|
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 |
1.93e-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: 460.31 E-value: 1.93e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 186 ELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDgSFDDPNTVVAKKYFHAQLQLEQLQEENFRLE 265
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLE-SGDDSGTPGGKKYLLLQKQLEQLQEENFRLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 266 AAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKLQDLNDLRKQVKTLQE 345
Cdd:pfam05622 80 TARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLGDLRRQVKLLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 346 TNMMYMHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKE 425
Cdd:pfam05622 160 RNAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 426 TNEELRCSQVQQDHLNQTDASATKSY---ENLAAEIMPVEYREVFIRLQHENKMLRLQQEGSENERIEELQEQLEQKHRK 502
Cdd:pfam05622 240 TNEELRCAQLQQAELSQADALLSPSSdpgDNLAAEIMPAEIREKLIRLQHENKMLRLGQEGSYRERLTELQQLLEDANRR 319
|
330 340 350
....*....|....*....|....*....|..
gi 578799215 503 MNELETEQRLSKERIRELQQQIEDLQKSLQEQ 534
Cdd:pfam05622 320 KNELETQNRLANQRILELQQQVEELQKALQEQ 351
|
|
| HkD_Hook1 |
cd22225 |
Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a ... |
15-163 |
2.32e-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: 294.84 E-value: 2.32e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 15 CDSLMIWLQTFNTASPCQDVKQLTSGVAMAQVLHQIDAAWFNESWLSRIKEDVGDNWRIKASNVKKVLQGIMSYYHEFLG 94
Cdd:cd22225 2 CDSLIIWLQTFNTAAPCQTVQDLTSGVAMAQVLHQIDSSWFDESWLSRIKEDVGDNWRIKMSNLKKILQGIVDYYHEFLD 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578799215 95 QQISEALIPDLNQITECSDPVELGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQELMSKE 163
Cdd:cd22225 82 QQISEFLLPDLNRIAEHSDPVELGRLLQLILGCAVNCEKKQEHIQNIMTLEESVQHVVMTAIQELMSKE 150
|
|
| HOOK_N |
pfam19047 |
HOOK domain; This domain is found at the N-terminus of HOOK proteins. |
15-163 |
9.93e-90 |
|
HOOK domain; This domain is found at the N-terminus of HOOK proteins.
Pssm-ID: 465958 Cd Length: 151 Bit Score: 272.74 E-value: 9.93e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 15 CDSLMIWLQTFNTASPCQDVKQLTSGVAMAQVLHQIDAAWFNESWLSRIKEDVGDNWRIKASNVKKVLQGIMSYYHEFLG 94
Cdd:pfam19047 3 CDSLLTWLQTFNVPAPCATVEDLTDGVAMAQVLHQIDPSWFTEAWLSRIKEDVGDNWRLKVSNLKKILQSVVDYYQDVLG 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578799215 95 QQISEALIPDLNQITECSDPVELGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQELMSKE 163
Cdd:pfam19047 83 QQISDFLLPDVNLIGEHSDPAELGRLLQLILGCAVNCEKKQEYIQQIMTLEESVQHVVMTAIQELMSKD 151
|
|
| HkD_Hook |
cd22222 |
Hook domain found in Hook family of microtubule-binding proteins; The Hook family includes ... |
15-161 |
1.45e-85 |
|
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: 261.80 E-value: 1.45e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 15 CDSLMIWLQTFNTASPCQDVKQLTSGVAMAQVLHQIDAAWFNESWLSRIKEDVGDNWRIKASNVKKVLQGIMSYYHEFLG 94
Cdd:cd22222 1 CDSLLQWLQTFNLIAPHATAEDLSDGVAIAQVLNQIDPEYFSDSWLSKIKPDVGDNWRLKVSNLKKILKGIVDYYSEVLG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578799215 95 QQISEALIPDLNQITECSDPVELGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQELMS 161
Cdd:cd22222 81 QQISGFTMPDVNAIAEKEDPKELGRLLQLVLGCAVNCERKEEYIQAIMGLEESVQHVVMEAIQELMS 147
|
|
| HkD_Hook2 |
cd22227 |
Hook domain found in protein Hook 2 (Hook2) and similar proteins; Hook2 is a ... |
15-162 |
6.50e-72 |
|
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: 226.68 E-value: 6.50e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 15 CDSLMIWLQTFNTASPCQDVKQLTSGVAMAQVLHQIDAAWFNESWLSRIKEDVGDNWRIKASNVKKVLQGIMSYYHEFLG 94
Cdd:cd22227 3 CDSLLTWLQTFQVPSPCSSYQDLTSGVAIAQVLNRIDPSWFNEAWLGRIKEDTGDNWRLKVSNLKKILQSLLEYYQDVLG 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578799215 95 QQISEALIPDLNQITECSDPVELGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQELMSK 162
Cdd:cd22227 83 HQVSEDHLPDVNLIGEFSDDTELGKLLQLVLGCAISCEKKQEHIQQIMTLEESVQHVVMEAIQELLTK 150
|
|
| HkD_Hook3 |
cd22226 |
Hook domain found in protein Hook 3 (Hook3) and similar proteins; Hook3 is an adaptor protein ... |
15-162 |
1.67e-71 |
|
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: 225.62 E-value: 1.67e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 15 CDSLMIWLQTFNTASPCQDVKQLTSGVAMAQVLHQIDAAWFNESWLSRIKEDVGDNWRIKASNVKKVLQGIMSYYHEFLG 94
Cdd:cd22226 6 CESLLTWIQTFNVDAPCQTVEDLTSGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEILG 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578799215 95 QQISEALIPDLNQITECSDPVELGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQELMSK 162
Cdd:cd22226 86 QQINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMSK 153
|
|
| HkD_SF |
cd22211 |
Hook domain-containing proteins superfamily; The Hook domain superfamily includes Hook adaptor ... |
16-161 |
2.22e-48 |
|
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: 164.76 E-value: 2.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 16 DSLMIWLQTFNTASPCQDVKQLTSGVAMAQVLHQIDAAWFNESWLSriKEDVGDNWRIKASNVKKVLQGIMSYYHEFLGQ 95
Cdd:cd22211 2 AALLAWINTFPLSSPVESLDDLSDGVVLAEILSQIDPSYFDSEWLE--SRDSSDNWVLKLNNLKKLYRSLSKYYREVLGQ 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578799215 96 QISEALIPDLNQITECSDPVELGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQELMS 161
Cdd:cd22211 80 QLSDLPLPDLSAIARDGDEEEIVKLLELVLGAAVQCENKEEYIARIQQLDESTQAELMLIIQEVLE 145
|
|
| HkD_HkRP |
cd22223 |
Hook domain found in the Hook-related protein (HkRP) family; The HkRP family includes Daple, ... |
17-159 |
6.11e-22 |
|
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: 92.27 E-value: 6.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 17 SLMIWLQTFNTASPCQ-DVKQLTSGVAMAQVLHQIDAAWFNESWLSRIKEDVgdNWRIKasNVKKVLQGIMSYYHEFLGQ 95
Cdd:cd22223 5 PLVTWAKTFADDGSAElSYTDLVDGVFLNNVMLQIDPRPFSEVSNRNVDDDV--NARIQ--NLDLLLRNIKSFYQEVLQQ 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 96 QISEALiPDLNQIteCSDP------VELGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQEL 159
Cdd:cd22223 81 LIVMKL-PDILTI--GREPeseqslEELEKLLLLLLGCAVQCERKEEFIERIKNLDLEVQHALVACIQEV 147
|
|
| HkD_Daple |
cd22228 |
Hook domain found in Daple (Dvl-associating protein with a high frequency of leucine residues) ... |
18-159 |
2.94e-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: 2.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 18 LMIWLQTFNTASPCQDVK-----QLTSGVAMAQVLHQIDAAWFNEswlsRIKEDVGDNWRIKASNVKKVLQGIMSYYHEF 92
Cdd:cd22228 6 LVTWVKTFGPLGFGSEDKlsmymDLVDGVFLNKIMLQIDPRPTNQ----RVNKHVNNDVNLRIQNLTILVRHIKTYYQEV 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578799215 93 LGQQISEALiPDLNQITEcsDPV------ELGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQEL 159
Cdd:cd22228 82 LQQLIVMNL-PNVLMIGK--DPLsgksmeEIKKMLLLVLGCAVQCERKEEFIERIKQLDIETQAAIVSHIQEV 151
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
181-532 |
3.11e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.23 E-value: 3.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 181 KRALEELQEalaEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVVAKKYFHAQLQLEQLQEE 260
Cdd:TIGR02168 676 RREIEELEE---KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 261 NFRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEI-YRQKLQDLNDLRKQ 339
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEeAANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 340 VKTLQETNMMYMHNTVSLEEELKKANAA----RTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKER 415
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEieelEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 416 LIEQRDTLKETNE--ELRCSQVQQDHLNQTDAsATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQE----GSENER- 488
Cdd:TIGR02168 913 LRRELEELREKLAqlELRLEGLEVRIDNLQER-LSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKikelGPVNLAa 991
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 578799215 489 IEELQEQleqkhrkmneleteqrlsKERIRELQQQIEDLQKSLQ 532
Cdd:TIGR02168 992 IEEYEEL------------------KERYDFLTAQKEDLTEAKE 1017
|
|
| HkD_Girdin |
cd22229 |
Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation ... |
18-159 |
3.80e-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: 58.65 E-value: 3.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 18 LMIWLQTF-----NTASPCQDVKQLTSGVAMAQVLHQIDAAWFNEswlsRIKEDVGDNWRIKASNVKKVLQGIMSYYHEF 92
Cdd:cd22229 9 LVTWVKTFgplatGNGTPLDEYVALVDGVFLNEVMLQINPKSSNQ----RVNKKVNNDASLRIQNLSILVKQIKLYYQET 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578799215 93 LGQQISEALiPDL-----NQITEcSDPVELGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQEL 159
Cdd:cd22229 85 LQQLIMMSL-PNVlvlgrNPLSE-QGTEEMKKLLLLLLGCAVQCERKEEFIERIQTLDFDTKAAVAAHIQEV 154
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
173-532 |
