENE------------RIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQ 534
Cdd:PRK02224 482 AELEDLEEEVEEVEERleraedlveaedRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEK 556
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
368-549 |
2.26e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 368 RAQLETYKRQV------QDLHTKLssESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDT----LKETNEELRCSKAQQ 437
Cdd:TIGR02168 199 ERQLKSLERQAekaeryKELKAEL--RELELALLVLRLEELREELEELQEELKEAEEELEEltaeLQELEEKLEELRLEV 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 438 DHLNQADASATKSYENLAAEIMPVEYREVFIRlqheNKMLRLQQEgtenerIEQLQEQLEQKHRKMNELETEQRLSKERI 517
Cdd:TIGR02168 277 SELEEEIEELQKELYALANEISRLEQQKQILR----ERLANLERQ------LEELEAQLEELESKLDELAEELAELEEKL 346
|
170 180 190
....*....|....*....|....*....|..
gi 568929948 518 GELQQQIEDLQKSLQEQGSKSEGESKSSHAWR 549
Cdd:TIGR02168 347 EELKEELESLEAELEELEAELEELESRLEELE 378
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
317-549 |
3.02e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 317 NKLESTvevyRQKLQDLND----LRKQVKSLQEtnmmymhntvsleeelKKANAARAQleTYKRQVQDLHTKLSSesKRA 392
Cdd:COG1196 179 RKLEAT----EENLERLEDilgeLERQLEPLER----------------QAEKAERYR--ELKEELKELEAELLL--LKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 393 DTLAFEMKRLEEKHETLLKEKERLIEQRDTLKETNEELRcskAQQDHLNQADASATKSYENLAAEImpveyrevfIRLQH 472
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELR---LELEELELELEEAQAEEYELLAEL---------ARLEQ 302
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568929948 473 ENKMLRLQQEGTEnERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQGSKSEGESKSSHAWR 549
Cdd:COG1196 303 DIARLEERRRELE-ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
95-533 |
5.18e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 5.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 95 QQISEELIPDLNQITECADpvELGRLLQLILGCAVNCEKKQEHIKNIMTLEESVQHVVMTAIQELMSKEIVISPASDTVG 174
Cdd:COG1196 368 LEAEAELAEAEEELEELAE--ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 175 ELEQQLKRALEELQEAIAEKEELKQRCQELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAKK-----YFH 249
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAglrglAGA 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 250 VQLQLEQLQEENYRLEAAKDDYRVHC----EELEKQLIEFQHRNDE-----LTSLAEETRALKDEIDVLRATSDKANKLE 320
Cdd:COG1196 526 VAVLIGVEAAYEAALEAALAAALQNIvvedDEVAAAAIEYLKAAKAgratfLPLDKIRARAALAAALARGAIGAAVDLVA 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 321 STVEVYRQKLQDLNDLRKQVKSLQETNMMYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMK 400
Cdd:COG1196 606 SDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA 685
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 401 RLEEKHETLLKE-KERLIEQRDTLKETNEELRCSKAQQDHLNQADASATKSYENLAAEIMPVEYREvfirlqhenkmlrL 479
Cdd:COG1196 686 ERLAEEELELEEaLLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE-------------A 752
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568929948 480 QQEGTENERIEQLQEQLEQKHRKMNELET-------EQRLSKERIGELQQQIEDLQKSLQE 533
Cdd:COG1196 753 LEELPEPPDLEELERELERLEREIEALGPvnllaieEYEELEERYDFLSEQREDLEEARET 813
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
154-533 |
8.11e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.96 E-value: 8.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 154 TAIQELMSKEIVISPASDTVGELEQqLKRALEELQEAIA----EKEELKQRCQELDMQVTTLQDEKNSLVSENEMMNEKL 229
Cdd:PRK02224 231 QARETRDEADEVLEEHEERREELET-LEAEIEDLRETIAeterEREELAEEVRDLRERLEELEEERDDLLAEAGLDDADA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 230 DQLDGSFDDpntmvakkyfhvqlqleqlqeenyrLEAAKDDYRvhcEELEKQLIEFQHRNDELTSLAEETRALKDEIDVL 309
Cdd:PRK02224 310 EAVEARREE-------------------------LEDRDEELR---DRLEECRVAAQAHNEEAESLREDADDLEERAEEL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 310 RatsDKANKLESTVEVYRQKLQD----LNDLRKQVKSLQETnmmYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKL 385
Cdd:PRK02224 362 R---EEAAELESELEEAREAVEDrreeIEELEEEIEELRER---FGDAPVDLGNAEDFLEELREERDELREREAELEATL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 386 SSESKRAdtlafemkrleEKHETLLKEK---------------ERLIEQRDTLKETNEELRCSKAQQDHLNQADASATKS 450
Cdd:PRK02224 436 RTARERV-----------EEAEALLEAGkcpecgqpvegsphvETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 451 YEnLAAEIMPVEyrevfirlqhENKMLRLQQEGTENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKS 530
Cdd:PRK02224 505 VE-AEDRIERLE----------ERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREE 573
|
...
gi 568929948 531 LQE 533
Cdd:PRK02224 574 VAE 576
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
173-534 |
8.30e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 8.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 173 VGELEQQLKRALEELQEAIAEKEELKQRCQELDMQVTTLQDEKNSLVSENEMMNEKLDQldgsfddPNTMVAKKYFHVQL 252
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREY-------EGYELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 253 QLEQLQEENYRLEAAKDDYRVHCEELEKQLIEfqhRNDELTSLAEETRALKDEIDV-----LRATSDKANKLESTVEVYR 327
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEE---IEQLLEELNKKIKDLGEEEQLrvkekIGELEAEIASLERSIAEKE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 328 QKLQDLNDLRKQVKSLQETNMMYMHNtvsLEEELKKANAARAQLET----YKRQVQDLHTKLSSESKRADTLAFEMKRLE 403
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEE---LEREIEEERKRRDKLTEeyaeLKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 404 EKHETLLKEKERLIEQRDTLKETNEELRcskAQQDHLNQADASAtksyenlaaeimpveyrevfirlqhENKMLRLQQEG 483
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQEELQRLS---EELADLNAAIAGI-------------------------EAKINELEEEK 443
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 568929948 484 TE-NERIEQLQEQLEQKHRKMNELETEqrlsKERIGELQQQIEDLQKSLQEQ 534
Cdd:TIGR02169 444 EDkALEIKKQEWKLEQLAADLSKYEQE----LYDLKEEYDRVEKELSKLQRE 491
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
286-533 |
1.13e-06 |
|
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: 51.60 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 286 QHRNDELTSLAEETRALKDEIDVLRATSDKA-NKLESTVEVYRQKLQDLNDLRKQVKSLQEtnmmymhntvSLEEELKKA 364
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAELrKELEELEEELEQLRKELEELSRQISALRK----------DLARLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 365 NAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKETNEELRcskAQQDHLNQAD 444
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR---AELTLLNEEA 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 445 ASATKSYENLAAEIMPVEYREVFIRLQHENKmlrlqqegteNERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQI 524
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEEQIEEL----------SEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
....*....
gi 568929948 525 EDLQKSLQE 533
Cdd:TIGR02168 890 ALLRSELEE 898
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
132-534 |
1.39e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 132 EKKQEHIKNIMTLEESVQhvvmtAIQELMSKEivispasdtvGELEQQLKR-ALEELQEAIAEKEELKQRCQELDMQVTT 210
Cdd:PRK03918 345 KKLKELEKRLEELEERHE-----LYEEAKAKK----------EELERLKKRlTGLTPEKLEKELEELEKAKEEIEEEISK 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 211 LQDEKNSLVSENEMMNEKLDQLDGS-----------FDDPNTMVAKKYfhvQLQLEQLQEENYRLEAAKDDYRVHCEELE 279
Cdd:PRK03918 410 ITARIGELKKEIKELKKAIEELKKAkgkcpvcgrelTEEHRKELLEEY---TAELKRIEKELKEIEEKERKLRKELRELE 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 280 KQLIEfQHRNDELTSLAEETRALKDEIDVLratsdKANKLESTVEVYRQKLQDLNDLRKQVKSLqetnmmymhntvslEE 359
Cdd:PRK03918 487 KVLKK-ESELIKLKELAEQLKELEEKLKKY-----NLEELEKKAEEYEKLKEKLIKLKGEIKSL--------------KK 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 360 ELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEM-------------------------KRLEEKHETLLKEKE 414
Cdd:PRK03918 547 ELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESveeleerlkelepfyneylelkdaeKELEREEKELKKLEE 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 415 RLIEQRDTLKETNEELRCSKAQQDHLNQadASATKSYENLaaeimpveyREVFIRLQHENKMLRLQQEGTENER------ 488
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEELEK--KYSEEEYEEL---------REEYLELSRELAGLRAELEELEKRReeikkt 695
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 568929948 489 IEQLQEQLEQKHRKMNELETEQRlSKERIGELQQQIEDLQKSLQEQ 534
Cdd:PRK03918 696 LEKLKEELEEREKAKKELEKLEK-ALERVEELREKVKKYKALLKER 740
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
196-529 |
1.40e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.22 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 196 ELKQRCQELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAKKYFHVQLQLEQLQEENYRLEAAKDDYRVHC 275
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 276 EELEKQLIEFQHRNDELTSLAEETRALKDEIDVLratsdKANKLESTVEVYRQKLQDLND-LRKQVKSLQETNmmymhnt 354
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELEEDLHKLEEALNDL-----EARLSHSRIPEIQAELSKLEEeVSRIEARLREIE------- 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 355 VSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKETNEELRCS- 433
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQl 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 434 KAQQDHLNQADASATKSYEN---LAAEIMPVEYREVFIrlqhENKMLRLQQEGTENERIEQLQEQLEQKHRKMNELET-- 508
Cdd:TIGR02169 899 RELERKIEELEAQIEKKRKRlseLKAKLEALEEELSEI----EDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPvn 974
|
330 340
....*....|....*....|....*.
gi 568929948 509 -----EQRLSKERIGELQQQIEDLQK 529
Cdd:TIGR02169 975 mlaiqEYEEVLKRLDELKEKRAKLEE 1000
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
414-534 |
1.97e-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: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 414 ERLIEQRDTLKETNEELRCSKAQQDHLNQADASATKsYENLAAEIMPVEYREVFIRLQHENKMLRLQQEgteneRIEQLQ 493
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLEPIRELAER-YAAARERLAELEYLRAALRLWFAQRRLELLEA-----ELEELR 301
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 568929948 494 EQLEQKHRKMNELETEQRLSKE---------------RIGELQQQIEDLQKSLQEQ 534
Cdd:COG4913 302 AELARLEAELERLEARLDALREeldeleaqirgnggdRLEQLEREIERLERELEER 357
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
273-533 |
2.37e-06 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 50.31 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 273 VHCEELEKQLIEFQHRndELTSLAEEtraLKDEIDVLRATSDKANKLESTVEVYrqKLQDLNDLRKQVKSlqetnmmymh 352
Cdd:PRK05771 31 VHIEDLKEELSNERLR--KLRSLLTK---LSEALDKLRSYLPKLNPLREEKKKV--SVKSLEELIKDVEE---------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 353 NTVSLEEELKKANAARAQLETYKRqvqdlhtKLSSESKRADTL-AFEmkrLEEKhetLLKEKERLIEQRDTLKETNEELr 431
Cdd:PRK05771 94 ELEKIEKEIKELEEEISELENEIK-------ELEQEIERLEPWgNFD---LDLS---LLLGFKYVSVFVGTVPEDKLEE- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 432 cSKAQQDHLNQADASATKSYENLAAeIMPVEYREVFIRL--QHENKMLRLQQEGTENERIEQLQEQLEQKHRKMNELete 509
Cdd:PRK05771 160 -LKLESDVENVEYISTDKGYVYVVV-VVLKELSDEVEEElkKLGFERLELEEEGTPSELIREIKEELEEIEKERESL--- 234
|
250 260
....*....|....*....|....
gi 568929948 510 qrlsKERIGELQQQIEDLQKSLQE 533
Cdd:PRK05771 235 ----LEELKELAKKYLEELLALYE 254
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
134-526 |
2.60e-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: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 134 KQEHIKNIMTLEESVQHVVMTAIQE---LMSKEIVISPASDTVGELEQQLKRALEELQEAIAEKEELKQRCQELDMQVTT 210
Cdd:pfam05483 228 EEEYKKEINDKEKQVSLLLIQITEKenkMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQR 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 211 LQDEKNSLVSENEMMNEKLDQL----DGSFDDPNTMVAKKYFHVQLQLEQL-------QEENYRLEAAKDDYRVHCEELE 279
Cdd:pfam05483 308 SMSTQKALEEDLQIATKTICQLteekEAQMEELNKAKAAHSFVVTEFEATTcsleellRTEQQRLEKNEDQLKIITMELQ 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 280 KQLIEFQH-----RNDEL------TSLAEETRALKDEIDVLRATSDKANKLESTVEVYRQKLQDLNDLRKQVKSLQETNM 348
Cdd:pfam05483 388 KKSSELEEmtkfkNNKEVeleelkKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 349 MYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSEskrADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKETNE 428
Cdd:pfam05483 468 HYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQE---ASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEM 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 429 ELR-----CSKAQQDHLNQADASATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGTENERIEQLQE--------- 494
Cdd:pfam05483 545 NLRdelesVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQenkalkkkg 624
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 568929948 495 -----QLEQKHRKMNELETEQRLSKERIGEL----QQQIED 526
Cdd:pfam05483 625 saenkQLNAYEIKVNKLELELASAKQKFEEIidnyQKEIED 665
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
311-533 |
3.02e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 311 ATSDKANKLESTVEVYRQKLQDLNDLRKQVKSLQEtnmmymhntvSLEEELKKANAARAQLEtykRQVQDLHTKLSSESK 390
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEK----------ALLKQLAALERRIAALA---RRIRALEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 391 RADTLAFEMKRLEEKHETLLKEKERLI------EQRDTLK-----ETNEELRCSKAQQDHLNQADASATKSYENLAAEIm 459
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKEELAELLralyrlGRQPPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL- 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568929948 460 pveyREVFIRLQHENKMLRLQQEGTENERiEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQE 533
Cdd:COG4942 163 ----AALRAELEAERAELEALLAELEEER-AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
169-533 |
1.67e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 169 ASDTVGELEQQLKRALEELQEAIAEKEELKQRCQELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMvAKKYF 248
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL-KEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 249 HVQLQLEQLQEENYRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSL---AEETRALKDE----IDVLRATSDKANKLES 321
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELkekAEEYIKLSEFyeeyLDELREIEKRLSRLEE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 322 TVEVYRQKLQDLNDLRKQVKSLQETNMMYMHNTVSLEEELKKANAARAQLEtykrQVQDLHTKLSSES-----KRADTLA 396
Cdd:PRK03918 322 EINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE----ELERLKKRLTGLTpekleKELEELE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 397 FEMKRLEEKHETLLKEKERLIEQRDTLKETNEELRCSKAQ---------QDHLNQADASATKSYENLAAEI--------- 458
Cdd:PRK03918 398 KAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgreltEEHRKELLEEYTAELKRIEKELkeieekerk 477
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568929948 459 MPVEYREVFIRLQHENKMLRLQQEGtenERIEQLQEQLEQ-KHRKMNELETEQRLSKERIGELQQQIEDLQKSLQE 533
Cdd:PRK03918 478 LRKELRELEKVLKKESELIKLKELA---EQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEK 550
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
132-533 |
2.05e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 132 EKKQEHIKNIMTLEESVQHVVMTAIQELMSKEIVISPASDTVGELEQQLKRALEELQEAIAEKE---ELKQRCQELDMQV 208
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEeieELEKELESLEGSK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 209 TTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTM--VAKKYFHVQLQLEQLQEENYRLEAAKDDYRVHCEELEKQLIEFQ 286
Cdd:PRK03918 255 RKLEEKIRELEERIEELKKEIEELEEKVKELKELkeKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 287 HRNDELTSLAEETRALKDEIDVLRatsdkanKLESTVEVYRQKLQDLNDLRKQVKSLQETNMMYMHNTVS-----LEEEL 361
Cdd:PRK03918 335 EKEERLEELKKKLKELEKRLEELE-------ERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEkakeeIEEEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 362 KKANAARAQLETYKRQVQDLHTKLSS-------------ESKRADTLA----------FEMKRLEEKHETLLKEKERLIE 418
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKKakgkcpvcgreltEEHRKELLEeytaelkrieKELKEIEEKERKLRKELRELEK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 419 QRD------TLKETNEELRCSKAQQDHLNQADASA-TKSYENLaaeimpveyREVFIRLQHENKMLRlqqegTENERIEQ 491
Cdd:PRK03918 488 VLKkeseliKLKELAEQLKELEEKLKKYNLEELEKkAEEYEKL---------KEKLIKLKGEIKSLK-----KELEKLEE 553
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 568929948 492 LQEQLEQKHRKMNELETEQRLSKERIGELQ-QQIEDLQKSLQE 533
Cdd:PRK03918 554 LKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKE 596
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
177-533 |
2.20e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 177 EQQLKRALEELQEAIAEKEELKQRCQELDMQVTTLQDEKNSLvsenemmnEKLDQLDGSFDDpntmvakkyfhvqlqleq 256
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL--------QRLAEYSWDEID------------------ 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 257 lqeenyrleaakddyrvhceelekqliefqhrndeLTSLAEETRALKDEIDVLRATSDKANKLESTVEVYRQKLQDLNDL 336
Cdd:COG4913 663 -----------------------------------VASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEE 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 337 RKQvkslqetnmmymhntvsLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKE-KER 415
Cdd:COG4913 708 LDE-----------------LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERElREN 770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 416 LIEQRDTLKETNEELRcskaqqDHLNQADASATKSYENLAAEIMPV-----EYREVFIRLQ------HENKMLRLQQEgT 484
Cdd:COG4913 771 LEERIDALRARLNRAE------EELERAMRAFNREWPAETADLDADleslpEYLALLDRLEedglpeYEERFKELLNE-N 843
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 568929948 485 ENERIEQLQEQLEQKHRkmneleteqrlskerigELQQQIEDLQKSLQE 533
Cdd:COG4913 844 SIEFVADLLSKLRRAIR-----------------EIKERIDPLNDSLKR 875
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
169-425 |
2.92e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 169 ASDTVGELEQQLKRALEELQEAIAEKEELKQRCQELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFddpntmvakkyf 248
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL------------ 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 249 hvqlqleqlqeenyrleaakddyrvhcEELEKQLIEFQHRNDELtsLAEETRALKDEIDVLRATSDKANKLESTVEVYRQ 328
Cdd:COG1196 361 ---------------------------AEAEEALLEAEAELAEA--EEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 329 KLQDLNDLRKQVKSLQEtnmmymhntvSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHET 408
Cdd:COG1196 412 LLERLERLEEELEELEE----------ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
250
....*....|....*..