8.08e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.01 E-value: 8.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 173 VGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQldgsfddPNTVVAKKYFHAQL 252
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREY-------EGYELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 253 QLEQLQEENFRLEAAKDDYRVHCEELEKQLIEfqhRNDELTSLAEETRALKDE--IDVLRATSDKANKLESTVEIYRQKL 330
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEE---IEQLLEELNKKIKDLGEEeqLRVKEKIGELEAEIASLERSIAEKE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 331 QDLNDLRKQVKTLQETNMMYMHNTVSLEEELKKANAARTQLET----YKRQVQDLHVKLSSESKRADTLAFEMKRLEEKH 406
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEeyaeLKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 407 EALLKEKERLIEQRDTLKETNEELRcSQVQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGSEN 486
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLS-EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD 473
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 578799215 487 --ERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQ 532
Cdd:TIGR02169 474 lkEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
263-533 |
2.48e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.46 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 263 RLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDV-LRATSDKANKLESTVEIYRQKLQDLN----DLR 337
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqISALRKDLARLEAEVEQLEERIAQLSkeltELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 338 KQVKTLQETNMMYMHNTVSLEEELKK----ANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEK 413
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEEleaqIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 414 ERLIEQRDTLKETNEELrcsQVQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGSENERIE--- 490
Cdd:TIGR02168 841 EDLEEQIEELSEDIESL---AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRrel 917
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 578799215 491 -ELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQE 533
Cdd:TIGR02168 918 eELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALEN 961
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
277-534 |
1.11e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 277 ELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRAtsdKANKLESTVEIYRQKLQDLNDlrkqvktlqetnmmymhntvS 356
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEA---ELAELEAELEELRLELEELEL--------------------E 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 357 LEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKETNEELRcsqvq 436
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE----- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 437 qdhlnQTDASATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGSENERIEELQEQLEQkhrKMNELETEQRLSKER 516
Cdd:COG1196 358 -----AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE---RLERLEEELEELEEA 429
|
250
....*....|....*...
gi 578799215 517 IRELQQQIEDLQKSLQEQ 534
Cdd:COG1196 430 LAELEEEEEEEEEALEEA 447
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
170-529 |
1.19e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 170 NDAVGELEQQLKRAleELQEALAEK-EELRQRCEELDMQVTTLQdeknslvsenemMNEKLDQLDgsfddpntvvakkyf 248
Cdd:TIGR02168 192 EDILNELERQLKSL--ERQAEKAERyKELKAELRELELALLVLR------------LEELREELE--------------- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 249 haqlqleqlqeenfRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEID-VLRATSDKANKLESTVEIYR 327
Cdd:TIGR02168 243 --------------ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQkELYALANEISRLEQQKQILR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 328 QKLQDLNDLRKQVKTLQETnmmymhntvsLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMK-RLEEKH 406
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEE----------LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELEsRLEELE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 407 EALLKEKERLIEQRDTLKETNEELRCSQVQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGSE- 485
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELEr 458
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 578799215 486 -NERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQK 529
Cdd:TIGR02168 459 lEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
179-525 |
1.67e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 179 QLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVVAKKyfhaqlqLEQLQ 258
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL-------EQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 259 EENFRLEAAKDDYrvhcEELEKQLIEFQHRNDEltsLAEETRALKDEIDVLRAtsdkanklestveiyrqklqDLNDLRK 338
Cdd:TIGR02168 306 ILRERLANLERQL----EELEAQLEELESKLDE---LAEELAELEEKLEELKE--------------------ELESLEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 339 QVKTLQETnmmymhntvsLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLIE 418
Cdd:TIGR02168 359 ELEELEAE----------LEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 419 QRDTLketneELRCSQVQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGSENERIEELQEQLEQ 498
Cdd:TIGR02168 429 KLEEA-----ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
330 340
....*....|....*....|....*..
gi 578799215 499 KHRKMNELETEQRLSKERIRELQQQIE 525
Cdd:TIGR02168 504 FSEGVKALLKNQSGLSGILGVLSELIS 530
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
175-431 |
2.18e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 175 ELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDqldgsfddpntvvakkyfHAQLQL 254
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA------------------RLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 255 EQLQEENFRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEID--VLRATSDKANKLESTVEIYRQKLQD 332
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEeaLLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 333 LNDLRKQVKTLQETNMMYMHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKE 412
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
250
....*....|....*....
gi 578799215 413 KERLIEQRDTLKETNEELR 431
Cdd:COG1196 472 AALLEAALAELLEELAEAA 490
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
170-430 |
2.07e-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: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 170 NDAVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVVAKKYFH 249
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 250 AQLQLEQLQEENFRLEAAK----------DDYRVHCEELEKQLIEFQhrnDELTSLAEETRALKDEIDVLRATsdkANKL 319
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSedieslaaeiEELEELIEELESELEALL---NERASLEEALALLRSELEELSEE---LREL 906
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 320 ESTVEIYRQKLQDLNDLRKQVKT-LQETNMMYMHNT--------VSLEEELKKANAARTQLETYKRQVQDLHVKLsSESK 390
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELrLEGLEVRIDNLQerlseeysLTLEEAEALENKIEDDEEEARRRLKRLENKI-KELG 985
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 578799215 391 RADTLAF-EMKRLEEKHEALLKEKERLIEQRDTLKETNEEL 430
Cdd:TIGR02168 986 PVNLAAIeEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
271-534 |
2.75e-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: 53.52 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 271 YRVHCEELEKQLIEFQHRNDELTSLAEEtraLKDEIDVLRATSDKANKLESTVEIYRQK-----LQDLNDLRKQVKTLQE 345
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDRLEDILNE---LERQLKSLERQAEKAERYKELKAELRELelallVLRLEELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 346 TNMMYMHNTVSLEEELKKANAartQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALlkeKERLIEQRDTLKE 425
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEE---KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIL---RERLANLERQLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 426 TNEELRCSQVQQDHLNQTDASATKSYENLAAEIMpveyrevfiRLQHENKMLRLQQEGSENeRIEELQEQLEQKHRKMNE 505
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELE---------SLEAELEELEAELEELES-RLEELEEQLETLRSKVAQ 390
|
250 260
....*....|....*....|....*....
gi 578799215 506 LETEQRLSKERIRELQQQIEDLQKSLQEQ 534
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERL 419
|
|
| HkD_Gipie |
cd22230 |
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar ... |
36-159 |
2.93e-07 |
|
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar proteins; Gipie, also called coiled-coil domain-containing protein 88B (CCDC88B), or brain leucine zipper domain-containing protein, or Hook-related protein 3 (HkRP3), is a novel actin cytoskeleton-binding protein and Akt substrate that regulates cell migratory responses in various biological contexts. It acts as a positive regulator of T-cell maturation and inflammatory function. As a microtubule-binding protein, Gipie regulates lytic granule clustering and NK cell killing.