gi 568929948 409 LLKEKERLIEQRDTLKE 425
Cdd:COG1196 482 LLEELAEAAARLLLLLE 498
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
290-533 |
4.34e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 290 DELTSLAEETRALKDEI------DVLRATSDKANKLESTVEVYRQKLQDLNDLRK--QVKSLQETNMMYMH--------- 352
Cdd:COG3206 71 SGLSSLSASDSPLETQIeilksrPVLERVVDKLNLDEDPLGEEASREAAIERLRKnlTVEPVKGSNVIEISytspdpela 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 353 ----NTVS---LEE--ELKKANAARA------QLETYKRQVQDLHTKLSSESKRADTLAfemkrLEEKHETLLkekERLI 417
Cdd:COG3206 151 aavaNALAeayLEQnlELRREEARKAlefleeQLPELRKELEEAEAALEEFRQKNGLVD-----LSEEAKLLL---QQLS 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 418 EQRDTLKETNEELRCSKAQQDHLNQADASATKSYENLAAEIMPVEYREVFIRLqhENKMLRLQQEGTEN--------ERI 489
Cdd:COG3206 223 ELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAEL--EAELAELSARYTPNhpdvialrAQI 300
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 568929948 490 EQLQEQLEQKHRK-MNELETEQRLSKERIGELQQQIEDLQKSLQE 533
Cdd:COG3206 301 AALRAQLQQEAQRiLASLEAELEALQAREASLQAQLAQLEARLAE 345
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
359-534 |
5.77e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 5.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 359 EELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLiEQRDTLKETNEELRCSKAQQD 438
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL-PLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 439 HLNQADasatKSYENLAAEImpVEYREVFIRLQHENKMLRLQQEGTENERIEQLQEQLEQKHRKMNELETEQRLSKERIG 518
Cdd:COG4717 150 ELEERL----EELRELEEEL--EELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170
....*....|....*.
gi 568929948 519 ELQQQIEDLQKSLQEQ 534
Cdd:COG4717 224 ELEEELEQLENELEAA 239
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
263-534 |
6.02e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 263 RLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETraLKDEIDVLRATSDKANKLESTVevyRQKLQDLNDLRKQVKS 342
Cdd:PRK04863 855 DHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADET--LADRVEEIREQLDEAEEAKRFV---QQHGNALAQLEPIVSV 929
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 343 LQETNMMYmhntvsleEELKKA-NAARAQLETYKRQVQDLhtklSSESKRADTLAFE--MKRLEEKHETLLKEKERLIEQ 419
Cdd:PRK04863 930 LQSDPEQF--------EQLKQDyQQAQQTQRDAKQQAFAL----TEVVQRRAHFSYEdaAEMLAKNSDLNEKLRQRLEQA 997
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 420 RDTLKETNEELRCSKAQQDHLNQADASATKSYENlaaeimpveYREVFIRLQHENKMLRLQ-QEGTEN---ERIEQLQEQ 495
Cdd:PRK04863 998 EQERTRAREQLRQAQAQLAQYNQVLASLKSSYDA---------KRQMLQELKQELQDLGVPaDSGAEErarARRDELHAR 1068
|
250 260 270
....*....|....*....|....*....|....*....
gi 568929948 496 LEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQ 534
Cdd:PRK04863 1069 LSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEM 1107
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
298-529 |
8.24e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 8.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 298 ETRALKDEIDVLRATSDKANKLESTVEVYRQKLQDLNDLRKQVKSLQEtnmmymhntvsLEEELKKANAARAQLETYKRQ 377
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALEDAREQIELLEPIRELAERYAA-----------ARERLAELEYLRAALRLWFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 378 --VQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQR-----DTLKETNEELRcskAQQDHLNQADASATKs 450
Cdd:COG4913 288 rrLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrgnggDRLEQLEREIE---RLERELEERERRRAR- 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 451 YENLAAEI-MPVEY-REVFIRLQHENKMLRlqqegtenERIEQLQEQLEQKHRkmnELETEQRLSKERIGELQQQIEDLQ 528
Cdd:COG4913 364 LEALLAALgLPLPAsAEEFAALRAEAAALL--------EALEEELEALEEALA---EAEAALRDLRRELRELEAEIASLE 432
|
.
gi 568929948 529 K 529
Cdd:COG4913 433 R 433
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
327-559 |
8.41e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 8.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 327 RQKLQDLNDLRKQVKSLQETnmmymhntvsLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKH 406
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKE----------LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 407 ETLlkeKERLIEQRDTLKEtneelRCSKAQQDHLNQADASATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGTEN 486
Cdd:COG4942 93 AEL---RAELEAQKEELAE-----LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568929948 487 ERiEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQGSKSEGESKSSHAWRHLICAYIRPA 559
Cdd:COG4942 165 LR-AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
131-533 |
1.41e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 131 CEKKQEHIKNIMTLEESVQHVVMTAIQELMSKEIVISPASDTVGELEQQLKRALEELQEAIaekEELKQRCQELDMQVTT 210
Cdd:PRK02224 270 TEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRL---EECRVAAQAHNEEAES 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 211 LQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAKKYFHVQLQLEQLQEenyrLEAAKDDYRVHCEELEKQLIEFQHRND 290
Cdd:PRK02224 347 LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE----LRERFGDAPVDLGNAEDFLEELREERD 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 291 ELTSLAEETRAlkdEIDVLRATSDKANKLE------------------STVEVYRQKLQDLNDLRKQVKSLQETNMMYMH 352
Cdd:PRK02224 423 ELREREAELEA---TLRTARERVEEAEALLeagkcpecgqpvegsphvETIEEDRERVEELEAELEDLEEEVEEVEERLE 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 353 NTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLE----EKHETLLKEKERLIEQRDTLKETNE 428
Cdd:PRK02224 500 RAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEaeaeEKREAAAEAEEEAEEAREEVAELNS 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 429 ELRCSKAQQDHLNQADASATKsYENLAAEI------------MPVEYREvfiRLQHENKMLRLQQEGTENERIEQLQEQL 496
Cdd:PRK02224 580 KLAELKERIESLERIRTLLAA-IADAEDEIerlrekrealaeLNDERRE---RLAEKRERKRELEAEFDEARIEEAREDK 655
|
410 420 430
....*....|....*....|....*....|....*..
gi 568929948 497 EQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQE 533
Cdd:PRK02224 656 ERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEE 692
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
169-420 |
1.88e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 169 ASDTVGELEQQLKRALEELQEAIAEKEELKQRCQELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTmvakkyf 248
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 249 hvqlqleqlqeenyRLEAAKDDYRVHCEELEKQLIEFQ--HRNDELTSLAEETRALkDEIDVLRATSDKANKLESTVEVY 326
Cdd:COG4942 91 --------------EIAELRAELEAQKEELAELLRALYrlGRQPPLALLLSPEDFL-DAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 327 RQKLQDLNDLRKQVKSLQETnmmymhntvsLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKH 406
Cdd:COG4942 156 RADLAELAALRAELEAERAE----------LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
250
....*....|....
gi 568929948 407 ETLLKEKERLIEQR 420
Cdd:COG4942 226 EALIARLEAEAAAA 239
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
172-534 |
1.96e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 172 TVGELEQQLKRALEELQEAIAEKEELKQRCQELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAKKY---- 247
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSglsg 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 248 FHVQLQLEQLQEENYR------LEAAKDDYRVHCEELEKQLIEFQHRNdeltslaEETRALKDEIDVLRATSDKANKLES 321
Cdd:TIGR02168 521 ILGVLSELISVDEGYEaaieaaLGGRLQAVVVENLNAAKKAIAFLKQN-------ELGRVTFLPLDSIKGTEIQGNDREI 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 322 tVEVYRQKLQDLNDLRKQVKSLQEtNMMYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSE------SKRADTL 395
Cdd:TIGR02168 594 -LKNIEGFLGVAKDLVKFDPKLRK-ALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGgvitggSAKTNSS 671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 396 AFEMKRLEEKHETLLKEKERLIEqrdtlkETNEELRCSKAQQDHLNQADASATKSYENLAAEIMPVEYREVFIRLQHENK 475
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIA------ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 568929948 476 MLRLQQEgteNERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQ 534
Cdd:TIGR02168 746 EERIAQL---SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL 801
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
169-533 |
2.13e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 169 ASDTVGELEQQL---KRALEELQEAI----AEKEELKQRCQELDMQVTTLQDEKNsLVSENEMMNEKLDQLDGSFDDPNT 241
Cdd:PRK04863 284 HLEEALELRRELytsRRQLAAEQYRLvemaRELAELNEAESDLEQDYQAASDHLN-LVQTALRQQEKIERYQADLEELEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 242 MVAKKYFHVQLQLEQLQEENYRLEAAKDDYrvhcEELEKQLIEFQHRNDELtslaeETRALK--------DEIDVLRATS 313
Cdd:PRK04863 363 RLEEQNEVVEEADEQQEENEARAEAAEEEV----DELKSQLADYQQALDVQ-----QTRAIQyqqavqalERAKQLCGLP 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 314 D-KANKLESTVEVYRQKLQDLNDLRKQvkslqetnmmymhntvsLEEELKKANAARAQLEtykrQVQDLHTKLSSESKRA 392
Cdd:PRK04863 434 DlTADNAEDWLEEFQAKEQEATEELLS-----------------LEQKLSVAQAAHSQFE----QAYQLVRKIAGEVSRS 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 393 DtlAFEMKR-LEEKHETLLKEKERLIEQRDTLKEtneelrcskAQQDHLNQADAsatksyenlaaeimpveyrevfIRLQ 471
Cdd:PRK04863 493 E--AWDVAReLLRRLREQRHLAEQLQQLRMRLSE---------LEQRLRQQQRA----------------------ERLL 539
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568929948 472 HENKMlRLQQEGTENERIEQLQEQLEQKhrkMNELETEQRLSKERIGELQQQIEDLQKSLQE 533
Cdd:PRK04863 540 AEFCK-RLGKNLDDEDELEQLQEELEAR---LESLSESVSEARERRMALRQQLEQLQARIQR 597
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
338-552 |
2.48e-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: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 338 KQVKSLQE--TNMMymhntvsLEEE--LKKANAARAQLETYKRqvqdLHTKLSSESKRADTLAfEMKRLEEKHETLLKEK 413
Cdd:COG4913 204 KPIGDLDDfvREYM-------LEEPdtFEAADALVEHFDDLER----AHEALEDAREQIELLE-PIRELAERYAAARERL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 414 ERLIEQRDTLK--ETNEELRCSKAQQDHLNQADASATKSYENLAAEImpveyrevfIRLQHENKMLRLQQEGTENERIEQ 491
Cdd:COG4913 272 AELEYLRAALRlwFAQRRLELLEAELEELRAELARLEAELERLEARL---------DALREELDELEAQIRGNGGDRLEQ 342
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568929948 492 LQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQGSKSEGESKSSHAWRHLI 552
Cdd:COG4913 343 LEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEAL 403
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
357-534 |
2.52e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 357 LEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKE----KERLIEQRDTLKETNEELRC 432
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeaEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 433 SKAQQDHLNQADASatksyENLAAEIMPVEYREVFIRlqHENKMLRLQQEgtENERIEQLQEQLEQKHRKMNELETEQRL 512
Cdd:COG3883 98 SGGSVSYLDVLLGS-----ESFSDFLDRLSALSKIAD--ADADLLEELKA--DKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180
....*....|....*....|..
gi 568929948 513 SKERIGELQQQIEDLQKSLQEQ 534
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAE 190
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
263-533 |
2.54e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 263 RLEAAKDDYRVHCEELEKQLIEfQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEVYRQKLQDLNDLRKQVKS 342
Cdd:PTZ00121 1225 KAEAVKKAEEAKKDAEEAKKAE-EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKK 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 343 LQETNMMyMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDT 422
Cdd:PTZ00121 1304 ADEAKKK-AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA 1382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 423 LKETNEELRCS----------KAQQDHLNQADASATKSYE--NLAAEIMPVEyrEVFIRLQHENKMLRLQQEGTENERIE 490
Cdd:PTZ00121 1383 AKKKAEEKKKAdeakkkaeedKKKADELKKAAAAKKKADEakKKAEEKKKAD--EAKKKAEEAKKADEAKKKAEEAKKAE 1460
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 568929948 491 QLQEQLEQKhRKMNELETEQRlSKERIGELQQQIEDLQKSLQE 533
Cdd:PTZ00121 1461 EAKKKAEEA-KKADEAKKKAE-EAKKADEAKKKAEEAKKKADE 1501
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
177-456 |
2.64e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 177 EQQLKRALEELQEAIAEKEELKQRCQELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGsfddpntmvakkyfhvqlqleq 256
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA---------------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 257 lqeenyRLEAAKDDYRVHCEELEKQLIEFQhRNDELTSLAEEtralkdeidVLRATS-----DKANKLESTVEVYRQKLQ 331
Cdd:COG3883 73 ------EIAEAEAEIEERREELGERARALY-RSGGSVSYLDV---------LLGSESfsdflDRLSALSKIADADADLLE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 332 DLNDLRKQVKSLQEtnmmymhntvSLEEELKKANAARAQLETYKRQVQdlhTKLSSESKRADTLAFEMKRLEEKHETLLK 411
Cdd:COG3883 137 ELKADKAELEAKKA----------ELEAKLAELEALKAELEAAKAELE---AQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 568929948 412 EKERLIEQRDTLKETNEELRCSKAQQDHLNQADASATKSYENLAA 456
Cdd:COG3883 204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
269-533 |
2.70e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 269 DDYRVHCEELEKQLIEFQHRNDELTS---LAEETRALKDEIDVLRATSDKANKL----ESTVEVYRQKLQDLN----DLR 337
Cdd:PRK02224 471 EEDRERVEELEAELEDLEEEVEEVEErleRAEDLVEAEDRIERLEERREDLEELiaerRETIEEKRERAEELReraaELE 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 338 KQVKSLQETNMMYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLI 417
Cdd:PRK02224 551 AEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLA 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 418 EQRD---TLKETNEELRCSKAQQDHlnqadASATKSYENLAAEIMpvEYREVFIRLQH-----ENKMLRLQQEGTENERI 489
Cdd:PRK02224 631 EKRErkrELEAEFDEARIEEAREDK-----ERAEEYLEQVEEKLD--ELREERDDLQAeigavENELEELEELRERREAL 703
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 568929948 490 EQLQEQLEQKHrkmNELETEQRLSKERIGELQQQ-IEDLQKSLQE 533
Cdd:PRK02224 704 ENRVEALEALY---DEAEELESMYGDLRAELRQRnVETLERMLNE 745
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
176-533 |
3.64e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.42 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 176 LEQQLKRALEELQEAIAEKEELKQRCQELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAKKYFHVQLQLE 255
Cdd:TIGR00618 533 GEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLAC 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 256 QLQEENYRLEAAKDDYRVHCEELEKQLiEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTvevyRQKLQDLND 335
Cdd:TIGR00618 613 EQHALLRKLQPEQDLQDVRLHLQQCSQ-ELALKLTALHALQLTLTQERVREHALSIRVLPKELLASR----QLALQKMQS 687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 336 LRKQVKSLQETnmmymhntvsLEEELKKANAARAQLETYKRQVQDL----HTKLSSESKRADTLAFEMKRLEEKHETLLK 411
Cdd:TIGR00618 688 EKEQLTYWKEM----------LAQCQTLLRELETHIEEYDREFNEIenasSSLGSDLAAREDALNQSLKELMHQARTVLK 757
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 412 EKErLIEQRDTLKETNEELRcsKAQQDHLNQADASATKSYENLAAEIMPVEyREVFIRLQHENKMLRLQQEGTENERiEQ 491
Cdd:TIGR00618 758 ART-EAHFNNNEEVTAALQT--GAELSHLAAEIQFFNRLREEDTHLLKTLE-AEIGQEIPSDEDILNLQCETLVQEE-EQ 832
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 568929948 492 LQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQE 533
Cdd:TIGR00618 833 FLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQL 874
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
132-431 |
4.19e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 132 EKKQEHIKNIMTLEESVQHVVMTAIQELMSKEIVISPASDTVGELEQQLKRALEELQEAIAEKEELKQRCQEldmqvttL 211
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQI-------L 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 212 QDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAkkyfhvqlqleqlqeenyRLEAAKDDYRVHCEELEKQLIEFQHRNDE 291
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELESKLDELAEELA------------------ELEEKLEELKEELESLEAELEELEAELEE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 292 LTS----LAEETRALKDEIDVLRAtsdKANKLESTVEVYRQKLQDLNDLRKQVKSLQEtnmmymhntvSLEEELKKAnaa 367
Cdd:TIGR02168 370 LESrleeLEEQLETLRSKVAQLEL---QIASLNNEIERLEARLERLEDRRERLQQEIE----------ELLKKLEEA--- 433
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568929948 368 raqletykrQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKETNEELR 431
Cdd:TIGR02168 434 ---------ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
276-529 |
4.59e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.59 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 276 EELEKQLIEFQHRNDELTSLAEETRALKDE-IDVLRATSDKANKLESTVEVYRQKLQDLNDLRK----QVKSLQEtnmmy 350
Cdd:COG1340 4 DELSSSLEELEEKIEELREEIEELKEKRDElNEELKELAEKRDELNAQVKELREEAQELREKRDelneKVKELKE----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 351 mhntvSLEEELKKANAARAQLETYKRQVQDLHTKLSSEskraDTLAFEMKRLEEKHET--LLKEKER-LIEQRDTLKETN 427
Cdd:COG1340 79 -----ERDELNEKLNELREELDELRKELAELNKAGGSI----DKLRKEIERLEWRQQTevLSPEEEKeLVEKIKELEKEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 428 EELRCSKAQQDHLNQADASATKSYENLAAEIMPV-EYREvfIRLQHENKMLRLQQEGTE-NERIEQLQEQLEQKHRKMNE 505
Cdd:COG1340 150 EKAKKALEKNEKLKELRAELKELRKEAEEIHKKIkELAE--EAQELHEEMIELYKEADElRKEADELHKEIVEAQEKADE 227
|
250 260
....*....|....*....|....
gi 568929948 506 LETEQRLSKERIGELQQQIEDLQK 529
Cdd:COG1340 228 LHEEIIELQKELRELRKELKKLRK 251
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
286-528 |
5.39e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 286 QHRNDELTSLAEETRALKDEIDVLRAtsdKANKLESTVEVYRQKlQDLNDLRKQVKSLQEtnmmymhNTVSLEEELKKAN 365
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRK---ELEEAEAALEEFRQK-NGLVDLSEEAKLLLQ-------QLSELESQLAEAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 366 AARAQLETYKRQVQdlhtKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKETNEELRCSKAQQDHLNQada 445
Cdd:COG3206 233 AELAEAEARLAALR----AQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRA--- 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 446 satksyeNLAAEImpveyREVFIRLQHENKMLRlQQEGTENERIEQLQEQLE---QKHRKMNELETEQRLSKERIGELQQ 522
Cdd:COG3206 306 -------QLQQEA-----QRILASLEAELEALQ-AREASLQAQLAQLEARLAelpELEAELRRLEREVEVARELYESLLQ 372
|
....*.