Pssm-ID: 411801 Cd Length: 170 Bit Score: 50.60 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 36 QLTSGVAMAQVLHQIDAawfNESWLSRIKEDVGDNWRiKASNVKKVLQGIMSYYHEFLGQQISEALiPDL-----NQITE 110
Cdd:cd22230 46 RLSNGDLLNRVMGIIDP---SPRGGPRMRGDDGPAAH-RVQNLHILWGRLRDFYQEELQQLILSPP-PDLqvmgrDPFTE 120
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 578799215 111 CSdPVELGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQEL 159
Cdd:cd22230 121 EA-VQELEKLLRLLLGAAVQCERRELFIRHIQGLDLDVQAELAEAIQEV 168
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
290-534 |
4.29e-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: 53.15 E-value: 4.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 290 DELTSLAEETRALKDEIDVLRatsDKANKLESTVEIYRQKLQDLNdlrKQVKTLQEtnmmymhntvSLEEELKKANAART 369
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQ---SELRRIENRLDELSQELSDAS---RKIGEIEK----------EIEQLEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 370 QLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKE---------KERLIEQRDTLKETNEELRCSQVQQDHL 440
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlndlearlsHSRIPEIQAELSKLEEEVSRIEARLREI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 441 NQTDASATKSYENLAAEImpvEYREVFIRLQHENKMLRLQQEGSENERIEELQEQLEQKHRKMNELETEQRLSKERIREL 520
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEI---QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL 894
|
250
....*....|....
gi 578799215 521 QQQIEDLQKSLQEQ 534
Cdd:TIGR02169 895 EAQLRELERKIEEL 908
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
317-549 |
4.52e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 4.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 317 NKLESTveiyRQKLQDLNDLRKQVKTlqetnmmymhNTVSLEEELKKANAARTqletYKRQVQDLHVKLSSesKRADTLA 396
Cdd:COG1196 179 RKLEAT----EENLERLEDILGELER----------QLEPLERQAEKAERYRE----LKEELKELEAELLL--LKLRELE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 397 FEMKRLEEKHEALLKEKERLIEQRDTLKETNEELRcsqVQQDHLNQTDASATKSYENLAAEImpveyrevfIRLQHENKM 476
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELR---LELEELELELEEAQAEEYELLAEL---------ARLEQDIAR 306
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578799215 477 LRLQQEGSEnERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKSEGESKSSHAWR 549
Cdd:COG1196 307 LEERRRELE-ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
171-528 |
6.57e-07 |
|
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: 52.43 E-value: 6.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 171 DAVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVT-------------TLQDEKNSLVSENEMMNE-KLDQLDGSF 236
Cdd:pfam15921 342 DKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQklladlhkrekelSLEKEQNKRLWDRDTGNSiTIDHLRREL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 237 DDPNTVVAkkyfhaqlqleqlqeenfRLEAAKDDYRVHCE-ELEKQLIEFQHRNDELTSLAEETRalkdeidvlratsdk 315
Cdd:pfam15921 422 DDRNMEVQ------------------RLEALLKAMKSECQgQMERQMAAIQGKNESLEKVSSLTA--------------- 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 316 anKLESTVEIYRQKLQDLndlrkqvktlqetnmmymhntvsleeelkkaNAARTQLETYKRQVQDLHVKLSSESKRADTL 395
Cdd:pfam15921 469 --QLESTKEMLRKVVEEL-------------------------------TAKKMTLESSERTVSDLTASLQEKERAIEAT 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 396 AFEMKRLEEKHEALLKEKERlieqrdtLKETNEELRCSQVQQDHLNQTDASATKSYEnlaaeimpveyrevFIRLQHENK 475
Cdd:pfam15921 516 NAEITKLRSRVDLKLQELQH-------LKNEGDHLRNVQTECEALKLQMAEKDKVIE--------------ILRQQIENM 574
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 578799215 476 MLRLQQEGSENERIEELQEQLEQ----KHRKMNELETEQRLSKERIRELQQQIEDLQ 528
Cdd:pfam15921 575 TQLVGQHGRTAGAMQVEKAQLEKeindRRLELQEFKILKDKKDAKIRELEARVSDLE 631
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
181-533 |
7.57e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 7.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 181 KRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGS----------FDDPNTVVAKKYFHA 250
Cdd:PRK03918 380 RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgreLTEEHRKELLEEYTA 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 251 QLQLEQLQEEnfRLEAAKDDYRVHCEELEKQLIEfQHRNDELTSLAEETRALKDEIDVLratsdKANKLESTVEIYRQKL 330
Cdd:PRK03918 460 ELKRIEKELK--EIEEKERKLRKELRELEKVLKK-ESELIKLKELAEQLKELEEKLKKY-----NLEELEKKAEEYEKLK 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 331 QDLNDLRKQVKtlqetnmmymhntvSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFE-MKRLEEKHEAL 409
Cdd:PRK03918 532 EKLIKLKGEIK--------------SLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFEsVEELEERLKEL 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 410 LKEKERLIEQRDTLKETNEELRCSQVQQDHLNQTDA----------SATKSYENLAAEIMPVEYREVfirlqhENKMLRL 479
Cdd:PRK03918 598 EPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEelaetekrleELRKELEELEKKYSEEEYEEL------REEYLEL 671
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 578799215 480 QQE-GSENERIEELQEQLEQKHRKMNELETEqrlsKERIRELQQQIEDLQKSLQE 533
Cdd:PRK03918 672 SRElAGLRAELEELEKRREEIKKTLEKLKEE----LEEREKAKKELEKLEKALER 722
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
163-534 |
1.22e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 163 EILSSPPNDAVGELEQQLKRALEELQEALAEKEELRQRCEELDmqvttlqdeknSLVSENEMMNEKLDQLDGSFDDPNTV 242
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEAD-----------EVLEEHEERREELETLEAEIEDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 243 VAKKyfhaqlqleqlqeenfrlEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRAT-SDKANKLES 321
Cdd:PRK02224 267 IAET------------------EREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREElEDRDEELRD 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 322 TVEIYRQKLQDLND----LRKQVKTLQETNMMYMHNTVSLEEELKkanAARTQLETYKRQVQDLHVKLSSESKRADTLAF 397
Cdd:PRK02224 329 RLEECRVAAQAHNEeaesLREDADDLEERAEELREEAAELESELE---EAREAVEDRREEIEELEEEIEELRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 398 EMKRLEEKHEALLKEKERLIEQRDTLKETNEELR--------------CSQVQQDHLNQTDASATKSYENLAAEImpvEY 463
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEATLRTARerveeaealleagkCPECGQPVEGSPHVETIEEDRERVEEL---EA 482
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578799215 464 REVFIRLQH---ENKMLRLQQEGSENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQ 534
Cdd:PRK02224 483 ELEDLEEEVeevEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEK 556
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
368-549 |
1.34e-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: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 368 RTQLETYKRQV------QDLHVKLssESKRADTLAFEMKRLEEKHEALLKEKERLIEQRDT----LKETNEELRCSQVQQ 437
Cdd:TIGR02168 199 ERQLKSLERQAekaeryKELKAEL--RELELALLVLRLEELREELEELQEELKEAEEELEEltaeLQELEEKLEELRLEV 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 438 DHLNQTDASATKSYENLAAEIMPVEYREVFIRlqheNKMLRLQQEgsenerIEELQEQLEQKHRKMNELETEQRLSKERI 517
Cdd:TIGR02168 277 SELEEEIEELQKELYALANEISRLEQQKQILR----ERLANLERQ------LEELEAQLEELESKLDELAEELAELEEKL 346
|
170 180 190
....*....|....*....|....*....|..
gi 578799215 518 RELQQQIEDLQKSLQEQGSKSEGESKSSHAWR 549
Cdd:TIGR02168 347 EELKEELESLEAELEELEAELEELESRLEELE 378
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
273-533 |
1.36e-06 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 51.08 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 273 VHCEELEKQLIEFQHRndELTSLAEEtraLKDEIDVLRATSDKANKLESTVEiyRQKLQDLNDLRKQVKTlqetnmmymh 352
Cdd:PRK05771 31 VHIEDLKEELSNERLR--KLRSLLTK---LSEALDKLRSYLPKLNPLREEKK--KVSVKSLEELIKDVEE---------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 353 NTVSLEEELKKANAARTQLETYKRqvqdlhvKLSSESKRADTL-AFEMKrleekhEALLKEKERLIEQRDTLKETNEELR 431
Cdd:PRK05771 94 ELEKIEKEIKELEEEISELENEIK-------ELEQEIERLEPWgNFDLD------LSLLLGFKYVSVFVGTVPEDKLEEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 432 CSQVQQDhlNQTDASATKSYENLAAeIMPVEYREVFIRL--QHENKMLRLQQEGSENERIEELQEQLEQKHRKMNELete 509
Cdd:PRK05771 161 KLESDVE--NVEYISTDKGYVYVVV-VVLKELSDEVEEElkKLGFERLELEEEGTPSELIREIKEELEEIEKERESL--- 234
|
250 260
....*....|....*....|....
gi 578799215 510 qrlsKERIRELQQQIEDLQKSLQE 533
Cdd:PRK05771 235 ----LEELKELAKKYLEELLALYE 254
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
170-523 |
2.49e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 170 NDAVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLdgsfddpntvvAKKYFH 249
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL-----------EEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 250 AQLQLEQLQEENFRLEAAKDDYRVHCEELEKQL--IEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYR 327
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALndLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 328 QKLQDLndlrkqVKTLQETNMMYMHNTVSLEEELKKANaarTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHE 407
Cdd:TIGR02169 829 EYLEKE------IQELQEQRIDLKEQIKSIEKEIENLN---GKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 408 ALLKEKERLIEQRDTLKETNEELRCS-QVQQDHLNQTDA---------SATKSYENLAAEIMPVEYRevfIRLQHENKML 477
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAKlEALEEELSEIEDpkgedeeipEEELSLEDVQAELQRVEEE---IRALEPVNML 976
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 578799215 478 RLQQEGSENERIEELQEQLEQkhrkmneLETEQRLSKERIRELQQQ 523
Cdd:TIGR02169 977 AIQEYEEVLKRLDELKEKRAK-------LEEERKAILERIEEYEKK 1015
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
178-533 |
6.37e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 6.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 178 QQLKRALEELQEALA----EKEELRQRCEELDMQVTTLQDEKNSLVSE-------NEMMNEKLDQLDGSFDDPNTVVAKK 246
Cdd:PRK02224 254 ETLEAEIEDLRETIAeterEREELAEEVRDLRERLEELEEERDDLLAEaglddadAEAVEARREELEDRDEELRDRLEEC 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 247 YFHAQLQLEQLQEENFR---LEAAKDDYRVHCEELEKqliEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTV 323
Cdd:PRK02224 334 RVAAQAHNEEAESLREDaddLEERAEELREEAAELES---ELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 324 EIYRQKLQ-DLNDLRKQVKTLqETNMMYMHNTVSLEEELKKA-------------------NAARTQLETYKRQVQDLHV 383
Cdd:PRK02224 411 EDFLEELReERDELREREAEL-EATLRTARERVEEAEALLEAgkcpecgqpvegsphvetiEEDRERVEELEAELEDLEE 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 384 KLSSESKRADTL------AFEMKRLEEKHEALlkeKERLIEQRDTLKETNEELRCSQVQQDHLN----QTDASATKSYEN 453
Cdd:PRK02224 490 EVEEVEERLERAedlveaEDRIERLEERREDL---EELIAERRETIEEKRERAEELRERAAELEaeaeEKREAAAEAEEE 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 454 LAAEIMPV-----EYREVFIRLQHENKMLRLQQEGSENE-RIEELQEQLEQKhrkmNELETEQRlskERIRELQQQIEDL 527
Cdd:PRK02224 567 AEEAREEVaelnsKLAELKERIESLERIRTLLAAIADAEdEIERLREKREAL----AELNDERR---ERLAEKRERKREL 639
|
....*.
gi 578799215 528 QKSLQE 533
Cdd:PRK02224 640 EAEFDE 645
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
171-526 |
6.52e-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: 48.95 E-value: 6.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 171 DAVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVT-----------TLQDEKNSLVSENEMMNEKLDQLDGSFDDP 239
Cdd:pfam05483 268 DKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQrsmstqkaleeDLQIATKTICQLTEEKEAQMEELNKAKAAH 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 240 NTVVAKKYFHAQLQLEQLQEENFRLEAAKDDYRVHCEELEKQLIEFQH-----RNDEL------TSLAEETRALKDEIDV 308
Cdd:pfam05483 348 SFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEmtkfkNNKEVeleelkKILAEDEKLLDEKKQF 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 309 LRATSDKANKLESTVEIYRQKLQDLNDLRKQVKTLQETNMMYMHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSE 388
Cdd:pfam05483 428 EKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQE 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 389 skrADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKETNEELR--CSQVQQDHLNQTD---ASATKSYENLAAEIMPVEY 463
Cdd:pfam05483 508 ---ASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRdeLESVREEFIQKGDevkCKLDKSEENARSIEYEVLK 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 464 REVFIRLQHENKMLRLQQEGSENERIEELQE--------------QLEQKHRKMNELETEQRLSKERIREL----QQQIE 525
Cdd:pfam05483 585 KEKQMKILENKCNNLKKQIENKNKNIEELHQenkalkkkgsaenkQLNAYEIKVNKLELELASAKQKFEEIidnyQKEIE 664
|
.
gi 578799215 526 D 526
Cdd:pfam05483 665 D 665
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
116-533 |
6.62e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 6.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 116 ELGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQELMSKEILSSPPNDAVGELEQQLKRALEELQEALAEKE 195
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 196 ELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVVAKKYFH---------AQLQLEQLQEENFRLEA 266
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglagavavlIGVEAAYEAALEAALAA 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 267 AKDDYRVHCEELEKQLIEFQHRNDE-----LTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKLQDLNDLRKQVK 341
Cdd:COG1196 547 ALQNIVVEDDEVAAAAIEYLKAAKAgratfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRT 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 342 TLQETNMMYMHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTL-AFEMKRLEEKHEALLKEKERLIEQR 420
Cdd:COG1196 627 LVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAElEELAERLAEEELELEEALLAEEEEE 706
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 421 DTLKETNEELRCSQVQQDHLNQTDASATKSYENLAAEIMPVEYREvfirlqhenkmlrLQQEGSENERIEELQEQLEQKH 500
Cdd:COG1196 707 RELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE-------------ALEELPEPPDLEELERELERLE 773
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 578799215 501 RKMNELET-------EQRLSKERIRELQQQIEDLQKSLQE 533
Cdd:COG1196 774 REIEALGPvnllaieEYEELEERYDFLSEQREDLEEARET 813
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
414-526 |
1.07e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 414 ERLIEQRDTLKETNEELRCSQVQQDHLNQTDASATKsYENLAAEIMPVEYREVFIRLQHENKMLRLQQEgseneRIEELQ 493
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLEPIRELAER-YAAARERLAELEYLRAALRLWFAQRRLELLEA-----ELEELR 301
|
90 100 110
....*....|....*....|....*....|...
gi 578799215 494 EQLEQKHRKMNELETEQRLSKERIRELQQQIED 526
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRG 334
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
244-533 |
1.17e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 244 AKKYFHAQLQLEqlqeenfRLEAAKDDYRVHCEELEKQLiefQHRNDELTSLAEETRALKDEIDVLRAtsdKANKLESTV 323
Cdd:COG1196 231 LLKLRELEAELE-------ELEAELEELEAELEELEAEL---AELEAELEELRLELEELELELEEAQA---EEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 324 EIYRQKLQDLNDLRKQvktlqetnmmymhNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAfemKRLE 403
Cdd:COG1196 298 ARLEQDIARLEERRRE-------------LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE---AELA 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 404 EKHEALLKEKERLIEQRDTLKETNEELRCSQVQQDHLNQTDASATKSYENLAAEImpveyrevfIRLQHENKMLRLQQEG 483
Cdd:COG1196 362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL---------ERLEEELEELEEALAE 432
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 578799215 484 SENERIEELQEQLEQKHRKmNELETEQRLSKERIRELQQQIEDLQKSLQE 533
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEE-AELEEEEEALLELLAELLEEAALLEAALAE 481
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
327-533 |
1.24e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 327 RQKLQDLNDLRKQVKTLQETnmmymhntvsLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKH 406
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKE----------LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 407 EALlkeKERLIEQRDTLKETneeLRCSQVQQDH------LNQTDASATKSYENLAAEIMPV------EYREVFIRLQHEN 474
Cdd:COG4942 93 AEL---RAELEAQKEELAEL---LRALYRLGRQpplallLSPEDFLDAVRRLQYLKYLAPArreqaeELRADLAELAALR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578799215 475 KMLRLQQEGSEN------ERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQE 533
Cdd:COG4942 167 AELEAERAELEAllaeleEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
263-534 |
1.27e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 263 RLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETraLKDEIDVLRATSDKANKLESTVeiyRQKLQDLNDLRKQVKT 342
Cdd:PRK04863 855 DHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADET--LADRVEEIREQLDEAEEAKRFV---QQHGNALAQLEPIVSV 929
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 343 LQETNMMYmhntvsleEELKKA-NAARTQLETYKRQVQDLhvklSSESKRADTLAFE--MKRLEEKHEALLKEKERLIEQ 419
Cdd:PRK04863 930 LQSDPEQF--------EQLKQDyQQAQQTQRDAKQQAFAL----TEVVQRRAHFSYEdaAEMLAKNSDLNEKLRQRLEQA 997
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 420 RDTLKETNEELRCSQVQQDHLNQTDASATKSYENlaaeimpveYREVFIRLQHENKMLRLQQEGSENERI----EELQEQ 495
Cdd:PRK04863 998 EQERTRAREQLRQAQAQLAQYNQVLASLKSSYDA---------KRQMLQELKQELQDLGVPADSGAEERArarrDELHAR 1068
|
250 260 270
....*....|....*....|....*....|....*....