gi 568929948 523 QIEDLQ 528
Cdd:COG3206 373 RLEEAR 378
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
291-527 |
7.23e-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: 42.63 E-value: 7.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 291 ELTSLAEETRALKDEIDVLRATSdkaNKLESTVEVYRQKLQDLNDLRKQVKSLQETNMMymHNTVSLEEELKKANAARAQ 370
Cdd:COG3096 837 ELAALRQRRSELERELAQHRAQE---QQLRQQLDQLKEQLQLLNKLLPQANLLADETLA--DRLEELREELDAAQEAQAF 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 371 LETYKRQVQDLHTKLSSeskradtlafeMKRLEEKHETLLKEKERLIEQRDTLKETNEELRCSKAQQDHLNQADASAtks 450
Cdd:COG3096 912 IQQHGKALAQLEPLVAV-----------LQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSYEDAVG--- 977
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568929948 451 yenlaaeiMPVEYREVFIRLQHenKMLRLQQEGTE-NERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDL 527
Cdd:COG3096 978 --------LLGENSDLNEKLRA--RLEQAEEARREaREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEEL 1045
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
263-457 |
7.68e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 7.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 263 RLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIdvlRATSDKANKLESTVEVYRQKLQDLN-DLRKQVK 341
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI---RALEQELAALEAELAELEKEIAELRaELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 342 SLQE-TNMMYMHNTVSLEEELKKANAARAQLetykRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQR 420
Cdd:COG4942 105 ELAElLRALYRLGRQPPLALLLSPEDFLDAV----RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 568929948 421 DTLKETNEELRCSKAQQDHLNQADASATKSYENLAAE 457
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
428-534 |
8.81e-04 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 42.28 E-value: 8.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 428 EELRcsKAQQDHLNQAdasATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGTENERIEQLQEQLEQKHRKMNELE 507
Cdd:pfam13779 516 QELR--EALDDYMQAL---AEQAQQNPQDLQQPDDPNAQEMTQQDLQRMLDRIEELARSGRRAEAQQMLSQLQQMLENLQ 590
|
90 100
....*....|....*....|....*....
gi 568929948 508 TEQR--LSKERIGELQQQIEDLQKSLQEQ 534
Cdd:pfam13779 591 AGQPqqQQQQGQSEMQQAMDELGDLLREQ 619
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
180-533 |
8.90e-04 |
|
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: 42.31 E-value: 8.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 180 LKRALEELQEAIAEKEELKQRCQELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAKKYFHVQLQLEQLqe 259
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKI-- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 260 enyrleaakddyrvhcEELEKQLIEFQHRNDELTSLAEE--TRALKDEIDvlratsDKANKLESTVEVYRQKLQDLNDLR 337
Cdd:TIGR04523 284 ----------------KELEKQLNQLKSEISDLNNQKEQdwNKELKSELK------NQEKKLEEIQNQISQNNKIISQLN 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 338 KQVKSLQETNMMYMHNTVSLEEELKKANAA-----------RAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKH 406
Cdd:TIGR04523 342 EQISQLKKELTNSESENSEKQRELEEKQNEieklkkenqsyKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEK 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 407 ETLLKEKERLIEQRDTLKETNEElrcskaqqdhLNQADASATKSYENLaaeimpveyrEVFIRLQHENKMLRLQQEGTEN 486
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNNSEIKD----------LTNQDSVKELIIKNL----------DNTRESLETQLKVLSRSINKIK 481
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 568929948 487 ERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQE 533
Cdd:TIGR04523 482 QNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEK 528
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
165-533 |
1.02e-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: 42.04 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 165 VISPASDTVGELEQQLKRALEELQEAIAEKEELKQRCQELDMQvttlqdeknslVSENEMMNEKLDQLDGSFDDPNTMVA 244
Cdd:pfam05557 105 VISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAK-----------ASEAEQLRQNLEKQQSSLAEAEQRIK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 245 KKYFHVQLQLEQLQEenyrLEAAKDDYrVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRA-------TSDKAN 317
Cdd:pfam05557 174 ELEFEIQSQEQDSEI----VKNSKSEL-ARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRklereekYREEAA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 318 KLESTVEVYRQKLQ-----------DLN---DLRKQVKSLQETNMMYMHNTVSLEEELKKANAARAQLETYKRQVQDLHT 383
Cdd:pfam05557 249 TLELEKEKLEQELQswvklaqdtglNLRspeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIE 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 384 KLSSESKRADTLAfemKRLEEKHETLLKEkerlieqRDTLKETNEELrcskaqQDHLNQADASATKSYENLAAEIMPVEY 463
Cdd:pfam05557 329 DLNKKLKRHKALV---RRLQRRVLLLTKE-------RDGYRAILESY------DKELTMSNYSPQLLERIEEAEDMTQKM 392
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 464 REVFIRLQHenKMLRLQQEGTENERIEQLQEQlEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQE 533
Cdd:pfam05557 393 QAHNEEMEA--QLSVAEEELGGYKQQAQTLER-ELQALRQQESLADPSYSKEEVDSLRRKLETLELERQR 459
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
265-534 |
1.06e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 265 EAAKDDYRVHCEELEKQlIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEVYRqKLQDLNDLRKQVKSLQ 344
Cdd:PTZ00121 1370 EKKKEEAKKKADAAKKK-AEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK-KADEAKKKAEEAKKAD 1447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 345 ETNmmymhntvSLEEELKKANAARAQLETyKRQVQDLHTKlSSESKRADTLAFEMKRLEEKHETLlKEKERLIEQRDTLK 424
Cdd:PTZ00121 1448 EAK--------KKAEEAKKAEEAKKKAEE-AKKADEAKKK-AEEAKKADEAKKKAEEAKKKADEA-KKAAEAKKKADEAK 1516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 425 ETNEELRCSKAQQDHLNQADASATKSYENLAAEimpveyrevfirlqhENKMLRLQQEGTENERIEQLQEQLEQKHRKMN 504
Cdd:PTZ00121 1517 KAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD---------------ELKKAEELKKAEEKKKAEEAKKAEEDKNMALR 1581
|
250 260 270
....*....|....*....|....*....|
gi 568929948 505 ELETEQRLSKERIGELQQQIEDLQKSLQEQ 534
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKAEE 1611
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
175-530 |
1.07e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 175 ELEQQLKRALEELQEAIAEKEELKQRCQELDMQVTTLQD--EKNSLVSENEMMNEKLDQLDGSFDDPNTMVAKKYF---- 248
Cdd:COG4717 92 ELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPERLEELEERLEELRELEEELEEleae 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 249 HVQLQLEQLQEENYRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLE-------- 320
Cdd:COG4717 172 LAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEErlkearll 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 321 ----STVEVYRQKLQDLNDLRKQVKSLQETNM--------MYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSE 388
Cdd:COG4717 252 lliaAALLALLGLGGSLLSLILTIAGVLFLVLgllallflLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLP 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 389 SKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTlketneeLRCSKAQQDHLNQADASATKSYENLAAEImpVEYREVFI 468
Cdd:COG4717 332 PDLSPEELLELLDRIEELQELLREAEELEEELQL-------EELEQEIAALLAEAGVEDEEELRAALEQA--EEYQELKE 402
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568929948 469 RLQHENKMLRLQ----QEGTENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKS 530
Cdd:COG4717 403 ELEELEEQLEELlgelEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED 468
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
377-533 |
1.10e-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: 40.68 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 377 QVQDLHTKLSSESKRADTLAFEMKRLEEKHETLlkeKERLIEQRDTLKETNEELrcsKAQQDHLNQADASATKSYENLAA 456
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAAL---EARLEAAKTELEDLEKEI---KRLELEIEEVEARIKKYEEQLGN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 457 EIMPVEYREvfirLQHENKMLRLQQEGTE------NERIEQLQEQLEQKHRKMNELETEqrlSKERIGELQQQIEDLQKS 530
Cdd:COG1579 85 VRNNKEYEA----LQKEIESLKRRISDLEdeilelMERIEELEEELAELEAELAELEAE---LEEKKAELDEELAELEAE 157
|
...