gi 578799215 496 LEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQ 534
Cdd:PRK04863 1069 LSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEM 1107
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
391-534 |
2.68e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 391 RADTLAFEMKRLEEKHEALLKEKErlieQRDTLketneelrcSQVQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRL 470
Cdd:COG4913 226 AADALVEHFDDLERAHEALEDARE----QIELL---------EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL 292
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578799215 471 QhENKMLRLQQE-GSENERIEELQEQLEQKHRKMNELETEQRLSK-ERIRELQQQIEDLQKSLQEQ 534
Cdd:COG4913 293 L-EAELEELRAElARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEER 357
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
177-533 |
2.87e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 177 EQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLvsenemmnEKLDQLDGSFDDpntvvakkyfhaqlqleq 256
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL--------QRLAEYSWDEID------------------ 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 257 lqeenfrleaakddyrvhceelekqliefqhrndeLTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKLQDLNDL 336
Cdd:COG4913 663 -----------------------------------VASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEE 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 337 RKQvktlqetnmmymhntvsLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKE-KER 415
Cdd:COG4913 708 LDE-----------------LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERElREN 770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 416 LIEQRDTLKETNEELRcsqvqqDHLNQTDASATKSYENLAAEIMPV-----EYREVFIRLQ------HENKMLRLQQEgS 484
Cdd:COG4913 771 LEERIDALRARLNRAE------EELERAMRAFNREWPAETADLDADleslpEYLALLDRLEedglpeYEERFKELLNE-N 843
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 578799215 485 ENERIEELQEQLEQKhrkmneleteqrlskerIRELQQQIEDLQKSLQE 533
Cdd:COG4913 844 SIEFVADLLSKLRRA-----------------IREIKERIDPLNDSLKR 875
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
173-534 |
3.63e-05 |
|
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: 46.97 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 173 VGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVVAKKYFHAQL 252
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGI 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 253 QLEQLQEENFR----------LEAAKDDYRVHCEELEKQLIEFQHRNdeltslaEETRALKDEIDVLRATSDKANKLEST 322
Cdd:TIGR02168 522 LGVLSELISVDegyeaaieaaLGGRLQAVVVENLNAAKKAIAFLKQN-------ELGRVTFLPLDSIKGTEIQGNDREIL 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 323 VEIyRQKLQDLNDLRKQVKTLQEtNMMYMHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSE------SKRADTLA 396
Cdd:TIGR02168 595 KNI-EGFLGVAKDLVKFDPKLRK-ALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGgvitggSAKTNSSI 672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 397 FEMKRLEEKHEALLKEKERLIEqrdtlkETNEELRCSQVQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRLQHENKM 476
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIA------ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 578799215 477 LRLQQEGSEnerIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQ 534
Cdd:TIGR02168 747 ERIAQLSKE---LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL 801
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
298-529 |
4.12e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 298 ETRALKDEIDVLRATSDKANKLESTVEIYRQKLQDLNDLRKQVKTLQEtnmmymhntvsLEEELKKANAARTQLETYKRQ 377
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALEDAREQIELLEPIRELAERYAA-----------ARERLAELEYLRAALRLWFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 378 --VQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLIEQR-----DTLKETNEELRCSQVQQDHLNQtdasATKS 450
Cdd:COG4913 288 rrLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrgnggDRLEQLEREIERLERELEERER----RRAR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 451 YENLAAEI-MPVEY-REVFIRLQHENKMLRlqqegsenERIEELQEQLEQKHRkmnELETEQRLSKERIRELQQQIEDLQ 528
Cdd:COG4913 364 LEALLAALgLPLPAsAEEFAALRAEAAALL--------EALEEELEALEEALA---EAEAALRDLRRELRELEAEIASLE 432
|
.
gi 578799215 529 K 529
Cdd:COG4913 433 R 433
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
174-533 |
4.51e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 174 GELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVvAKKYFHAQLQ 253
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL-KEEIEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 254 LEQLQEENFRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKlqdL 333
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEE---I 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 334 NDLRKQVKTLQETNmmymHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSS-ESKRADTLAFEMKRLEEKHEALLKE 412
Cdd:PRK03918 324 NGIEERIKELEEKE----ERLEELKKKLKELEKRLEELEERHELYEEAKAKKEElERLKKRLTGLTPEKLEKELEELEKA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 413 KERLIEQRDTLKETNEELRcsqvqqdhlnQTDASATKSYENL--AAEIMPVEYREvfIRLQHENKMLR-----LQQEGSE 485
Cdd:PRK03918 400 KEEIEEEISKITARIGELK----------KEIKELKKAIEELkkAKGKCPVCGRE--LTEEHRKELLEeytaeLKRIEKE 467
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 578799215 486 NERIEELQEQLEQKHRKM-NELETEQRLSKEriRELQQQIEDLQKSLQE 533
Cdd:PRK03918 468 LKEIEEKERKLRKELRELeKVLKKESELIKL--KELAEQLKELEEKLKK 514
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
181-533 |
6.23e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 181 KRALEEL----QEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQldgsfDDPNTVVAKKYFHAQLQLEQ 256
Cdd:PTZ00121 1314 AKKADEAkkkaEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEA-----AEKKKEEAKKKADAAKKKAE 1388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 257 LQEENFRLEAAKDDYRVHCEELEKQLIEfQHRNDELTSLAEETRAlKDEIDVLRATSDKANKLESTVEiYRQKLQDLNDL 336
Cdd:PTZ00121 1389 EKKKADEAKKKAEEDKKKADELKKAAAA-KKKADEAKKKAEEKKK-ADEAKKKAEEAKKADEAKKKAE-EAKKAEEAKKK 1465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 337 RKQVKTLQETNmmymhntvSLEEELKKANAARTQLETYKRQVQDLHvKLSSESKRADTL--------AFEMKRLEEKHEA 408
Cdd:PTZ00121 1466 AEEAKKADEAK--------KKAEEAKKADEAKKKAEEAKKKADEAK-KAAEAKKKADEAkkaeeakkADEAKKAEEAKKA 1536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 409 LLKEKERLIEQRDTLKETnEELRCSQ----VQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGS 484
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKA-EELKKAEekkkAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578799215 485 ENERI--------EELQEQLEQ-------KHRKMNELETEQRLSKERIRELQQQIEDLQKSLQE 533
Cdd:PTZ00121 1616 EEAKIkaeelkkaEEEKKKVEQlkkkeaeEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE 1679
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
172-425 |
9.68e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 9.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 172 AVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFddpntvvakkyfhaq 251
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL--------------- 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 252 lqleqlqeenfrleaakddyrvhcEELEKQLIEFQHRNDELtsLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKLQ 331
Cdd:COG1196 361 ------------------------AEAEEALLEAEAELAEA--EEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 332 DLNDLRKQVKTLQEtnmmymhntvSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLK 411
Cdd:COG1196 415 RLERLEEELEELEE----------ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
250
....*....|....
gi 578799215 412 EKERLIEQRDTLKE 425
Cdd:COG1196 485 ELAEAAARLLLLLE 498
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
172-533 |
1.19e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 172 AVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDD-PNTVVAKKYFHA 250
Cdd:PRK02224 336 AAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDaPVDLGNAEDFLE 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 251 QlqleqlqeenfrLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRA------LKDE--IDVLRATSDKANKLEST 322
Cdd:PRK02224 416 E------------LREERDELREREAELEATLRTARERVEEAEALLEAGKCpecgqpVEGSphVETIEEDRERVEELEAE 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 323 VEIYRQKLQDLNDLRKQVKTLQETNMmymhntvSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMkrl 402
Cdd:PRK02224 484 LEDLEEEVEEVEERLERAEDLVEAED-------RIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEA--- 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 403 EEKHEALLKEKERLIEQRDTLKETNEELRCSQVQQDHLNQTDASATKsYENLAAEI------------MPVEYREvfiRL 470
Cdd:PRK02224 554 EEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAA-IADAEDEIerlrekrealaeLNDERRE---RL 629
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578799215 471 QHENKMLRLQQEGSENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQE 533
Cdd:PRK02224 630 AEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEE 692
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
331-534 |
1.32e-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: 45.05 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 331 QDLNDLRKQVKTLQEtnmmymhntvSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALL 410
Cdd:TIGR02168 677 REIEELEEKIEELEE----------KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 411 -------KEKERLIEQRDTLKETNEELRCS-QVQQDHLNQTDASATKSYENLAAEI-MPVEYREVFIRLQHENKMLRLQQ 481
Cdd:TIGR02168 747 eriaqlsKELTELEAEIEELEERLEEAEEElAEAEAEIEELEAQIEQLKEELKALReALDELRAELTLLNEEAANLRERL 826
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 578799215 482 EGSENE------RIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQ 534
Cdd:TIGR02168 827 ESLERRiaaterRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL 885
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
133-533 |
1.46e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 133 KKQEHIQNIMTLEESVQHVVMTAIQELMSKEILSSPPNDAVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQ 212
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 213 DEKNSLVSENEMMNEKLDQLDGSFDDpntvvAKKYFHAQLQLEQLQEENFRLEAAKDDYRVHCEELEKQLIEFQHRNDEL 292
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELKEK-----AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 293 TSLAEETRALKDEIDVLRatsdkanKLESTVEIYRQKLQDLNDLRKQVKTLqetnmmymhNTVSLEEELKKANAARTQLE 372
Cdd:PRK03918 341 EELKKKLKELEKRLEELE-------ERHELYEEAKAKKEELERLKKRLTGL---------TPEKLEKELEELEKAKEEIE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 373 TYKRQVQDLHVKLSSESKRADTLAFEMKR-----------LEEKHEALLKEK--ERLIEQRDTLKETNEELRCSQVQQDH 439
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgreLTEEHRKELLEEytAELKRIEKELKEIEEKERKLRKELRE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 440 LNQTDASATK--SYENLAAEIMPVEYR-EVFIRLQHENKMLRLQQEGSENERIEELQEQLEQKHRKMNELETEQRLSKER 516
Cdd:PRK03918 485 LEKVLKKESEliKLKELAEQLKELEEKlKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKK 564
|
410
....*....|....*..
gi 578799215 517 IRELQQQIEDLQKSLQE 533
Cdd:PRK03918 565 LDELEEELAELLKELEE 581
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
357-533 |
1.79e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 357 LEEELKKA----NAARTQLETYKRQVqdlhvKLSSESKRADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKetneelrc 432
Cdd:COG3206 180 LEEQLPELrkelEEAEAALEEFRQKN-----GLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR-------- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 433 SQVQQDHLNQTDASATKSYENLAAEIMPVE--YREVFIRLQHEN-KMLRLQQEgsenerIEELQEQLEQKHRK-MNELET 508
Cdd:COG3206 247 AQLGSGPDALPELLQSPVIQQLRAQLAELEaeLAELSARYTPNHpDVIALRAQ------IAALRAQLQQEAQRiLASLEA 320
|
170 180
....*....|....*....|....*
gi 578799215 509 EQRLSKERIRELQQQIEDLQKSLQE 533
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAE 345
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
310-533 |
2.28e-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: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 310 RATSDKANKLESTVEIYRQKLQDLNDLRKQVKTLQEtnmmymhntvsLEEELKKANAARTQLETYKRQVQDLHVKLSSes 389
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREQIELLEP-----------IRELAERYAAARERLAELEYLRAALRLWFAQ-- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 390 KRADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKETNEELRcsqvqqdhlNQTDASATKSYENLAAEI--MPVEYREVF 467
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELE---------AQIRGNGGDRLEQLEREIerLERELEERE 358
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578799215 468 IRLQHENKMLRLQQEGSENERiEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQE 533
Cdd:COG4913 359 RRRARLEALLAALGLPLPASA-EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
359-534 |
2.67e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 359 EELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLiEQRDTLKETNEELRCSQVQQD 438
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL-PLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 439 HLNQTDasatKSYENLAAEImpVEYREVFIRLQHENKMLRLQQEGSENERIEELQEQLEQKHRKMNELETEQRLSKERIR 518
Cdd:COG4717 150 ELEERL----EELRELEEEL--EELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170
....*....|....*.
gi 578799215 519 ELQQQIEDLQKSLQEQ 534
Cdd:COG4717 224 ELEEELEQLENELEAA 239
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
171-533 |
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 578799215 171 DAVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVVakkyfha 250
Cdd:PRK02224 363 EEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATL------- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 251 QLQLEQLQEENFRLEAAK-----------------DDYRVHCEELEKQLIEFQHRNDELTS---LAEETRALKDEIDVLR 310
Cdd:PRK02224 436 RTARERVEEAEALLEAGKcpecgqpvegsphvetiEEDRERVEELEAELEDLEEEVEEVEErleRAEDLVEAEDRIERLE 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 311 ATSDKANKL----ESTVEIYRQKLQDLN----DLRKQVKTLQETNMMYMHNTVSLEEELKKANAARTQLETYKRQVQDLH 382
Cdd:PRK02224 516 ERREDLEELiaerRETIEEKRERAEELReraaELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIR 595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 383 VKLSseskRADTLAFEMKRLEEKHEALL----KEKERLIEQRD---TLKETNEELRCSQVQQDHlnqtdASATKSYENLA 455
Cdd:PRK02224 596 TLLA----AIADAEDEIERLREKREALAelndERRERLAEKRErkrELEAEFDEARIEEAREDK-----ERAEEYLEQVE 666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 456 AEIMpvEYREVFIRLQH-----ENKMLRLQQEGSENERIEELQEQLEQKHRKMNELETEQRLSKERIRelQQQIEDLQKS 530
Cdd:PRK02224 667 EKLD--ELREERDDLQAeigavENELEELEELRERREALENRVEALEALYDEAEELESMYGDLRAELR--QRNVETLERM 742
|
...
gi 578799215 531 LQE 533
Cdd:PRK02224 743 LNE 745
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
161-533 |
2.79e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.81 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 161 SKEILSSPPNDAVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPN 240
Cdd:pfam02463 655 EEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKI 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 241 TVVAKKYFHAQLQLEQLQEENFRLEAAKDDYRVHCEELEKQLIEFQHRNdeltslaEETRALKDEIDVLRATSDKANKLE 320
Cdd:pfam02463 735 NEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKT-------EKLKVEEEKEEKLKAQEEELRALE 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 321 STVEIYRQKLQDLNDLRKQVKTLQETNMMYMHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMK 400
Cdd:pfam02463 808 EELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDE 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 401 RLEEKHEALLKEKERLIEQRDTLKETNEELRCSQVQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRLQ-HENKMLRL 479
Cdd:pfam02463 888 LESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEeERNKRLLL 967
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 578799215 480 QQEGSENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQE 533
Cdd:pfam02463 968 AKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
480-534 |
3.41e-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: 43.21 E-value: 3.41e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 578799215 480 QQEGSENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQ 534
Cdd:COG4942 48 KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
400-534 |
3.58e-04 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 43.44 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 400 KRLEEKHEALLKEKERLIEQRDTLKETnEELRcsQVQQDHLNQTdasATKSYENLAAEIMPVEYREVFIRLQHENKMLRL 479
Cdd:pfam13779 489 RRLRAAQERLSEALERGASDEEIAKLM-QELR--EALDDYMQAL---AEQAQQNPQDLQQPDDPNAQEMTQQDLQRMLDR 562
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 578799215 480 QQEGSENERIEELQEQLEQKHRKMNELETEQR--LSKERIRELQQQIEDLQKSLQEQ 534
Cdd:pfam13779 563 IEELARSGRRAEAQQMLSQLQQMLENLQAGQPqqQQQQGQSEMQQAMDELGDLLREQ 619
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
357-534 |
3.77e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 357 LEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKE----KERLIEQRDTLKEtneelRC 432
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeaEAEIEERREELGE-----RA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 433 SQVQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRlqHENKMLRLQQEgsENERIEELQEQLEQKHRKMNELETEQRL 512
Cdd:COG3883 93 RALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIAD--ADADLLEELKA--DKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180
....*....|....*....|..