gi 568929948 531 LQE 533
Cdd:COG1579 158 LEE 160
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
410-533 |
1.11e-03 |
|
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: 41.98 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 410 LKEKERLIEQRDTLKETNEELRCSKAQQDHLNQADASATKSYENLAAEIMpveyrevfiRLQHENKMLrLQQEGTENERI 489
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIG---------EIEKEIEQL-EQEEEKLKERL 739
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 568929948 490 EQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQE 533
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALND 783
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
357-530 |
1.18e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 357 LEEELKKANAARAQLETYKRQVQ----------------DLHTKLSS-ESKRADTLAfEMKRLEEKHETLLKEKERLIEQ 419
Cdd:PRK02224 164 LEEYRERASDARLGVERVLSDQRgsldqlkaqieekeekDLHERLNGlESELAELDE-EIERYEEQREQARETRDEADEV 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 420 RDTLKETNEELRCSKAQQDHLNQADASATKSYENLAAEIMpvEYREVFIRLQHENKMLR--LQQEGTENERIEQLQEQLE 497
Cdd:PRK02224 243 LEEHEERREELETLEAEIEDLRETIAETEREREELAEEVR--DLRERLEELEEERDDLLaeAGLDDADAEAVEARREELE 320
|
170 180 190
....*....|....*....|....*....|....*
gi 568929948 498 QKhrkmnELETEQRLSKER--IGELQQQIEDLQKS 530
Cdd:PRK02224 321 DR-----DEELRDRLEECRvaAQAHNEEAESLRED 350
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
155-533 |
1.19e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.88 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 155 AIQELMSKEIVISPASDTVGELEQQLKRALEELQEAIAEKEELKQRCQELDMQVTTlQDEKNSLVSENEMMNEKLDQLDG 234
Cdd:pfam02463 650 KGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKE-QREKEELKKLKLEAEELLADRVQ 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 235 SFDDPNTMVAKKYFHVQLQLEQLQEENYRLEAAKDDYRVHCEELEKQLIEFQHRNdeltslaEETRALKDEIDVLRATSD 314
Cdd:pfam02463 729 EAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKT-------EKLKVEEEKEEKLKAQEE 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 315 KANKLESTVEVYRQKLQDLNDLRKQVKSLQETNMMYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADT 394
Cdd:pfam02463 802 ELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEE 881
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 395 LAFEMKRLEEKHETLLKEKERLIEQRDTLKETNEELRCSKAQQDHLNQADASATKSYENLAAEIMPVEYREVFIRLQ-HE 473
Cdd:pfam02463 882 QKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEeER 961
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 474 NKMLRLQQEGTENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQE 533
Cdd:pfam02463 962 NKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
263-431 |
1.46e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 263 RLEAAKDDYRVHCEELEKQLIEFQHR-----NDELTSLAEETRALKDEIDVLRATSDKA-NKLESTVEVYRQ-KLQDLND 335
Cdd:COG4913 263 RYAAARERLAELEYLRAALRLWFAQRrlellEAELEELRAELARLEAELERLEARLDALrEELDELEAQIRGnGGDRLEQ 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 336 LRKQVKSLQETnmmymHNTVS-----LEEELK----KANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKR----L 402
Cdd:COG4913 343 LEREIERLERE-----LEERErrrarLEALLAalglPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAalrdL 417
|
170 180
....*....|....*....|....*....
gi 568929948 403 EEKHETLLKEKERLIEQRDTLKETNEELR 431
Cdd:COG4913 418 RRELRELEAEIASLERRKSNIPARLLALR 446
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
107-373 |
1.65e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.45 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 107 QITECADPVE---LGRLLQLilgcAVNCEKKQEHIKNIMTLEESVQHVVMTaiQELMSKEIVISPASDTVGELEQQLKRA 183
Cdd:PRK05771 32 HIEDLKEELSnerLRKLRSL----LTKLSEALDKLRSYLPKLNPLREEKKK--VSVKSLEELIKDVEEELEKIEKEIKEL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 184 LEELQEAIAEKEELKQRCQEL------DMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAKKYfhvqlqleqL 257
Cdd:PRK05771 106 EEEISELENEIKELEQEIERLepwgnfDLDLSLLLGFKYVSVFVGTVPEDKLEELKLESDVENVEYISTD---------K 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 258 QEENYRLEAAKDDYrvhcEELEKQLIEFQHRNDELT---SLAEETRALKDEIDVLRAtsdkanKLESTVEVYRQKLQDLN 334
Cdd:PRK05771 177 GYVYVVVVVLKELS----DEVEEELKKLGFERLELEeegTPSELIREIKEELEEIEK------ERESLLEELKELAKKYL 246
|
250 260 270
....*....|....*....|....*....|....*....
gi 568929948 335 DLRKQVKSLqetnmmymhntvsLEEELKKANAARAQLET 373
Cdd:PRK05771 247 EELLALYEY-------------LEIELERAEALSKFLKT 272
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
292-534 |
1.75e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.25 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 292 LTSLAEETRALKDEIDVLRATSDKANKLESTVEVYRQKLQDLNDLRKQVKSLQETNMMYMHNTVS----LEEELKKANAA 367
Cdd:pfam05483 246 LIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMStqkaLEEDLQIATKT 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 368 RAQL-ETYKRQVQDLHTKLSSESKRADTLAFEMKRLEekhETLLKEKERLIEQRDTLKETNEELRCSKAQQDHLNQADAS 446
Cdd:pfam05483 326 ICQLtEEKEAQMEELNKAKAAHSFVVTEFEATTCSLE---ELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNN 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 447 ATKSYENLAAEIMPVEyrevfiRLQHENKMLRLQQE---GTENERIEQLQeqleQKHRKMNELETEQRLSKERIGELQQQ 523
Cdd:pfam05483 403 KEVELEELKKILAEDE------KLLDEKKQFEKIAEelkGKEQELIFLLQ----AREKEIHDLEIQLTAIKTSEEHYLKE 472
|
250
....*....|.
gi 568929948 524 IEDLQKSLQEQ 534
Cdd:pfam05483 473 VEDLKTELEKE 483
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
178-431 |
1.75e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 178 QQLKRALEELQEAIAEKEELKQrcqELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAKKYFHVQLQLEQL 257
Cdd:TIGR04523 387 KNLESQINDLESKIQNQEKLNQ---QKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTR 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 258 QEENYRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSD----KANKLESTVEVYRQKLQDL 333
Cdd:TIGR04523 464 ESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISslkeKIEKLESEKKEKESKISDL 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 334 ND-------------LRKQVKSLQETNMMYMHNTVSLEEELKKANAARAQLETYK----RQVQDLHTKLSSESKRADTLA 396
Cdd:TIGR04523 544 EDelnkddfelkkenLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKkdliKEIEEKEKKISSLEKELEKAK 623
|
250 260 270
....*....|....*....|....*....|....*
gi 568929948 397 FEMKRLEEKHETLLKEKERLIEQRDTLKETNEELR 431
Cdd:TIGR04523 624 KENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIR 658
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
276-533 |
1.76e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 276 EELEKQlIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEVYRQKLQDLNDLRKQVKSLQETNMMYMHNTV 355
Cdd:PTZ00121 1473 DEAKKK-AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADEL 1551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 356 SLEEELKKANAARaQLETYKRQVQDLHTKLssesKRADTL-AFEMKRLEEKHETLLKEKERLIEQRDTLKETN---EELR 431
Cdd:PTZ00121 1552 KKAEELKKAEEKK-KAEEAKKAEEDKNMAL----RKAEEAkKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKikaEELK 1626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 432 csKAQQDHLNQADASATKSYENLAAEIMPVEYREVFIRLQHENKmlrlqQEGTENERIEQLQEQLEQKHRKMNELETEQR 511
Cdd:PTZ00121 1627 --KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK-----KAEEDKKKAEEAKKAEEDEKKAAEALKKEAE 1699
|
250 260
....*....|....*....|..
gi 568929948 512 lSKERIGELQQQIEDLQKSLQE 533
Cdd:PTZ00121 1700 -EAKKAEELKKKEAEEKKKAEE 1720
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
280-533 |
1.83e-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: 41.48 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 280 KQLIEFQHR----NDELTSLAEETRALKDEidvLRATSDKANKLESTV------EVYRQKLQDLN-DLRKQ---VKSLQE 345
Cdd:COG3096 299 RQLAEEQYRlvemARELEELSARESDLEQD---YQAASDHLNLVQTALrqqekiERYQEDLEELTeRLEEQeevVEEAAE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 346 TNMMYMHNTVSLEEELKkanAARAQLETYKRQVQDLHTK----------------------LSSESKrADTLAFEMKRLE 403
Cdd:COG3096 376 QLAEAEARLEAAEEEVD---SLKSQLADYQQALDVQQTRaiqyqqavqalekaralcglpdLTPENA-EDYLAAFRAKEQ 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 404 EKHETLLKEKERLIEQRDTLKETNE--ELRCSKAQQDHLNQADASAT------KSYENLAAEIMPV--EYREVFIRLQHE 473
Cdd:COG3096 452 QATEEVLELEQKLSVADAARRQFEKayELVCKIAGEVERSQAWQTARellrryRSQQALAQRLQQLraQLAELEQRLRQQ 531
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568929948 474 NKMLRLQQE-----GTENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQE 533
Cdd:COG3096 532 QNAERLLEEfcqriGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKE 596
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
157-533 |
2.21e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 157 QELMSKEIVISPASDTVGELEQQLKRALEELQEAIAEKEELKQRCQELDMQVTTLQDEKNSLVSE-----NEMMNEKLDQ 231
Cdd:TIGR04523 239 QEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQkeqdwNKELKSELKN 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 232 LDGSFDDPNTMVAKKYFHVQLQLEQLQEENYRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRA 311
Cdd:TIGR04523 319 QEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLES 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 312 TSDKANKLESTVEVYRQKLQ-DLNDLRKQVKSLQETNmmymhntVSLEEELKKANAARAQLETykrQVQDLHTKLSSESK 390
Cdd:TIGR04523 399 KIQNQEKLNQQKDEQIKKLQqEKELLEKEIERLKETI-------IKNNSEIKDLTNQDSVKEL---IIKNLDNTRESLET 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 391 RADTLAFEMKRLEEKHETLLKEkerLIEQRDTLKETNEELRCSKAQQDHLNQADASATKSYENLAAEIMPVEYREVFIRL 470
Cdd:TIGR04523 469 QLKVLSRSINKIKQNLEQKQKE---LKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLED 545
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568929948 471 QHENKMLRLQQEGTENErIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQE 533
Cdd:TIGR04523 546 ELNKDDFELKKENLEKE-IDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEE 607
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
171-431 |
2.24e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 171 DTVGELEQQLKRALEELQEAIAEKEELKQRCQELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAKkyfhv 250
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKE----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 251 qlqleqlqeenyrLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLR-------ATSDKANKLESTV 323
Cdd:COG1340 76 -------------LKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEwrqqtevLSPEEEKELVEKI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 324 EVYRQKLQDLNDLRKQVKSLQETNmmymhntVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLafeMKRLE 403
Cdd:COG1340 143 KELEKELEKAKKALEKNEKLKELR-------AELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADEL---RKEAD 212
|
250 260
....*....|....*....|....*...