gi 578799215 513 SKERIRELQQQIEDLQKSLQEQ 534
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAE 190
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
407-534 |
3.91e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.40 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 407 EALLKEKERLIEQRDTLKETNEELRCSQVQQDHLNQtDASATKSYENLaaeimpveyreVFIRLQHENKMLRLQQEGSE- 485
Cdd:COG3096 292 RELFGARRQLAEEQYRLVEMARELEELSARESDLEQ-DYQAASDHLNL-----------VQTALRQQEKIERYQEDLEEl 359
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 578799215 486 NERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQ 534
Cdd:COG3096 360 TERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQ 408
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
307-533 |
4.60e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 307 DVLRATSDKANKLESTVE-IYRQKLQD-LNDLRKQVKTLQETNMMYMHNTVSLEEELKKANAArtqLETYKRQVQDLhvk 384
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQIEeKEEKDLHErLNGLESELAELDEEIERYEEQREQARETRDEADEV---LEEHEERREEL--- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 385 lsseskraDTLAFEMKRLEEKHEALLKEKERLIEQRDTLKETNEELRcsqVQQDHLNQTDASATKSYENLAAEIMPVEYR 464
Cdd:PRK02224 254 --------ETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELE---EERDDLLAEAGLDDADAEAVEARREELEDR 322
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578799215 465 EVFIRLQHENKMLRLQQEGSENER----IEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQE 533
Cdd:PRK02224 323 DEELRDRLEECRVAAQAHNEEAESlredADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE 395
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
175-534 |
4.68e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 175 ELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSL---VSENEMMNEKLDQLDG--SFDDPNTV--VAKKY 247
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELeerHELYEEAKAKKEELERlkKRLTGLTPekLEKEL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 248 FHAQLQLEQLQEENFRLEAAKDDYRVHCEELEKQLIEFQ----------------HRNDELTSLAEETRALKDEIDVLRA 311
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgrelteeHRKELLEEYTAELKRIEKELKEIEE 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 312 TSDKANKLESTVEIYRQKLQDLNDLRKQVKTLQEtnmmymhntvsLEEELKKANAArtQLETYKRQVQDLHVKLSSESKR 391
Cdd:PRK03918 474 KERKLRKELRELEKVLKKESELIKLKELAEQLKE-----------LEEKLKKYNLE--ELEKKAEEYEKLKEKLIKLKGE 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 392 ADTLAFEMKRLEEkheaLLKEKERLIEQRDTLKETNEELrcsqvqqdhLNQTDASATKSYENLAAEIMPVE--YREvFIR 469
Cdd:PRK03918 541 IKSLKKELEKLEE----LKKKLAELEKKLDELEEELAEL---------LKELEELGFESVEELEERLKELEpfYNE-YLE 606
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578799215 470 LQHENKMLRlqqegSENERIEELQEQLEQKHRKMNELETeqrlskeRIRELQQQIEDLQKSLQEQ 534
Cdd:PRK03918 607 LKDAEKELE-----REEKELKKLEEELDKAFEELAETEK-------RLEELRKELEELEKKYSEE 659
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
165-393 |
5.50e-04 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 42.92 E-value: 5.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 165 LSSPpnDAVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDqldgsfddpNTVVA 244
Cdd:pfam09726 391 LSKP--DALVRLEQDIKKLKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLH---------NAVSA 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 245 KKyfhaqlqleqlqeenfrleaaKDDYRVhcEELEKQLIEFQ-HRNDELTSLAEETRALKDEIDVL-RATSDKANKLEST 322
Cdd:pfam09726 460 KQ---------------------KDKQTV--QQLEKRLKAEQeARASAEKQLAEEKKRKKEEEATAaRAVALAAASRGEC 516
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578799215 323 VEIYRQKLQdlnDLRKQVKTLQetnmmymHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRAD 393
Cdd:pfam09726 517 TESLKQRKR---ELESEIKKLT-------HDIKLKEEQIRELEIKVQELRKYKESEKDTEVLMSALSAMQD 577
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
338-552 |
6.00e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 6.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 338 KQVKTLQE--TNMMymhntvsLEEE--LKKANAARTQLETYKRqvqdLHVKLSSESKRADTLAfEMKRLEEKHEALLKEK 413
Cdd:COG4913 204 KPIGDLDDfvREYM-------LEEPdtFEAADALVEHFDDLER----AHEALEDAREQIELLE-PIRELAERYAAARERL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 414 ERLIEQRDTLK--ETNEELRCSQVQQDHLNQTDASATKSYENLAAEImpveyrevfIRLQHENKMLRLQQEGSENERIEE 491
Cdd:COG4913 272 AELEYLRAALRlwFAQRRLELLEAELEELRAELARLEAELERLEARL---------DALREELDELEAQIRGNGGDRLEQ 342
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578799215 492 LQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKSEGESKSSHAWRHLI 552
Cdd:COG4913 343 LEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEAL 403
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
107-342 |
7.67e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.22 E-value: 7.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 107 QITECSDPVE---LGRLLQLilgcAINCEKKQEHIQNIMTLEESVQHVVMTaIQELMSKEILSSPpNDAVGELEQQLKRA 183
Cdd:PRK05771 32 HIEDLKEELSnerLRKLRSL----LTKLSEALDKLRSYLPKLNPLREEKKK-VSVKSLEELIKDV-EEELEKIEKEIKEL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 184 LEELQEALAEKEELRQRCEEL------DMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVVAKKYfhaqlqleqL 257
Cdd:PRK05771 106 EEEISELENEIKELEQEIERLepwgnfDLDLSLLLGFKYVSVFVGTVPEDKLEELKLESDVENVEYISTD---------K 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 258 QEENFRLEAAKDDYRVHCEELEK---QLIEFQHR---NDELTSLAEETRALKDEIDVLRAT-SDKANKLE----STVEIY 326
Cdd:PRK05771 177 GYVYVVVVVLKELSDEVEEELKKlgfERLELEEEgtpSELIREIKEELEEIEKERESLLEElKELAKKYLeellALYEYL 256
|
250
....*....|....*.