gi 568929948 404 EKHETLLKEKERLIEQRDTLKETNEELR 431
Cdd:COG1340 213 ELHKEIVEAQEKADELHEEIIELQKELR 240
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
167-379 |
2.30e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 167 SPASDTVGELEQQLKRALEELQEAIAEKEELKQRCQELDM---------QVTTLQDEKNSLVSENEMMNEKLDQLDGSFD 237
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLseeaklllqQLSELESQLAEARAELAEAEARLAALRAQLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 238 DPNTMVAkkyfhvqlqleqLQEENYRLEAAKDDYRvhceELEKQLIE----FQHRNDELTSLAEETRALKDEIDvlRATS 313
Cdd:COG3206 251 SGPDALP------------ELLQSPVIQQLRAQLA----ELEAELAElsarYTPNHPDVIALRAQIAALRAQLQ--QEAQ 312
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568929948 314 DKANKLESTVEVYRQKLQDLNDLRKQvkslqetnmmymhntvsLEEELKKANAARAQLETYKRQVQ 379
Cdd:COG3206 313 RILASLEAELEALQAREASLQAQLAQ-----------------LEARLAELPELEAELRRLEREVE 361
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
175-521 |
2.50e-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: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 175 ELEQQLKRALEELQEAIAEKEELKQRCQELDMQVTTLQDEKNSLVSENEMMNEKLDQLdgsfddpNTMVAKKYFHVQLQL 254
Cdd:TIGR00606 699 DLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKV-------NRDIQRLKNDIEEQE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 255 EQLQEENYRLEAAKD---DYRVhCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEVYRQKLQ 331
Cdd:TIGR00606 772 TLLGTIMPEEESAKVcltDVTI-MERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 332 DLNDLRKQVKSLQETNMMYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLK 411
Cdd:TIGR00606 851 LIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS 930
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 412 EKER-----LIEQRDTLKETNEELRCSKAQQDHLNQADASATKSYENLAAEIMpVEYREVFIRLQHENKMLRLQQEGTEN 486
Cdd:TIGR00606 931 SKETsnkkaQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVN-AQLEECEKHQEKINEDMRLMRQDIDT 1009
|
330 340 350
....*....|....*....|....*....|....*....
gi 568929948 487 ERIEQ--LQEQLEQKHR--KMNELETEQRLSKERIGELQ 521
Cdd:TIGR00606 1010 QKIQErwLQDNLTLRKRenELKEVEEELKQHLKEMGQMQ 1048
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
365-521 |
2.56e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 365 NAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQrdtLKETNEELRcSKAQQDhLNQAD 444
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEK---LQEEEDKLL-EEAEKE-AQQAI 579
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568929948 445 ASATKSyenlAAEImpveyrevfIRlqhenKMLRLQQEGTENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQ 521
Cdd:PRK00409 580 KEAKKE----ADEI---------IK-----ELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
289-533 |
2.65e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 289 NDELTSLAEETRALKDEIDVLRATSDKANKleSTVEVYRQKLQDLNDLRKQVKSLQETNMMYmHNTVSLEEELKKAnaaR 368
Cdd:TIGR04523 102 NSDLSKINSEIKNDKEQKNKLEVELNKLEK--QKKENKKNIDKFLTEIKKKEKELEKLNNKY-NDLKKQKEELENE---L 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 369 AQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKETNEELRCSKAQ--------QDHL 440
Cdd:TIGR04523 176 NLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEktteisntQTQL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 441 NQADASATKSYENLAAEIMPVEYREVFIR------LQHENKMLRLQQEgTENERIEQLQEQLEQKHRKMNELETEQRLSK 514
Cdd:TIGR04523 256 NQLKDEQNKIKKQLSEKQKELEQNNKKIKelekqlNQLKSEISDLNNQ-KEQDWNKELKSELKNQEKKLEEIQNQISQNN 334
|
250
....*....|....*....
gi 568929948 515 ERIGELQQQIEDLQKSLQE 533
Cdd:TIGR04523 335 KIISQLNEQISQLKKELTN 353
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
166-390 |
2.89e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.81 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 166 ISPASDTVGELEQQLKRALEELQEAIAEKEELKQRCQELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAK 245
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 246 KYfhvqlqleqlqeenYRLEAAKD---DYRVHCEELEKQLIEFQHRndeltsLAEETRALKDEIDvlratsdkanKLEST 322
Cdd:TIGR02168 913 LR--------------RELEELREklaQLELRLEGLEVRIDNLQER------LSEEYSLTLEEAE----------ALENK 962
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568929948 323 VEVYRQKLQD-LNDLRKQVKSLQETNMMYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESK 390
Cdd:TIGR02168 963 IEDDEEEARRrLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREAR 1031
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
353-528 |
2.98e-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: 40.71 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 353 NTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKETNEELRc 432
Cdd:COG3096 513 RLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLR- 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 433 skAQQDHLnqadasATKSYENLAAeimpveyREVFIRLQhenkmlrlQQEGTENERIEQLQEQLEQKHRKMNELETEQRL 512
Cdd:COG3096 592 --ARIKEL------AARAPAWLAA-------QDALERLR--------EQSGEALADSQEVTAAMQQLLEREREATVERDE 648
|
170
....*....|....*.
gi 568929948 513 SKERIGELQQQIEDLQ 528
Cdd:COG3096 649 LAARKQALESQIERLS 664
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
167-431 |
4.12e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 167 SPASDTVGELEQQLKRALEELQEAIAEKEELKQRCQELDmQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAKK 246
Cdd:PRK02224 464 SPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEEL 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 247 YFHVQLqleqlqeenyrLEAAKDDYRvhcEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLE---STV 323
Cdd:PRK02224 543 RERAAE-----------LEAEAEEKR---EAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIAdaeDEI 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 324 EVYRQKLQDLNDLRKQVKS-LQETNMMYMHNTVSLEEE-LKKANAARAQLETYKRQVQDlhtKLSSESKRADTLAFEMKR 401
Cdd:PRK02224 609 ERLREKREALAELNDERRErLAEKRERKRELEAEFDEArIEEAREDKERAEEYLEQVEE---KLDELREERDDLQAEIGA 685
|
250 260 270
....*....|....*....|....*....|
gi 568929948 402 LEEKhetlLKEKERLIEQRDTLKETNEELR 431
Cdd:PRK02224 686 VENE----LEELEELRERREALENRVEALE 711
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
367-533 |
4.36e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 367 ARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDtLKETNEELRCSKAQQDHLNQADAs 446
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID-VASAEREIAELEAELERLDASSD- 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 447 atksyenlaaeimpveyreVFIRLQhenkmlrlqqegtenERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIED 526
Cdd:COG4913 686 -------------------DLAALE---------------EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE 731
|
....*..
gi 568929948 527 LQKSLQE 533
Cdd:COG4913 732 LQDRLEA 738
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
265-502 |
4.49e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 265 EAAKDDYRVHCEELEKQliEFQHRNDELTSLAEETRALKDEIDVLRAT-----SDKANKLESTVEVYRQKLQDLNDLRK- 338
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKA--EELKKAEEKKKAEEAKKAEEDKNMALRKAeeakkAEEARIEEVMKLYEEEKKMKAEEAKKa 1615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 339 --------QVKSLQETNMMYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLL 410
Cdd:PTZ00121 1616 eeakikaeELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALK 1695
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 411 KEKERLIEQRDTLKETNEELR----CSKAQQDHLNQADASATKSYEN-LAAEIMPVEYREVfIRLQHENKMLRLQQEGTE 485
Cdd:PTZ00121 1696 KEAEEAKKAEELKKKEAEEKKkaeeLKKAEEENKIKAEEAKKEAEEDkKKAEEAKKDEEEK-KKIAHLKKEEEKKAEEIR 1774
|
250
....*....|....*..
gi 568929948 486 NERIEQLQEQLEQKHRK 502
Cdd:PTZ00121 1775 KEKEAVIEEELDEEDEK 1791
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
132-372 |
4.60e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 132 EKKQEHIKNIMTLEESVQHVVMTAIQELMSKEIVISPASDTVGELEQQLKRALEELQEAIAEKEELKQRCQELDMQVTTL 211
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 212 QDEKNSLVSENEMMNEKLDQLDGSFDDpntmvakkyfhVQLQLEQLQEENYRLEAAKDDYRVHCEELEKQLIEFQHRNDE 291
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAE-----------AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 292 LtsLAEETRALKDEIDVLRATSDKANKLESTVEVYRQKLQDLNDLRKQVKSLQETNMMYMHNTVSLEEELKKANAARAQL 371
Cdd:COG1196 419 L--EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
.
gi 568929948 372 E 372
Cdd:COG1196 497 L 497
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
290-533 |
4.74e-03 |
|
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: 40.05 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 290 DELTSLAEETRALKDEIDVLRATSDKANKLESTVEVYRQKLQDLNDLRKQVKSLQEtnMMYMHNTVSLEEELKKANAARA 369
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQA--LLKEKREYEGYELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 370 QLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRD-TLKETNEELrcsKAQQDHLNQADASAT 448
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlRVKEKIGEL---EAEIASLERSIAEKE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 449 KSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGTE----NERIEQLQEQLEQKHRKMNELETEQRLS----------- 513
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRrdklTEEYAELKEELEDLRAELEEVDKEFAETrdelkdyrekl 394
|
250 260
....*....|....*....|...
gi 568929948 514 ---KERIGELQQQIEDLQKSLQE 533
Cdd:TIGR02169 395 eklKREINELKRELDRLQEELQR 417
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
176-429 |
5.48e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 39.89 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 176 LEQQLKRALEELQEAIAEKEELKQRCQELDMQVTTlQDEKNSLVSEN----EMMNEKLDQLDGSFDDPNTMVAKKYFHVQ 251
Cdd:PLN02939 147 LNQARLQALEDLEKILTEKEALQGKINILEMRLSE-TDARIKLAAQEkihvEILEEQLEKLRNELLIRGATEGLCVHSLS 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 252 LQLEQLQEENYRLeaaKDDyrvhCEELEKQLIEFQHRNDELTSLAEEtRALKD------EIDVLRATSDKANKLESTVEV 325
Cdd:PLN02939 226 KELDVLKEENMLL---KDD----IQFLKAELIEVAETEERVFKLEKE-RSLLDaslrelESKFIVAQEDVSKLSPLQYDC 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 326 YRQKLQDLNDLRKQVKSLQETNMMYMHNTVSLEEELKKANAARAQLETYkrqvqdlhtKLSSEskRADTLAFEMKRLEEK 405
Cdd:PLN02939 298 WWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVS---------KFSSY--KVELLQQKLKLLEER 366
|
250 260 270
....*....|....*....|....*....|..
gi 568929948 406 HETLLKE--------KERLIEQRDTLKETNEE 429
Cdd:PLN02939 367 LQASDHEihsyiqlyQESIKEFQDTLSKLKEE 398
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
176-509 |
5.48e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 39.49 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 176 LEQQLKRALEELQEAIAEKEELKQRCQELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAKKYFHVQLQLE 255
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 256 QLQEENYRLEAAKDDYRVHCEELEkqliefqhrnDELTSLAEETRALKDEIDVLRATSDKANKLESTVEVYRQKLQdlND 335
Cdd:pfam07888 112 ELSEEKDALLAQRAAHEARIRELE----------EDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQ--AK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 336 LRKQVKSLQetnmmymhntvSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMkrlEEKHETLLKEKER 415
Cdd:pfam07888 180 LQQTEEELR-----------SLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEN---EALLEELRSLQER 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 416 LIEQRDTLKETNEELRCSKAQQDH----LNQADASATKSYENLAAeiMPVEYREVFIRLQHENKMLRLQQEgTENERIEQ 491
Cdd:pfam07888 246 LNASERKVEGLGEELSSMAAQRDRtqaeLHQARLQAAQLTLQLAD--ASLALREGRARWAQERETLQQSAE-ADKDRIEK 322
|
330
....*....|....*...
gi 568929948 492 LQEQLEQKHRKMNELETE 509
Cdd:pfam07888 323 LSAELQRLEERLQEERME 340
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
357-534 |
6.46e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 39.29 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 357 LEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHetlLK--EKERLIEQRDTLkeTN-EELRcS 433
Cdd:COG0497 153 LEELLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAAA---LQpgEEEELEEERRRL--SNaEKLR-E 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 434 KAQQ--DHLNQADASAT-----------------KSYENLAAEImpveyREVFIRLQ---HEnkmLRLQQEGTEN--ERI 489
Cdd:COG0497 227 ALQEalEALSGGEGGALdllgqalralerlaeydPSLAELAERL-----ESALIELEeaaSE---LRRYLDSLEFdpERL 298
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568929948 490 EQLQE------QLEQKHRK-MNEL-----ETEQRLSK-----ERIGELQQQIEDLQKSLQEQ 534
Cdd:COG0497 299 EEVEErlallrRLARKYGVtVEELlayaeELRAELAElensdERLEELEAELAEAEAELLEA 360
|
|
| PRK10361 |
PRK10361 |
DNA recombination protein RmuC; Provisional |
280-412 |
6.96e-03 |
|
DNA recombination protein RmuC; Provisional
Pssm-ID: 182409 [Multi-domain] Cd Length: 475 Bit Score: 39.20 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 280 KQLIEFQHRNDELTSLAEETRALKD-----EIDVLRATSdkanKLESTV----EVYRQKLQDLNDLRKQVKSLqeTNMMY 350
Cdd:PRK10361 50 QQITQSEHWRAECELLNNEVRSLQSintslEADLREVTT----RMEAAQqhadDKIRQMINSEQRLSEQFENL--ANRIF 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568929948 351 MHNTVSLEEELKKA-----NAARAQLETYKRQVQDlhtKLSSESKRADTLAFEMKRLEEKHETLLKE 412
Cdd:PRK10361 124 EHSNRRVDEQNRQSlnsllSPLREQLDGFRRQVQD---SFGKEAQERHTLAHEIRNLQQLNAQMAQE 187
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
169-526 |
8.22e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 39.23 E-value: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 169 ASDTVGELEQQLKRALEELQEAIAEKEELKQRCQELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAKKYF 248
Cdd:TIGR04523 305 EQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 249 HVQLQLEQLQEENYRLEAAKD-----DYRVHCEELEKQLIEFQHRN--DELTSLAEETRALKDEIDVLRAtsdKANKLES 321
Cdd:TIGR04523 385 EIKNLESQINDLESKIQNQEKlnqqkDEQIKKLQQEKELLEKEIERlkETIIKNNSEIKDLTNQDSVKEL---IIKNLDN 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 322 TVEVYRQKLQDLNDLRKQVKSLQETNmmyMHNTVSLEEELKKANAARAQLEtykRQVQDLHTKLSSESKRADTLAFEMKR 401
Cdd:TIGR04523 462 TRESLETQLKVLSRSINKIKQNLEQK---QKELKSKEKELKKLNEEKKELE---EKVKDLTKKISSLKEKIEKLESEKKE 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 402 LEEKhetlLKEKERLIEQRDTLKeTNEELrcsKAQQDHLNQADASATKSYENLAAEimPVEYREVFIRLQHENKMLRLQQ 481
Cdd:TIGR04523 536 KESK----ISDLEDELNKDDFEL-KKENL---EKEIDEKNKEIEELKQTQKSLKKK--QEEKQELIDQKEKEKKDLIKEI 605
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 568929948 482 EgTENERIEQLQEQL---EQKHRKMNELETEQRLSKERIGELQQQIED 526
Cdd:TIGR04523 606 E-EKEKKISSLEKELekaKKENEKLSSIIKNIKSKKNKLKQEVKQIKE 652
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
170-421 |
8.44e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 38.35 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 170 SDTVGELEQQLKRALEELQEAIAEKEELKQRCQELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTmVAKKYFH 249
Cdd:COG1340 14 EEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNE-KLNELRE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 250 VQLQLEQLQEENYRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEVYRQK 329
Cdd:COG1340 93 ELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKKALEKNEKLKELRAELKEL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 330 LQDLNDLRKQVKSLQEtNMMYMHNtvSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETL 409
Cdd:COG1340 173 RKEAEEIHKKIKELAE-EAQELHE--EMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKL 249
|
250
....*....|..
gi 568929948 410 LKEKERLIEQRD 421
Cdd:COG1340 250 RKKQRALKREKE 261
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
277-456 |
8.50e-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: 37.98 E-value: 8.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 277 ELEKQLIEFQHRndeLTSLAEETRALKDEIDVLRATSDKANK-LESTVEVYRQKLQDLNDLRKQVKSLQEtnmmyMHNTV 355
Cdd:COG1579 14 ELDSELDRLEHR---LKELPAELAELEDELAALEARLEAAKTeLEDLEKEIKRLELEIEEVEARIKKYEE-----QLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 356 SLEEELKkanAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDT-LKETNEEL-RCS 433
Cdd:COG1579 86 RNNKEYE---ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEeLAELEAELeELE 162
|
170 180
....*....|....*....|...
gi 568929948 434 KAQQDHLNQADASATKSYENLAA 456
Cdd:COG1579 163 AEREELAAKIPPELLALYERIRK 185
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
157-392 |
8.77e-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: 38.59 E-value: 8.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 157 QELMSKEIVISPASDTVGELEQQLKRALEELQEAIAEKEELKQRCQELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSF 236
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 237 DDpntMVAKKYfhvqlqlEQLQEENYRLEAAKDDYrvhcEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRAT-SDK 315
Cdd:COG4942 107 AE---LLRALY-------RLGRQPPLALLLSPEDF----LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAElEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568929948 316 ANKLESTVEVYRQKLQDLNDLRKQVKSLQEtnmmymhntvSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRA 392
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLA----------RLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
302-534 |
9.03e-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: 39.18 E-value: 9.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 302 LKDEIDVLRATSDKANKLESTVEVYRQKLQDLNDLRKQVKSLQETNMMYMHNTVSLEEEL-KKANAARAQLETYKRQVQD 380
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLaKEEEELKSELLKLERRKVD 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 381 LHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKETNEELRcskAQQDHLNQADASATKSYENLAaeimp 460
Cdd:pfam02463 312 DEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELE---KLQEKLEQLEEELLAKKKLES----- 383
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568929948 461 vEYREVFIRLQHENKMLRLQQEGTENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQ 534
Cdd:pfam02463 384 -ERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQ 456
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
276-458 |
9.86e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 38.66 E-value: 9.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 276 EELEKQLIEFQhrnDELTSLAEETRALKDEIDVLRATSDKANKLestVEVYRQKLQDLND-LRKQVKSLQETNmmymhNT 354
Cdd:COG3883 33 EAAQAELDALQ---AELEELNEEYNELQAELEALQAEIDKLQAE---IAEAEAEIEERREeLGERARALYRSG-----GS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929948 355 VSLEEELKKANaaraQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKETNEELRCSK 434
Cdd:COG3883 102 VSYLDVLLGSE----SFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180
....*....|....*....|....
gi 568929948 435 AQQDHLNQADASATKSYENLAAEI 458
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAEL 201
|
|
| |