gi 578799215 327 RQKLQDLNDLRKQVKT 342
Cdd:PRK05771 257 EIELERAEALSKFLKT 272
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
263-533 |
1.11e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 263 RLEAAKDDYRVHCEELEKQLIEfQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKLQDLNDLRKQVKT 342
Cdd:PTZ00121 1225 KAEAVKKAEEAKKDAEEAKKAE-EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKK 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 343 LQETNMMyMHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLIEQRDT 422
Cdd:PTZ00121 1304 ADEAKKK-AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA 1382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 423 LKETNEELRCS----------QVQQDHLNQTDASATKSYE--NLAAEIMPVEyrEVFIRLQHENKMLRLQQEGSENERIE 490
Cdd:PTZ00121 1383 AKKKAEEKKKAdeakkkaeedKKKADELKKAAAAKKKADEakKKAEEKKKAD--EAKKKAEEAKKADEAKKKAEEAKKAE 1460
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 578799215 491 ELQEQLEQKhRKMNELETEQRlSKERIRELQQQIEDLQKSLQE 533
Cdd:PTZ00121 1461 EAKKKAEEA-KKADEAKKKAE-EAKKADEAKKKAEEAKKKADE 1501
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
176-533 |
1.12e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.88 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 176 LEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVVAKKYFHAQLQLE 255
Cdd:TIGR00618 533 GEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLAC 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 256 QLQEENFRLEAAKDDYRVHCEELEKQLiEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTveiyRQKLQDLND 335
Cdd:TIGR00618 613 EQHALLRKLQPEQDLQDVRLHLQQCSQ-ELALKLTALHALQLTLTQERVREHALSIRVLPKELLASR----QLALQKMQS 687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 336 LRKQVKTLQETnmmymhntvsLEEELKKANAARTQLETYKRQVQDLHVKLSSE----SKRADTLAFEMKRLEEKHEALLK 411
Cdd:TIGR00618 688 EKEQLTYWKEM----------LAQCQTLLRELETHIEEYDREFNEIENASSSLgsdlAAREDALNQSLKELMHQARTVLK 757
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 412 EKErLIEQRDTLKETNEELRCSQVQqdHLNQTDASATKSYENLAAEIMPVEyREVFIRLQHENKMLRLQQEGSENERiEE 491
Cdd:TIGR00618 758 ART-EAHFNNNEEVTAALQTGAELS--HLAAEIQFFNRLREEDTHLLKTLE-AEIGQEIPSDEDILNLQCETLVQEE-EQ 832
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 578799215 492 LQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQE 533
Cdd:TIGR00618 833 FLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQL 874
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
302-528 |
1.36e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 302 LKDEIDVLRATSDKANK-LESTVEIYRQKLQDLndlRKQVKTLQETNmmymhNTVSLEEElkkANAARTQLETYKRQVQD 380
Cdd:COG3206 162 LEQNLELRREEARKALEfLEEQLPELRKELEEA---EAALEEFRQKN-----GLVDLSEE---AKLLLQQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 381 LHVKLSSESKRADTLAFEMKRLEEKHEALLKEKE--RLIEQRDTLKETNEELRcSQVQQDH--LNQTDASATKSYENLAA 456
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQSPViqQLRAQLAELEAELAELS-ARYTPNHpdVIALRAQIAALRAQLQQ 309
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578799215 457 EImpveyREVFIRLQHENKMLRlQQEGSENERIEELQEQLE---QKHRKMNELETEQRLSKERIRELQQQIEDLQ 528
Cdd:COG3206 310 EA-----QRILASLEAELEALQ-AREASLQAQLAQLEARLAelpELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
276-529 |
1.55e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 276 EELEKQLIEFQHRNDELTSLAEETRALKDE-IDVLRATSDKANKLESTVEIYRQKLQDLNDLRK----QVKTLQEtnmmy 350
Cdd:COG1340 4 DELSSSLEELEEKIEELREEIEELKEKRDElNEELKELAEKRDELNAQVKELREEAQELREKRDelneKVKELKE----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 351 mhntvSLEEELKKANAARTQLETYKRQVQDLHVKLSSEskraDTLAFEMKRLEEKHE--ALLKEKER-LIEQRDTLKETN 427
Cdd:COG1340 79 -----ERDELNEKLNELREELDELRKELAELNKAGGSI----DKLRKEIERLEWRQQteVLSPEEEKeLVEKIKELEKEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 428 EELRCSQVQQDHLNQTDASATKSYENLAAEIMPV-EYREvfIRLQHENKMLRLQQEGSE-NERIEELQEQLEQKHRKMNE 505
Cdd:COG1340 150 EKAKKALEKNEKLKELRAELKELRKEAEEIHKKIkELAE--EAQELHEEMIELYKEADElRKEADELHKEIVEAQEKADE 227
|
250 260
....*....|....*....|....
gi 578799215 506 LETEQRLSKERIRELQQQIEDLQK 529
Cdd:COG1340 228 LHEEIIELQKELRELRKELKKLRK 251
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
132-425 |
2.05e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.20 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 132 EKKQEHIQNIMTLEESVQHVVMTAIQELMSKEILSSPPNDAVGELEQQLKRALEELQEALAEKEELRQRCEEldmqvttL 211
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQI-------L 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 212 QDEKNSLVSENEMMNEKLDQLDGSFDDPNTVVAkkyfhaqlqleqlqeenfRLEAAKDDYRVHCEELEKQLIEFQHRNDE 291
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELESKLDELAEELA------------------ELEEKLEELKEELESLEAELEELEAELEE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 292 LTS----LAEETRALKDEIDVLRAtsdKANKLESTVEIYRQKLQDLNDLRKQVKTLQETNMMYMHNT--VSLEEELKKAN 365
Cdd:TIGR02168 370 LESrleeLEEQLETLRSKVAQLEL---QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAelKELQAELEELE 446
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 366 AARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKE 425
Cdd:TIGR02168 447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE 506
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
276-533 |
2.11e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 276 EELEKQlIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKLQDLNDLRKQVKTLQETNMMYMHNTV 355
Cdd:PTZ00121 1473 DEAKKK-AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADEL 1551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 356 SLEEELKKANAARtQLETYKRQVQDLHVKLssesKRADTL-AFEMKRLEEKHEALLKEKERLIEQRDtlKETNEELRCSQ 434
Cdd:PTZ00121 1552 KKAEELKKAEEKK-KAEEAKKAEEDKNMAL----RKAEEAkKAEEARIEEVMKLYEEEKKMKAEEAK--KAEEAKIKAEE 1624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 435 VQQDHLNQTDASATKSY---ENLAAEIMPVEYREVFIRLQHENKmlrlqQEGSENERIEELQEQLEQKHRKMNELETEQR 511
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKeaeEKKKAEELKKAEEENKIKAAEEAK-----KAEEDKKKAEEAKKAEEDEKKAAEALKKEAE 1699
|
250 260
....*....|....*....|..
gi 578799215 512 lSKERIRELQQQIEDLQKSLQE 533
Cdd:PTZ00121 1700 -EAKKAEELKKKEAEEKKKAEE 1720
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
178-534 |
2.22e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 178 QQLKRALEELQEALAEKEELRQRCEELDMQVTTlQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVVAKKYFHAQLQLEQL 257
Cdd:PTZ00121 1281 DELKKAEEKKKADEAKKAEEKKKADEAKKKAEE-AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEA 1359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 258 QEENFRLEAAK---DDYRVHCEELEKQlIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRqKLQDLN 334
Cdd:PTZ00121 1360 EAAEEKAEAAEkkkEEAKKKADAAKKK-AEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK-KADEAK 1437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 335 DLRKQVKTLQETNmmymhntvSLEEELKKANAARTQLETyKRQVQDLHVKlSSESKRADTLAFEMKRLEEKHEALlKEKE 414
Cdd:PTZ00121 1438 KKAEEAKKADEAK--------KKAEEAKKAEEAKKKAEE-AKKADEAKKK-AEEAKKADEAKKKAEEAKKKADEA-KKAA 1506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 415 RLIEQRDTLKETNEELRCSQVQQDHLNQTDASATKSYENLAAEimpveyrevfirlqhENKMLRLQQEGSENERIEELQE 494
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD---------------ELKKAEELKKAEEKKKAEEAKK 1571
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 578799215 495 QLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQ 534
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEE 1611
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
170-526 |
2.79e-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: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 170 NDAVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVVAKKyfh 249
Cdd:TIGR04523 334 NKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQK--- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 250 aqlqleqlqeenfrleaakdDYRVHCEELEKQLIEFQHRN--DELTSLAEETRALKDEIDVLRAtsdKANKLESTVEIYR 327
Cdd:TIGR04523 411 --------------------DEQIKKLQQEKELLEKEIERlkETIIKNNSEIKDLTNQDSVKEL---IIKNLDNTRESLE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 328 QKLQDLNDLRKQVKTLQETNMmymHNTVSLEEELKKANAARTQLEtykRQVQDLHVKLSSESKRADTLAFEMKRLEEKhe 407
Cdd:TIGR04523 468 TQLKVLSRSINKIKQNLEQKQ---KELKSKEKELKKLNEEKKELE---EKVKDLTKKISSLKEKIEKLESEKKEKESK-- 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 408 aLLKEKERLIEQRDTLKETN--EELRCSQVQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQegse 485
Cdd:TIGR04523 540 -ISDLEDELNKDDFELKKENleKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISS---- 614
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 578799215 486 nerIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIED 526
Cdd:TIGR04523 615 ---LEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKE 652
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
289-533 |
2.96e-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: 40.39 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 289 NDELTSLAEETRALKDEIDVLRATSDKANKleSTVEIYRQKLQDLNDLRKQVKTLQETNMMYmHNTVSLEEELKKAnaaR 368
Cdd:TIGR04523 102 NSDLSKINSEIKNDKEQKNKLEVELNKLEK--QKKENKKNIDKFLTEIKKKEKELEKLNNKY-NDLKKQKEELENE---L 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 369 TQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKETNEELRCSQVQ--------QDHL 440
Cdd:TIGR04523 176 NLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEktteisntQTQL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 441 NQTDASATKSYENLAAEIMPVEYREVFIR------LQHENKMLRLQQEgSENERIEELQEQLEQKHRKMNELETEQRLSK 514
Cdd:TIGR04523 256 NQLKDEQNKIKKQLSEKQKELEQNNKKIKelekqlNQLKSEISDLNNQ-KEQDWNKELKSELKNQEKKLEEIQNQISQNN 334
|
250
....*....|....*....
gi 578799215 515 ERIRELQQQIEDLQKSLQE 533
Cdd:TIGR04523 335 KIISQLNEQISQLKKELTN 353
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
262-534 |
3.93e-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: 40.00 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 262 FRLEAAKDDYRVHCEELEKQLIEFQhrnDELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQK----LQDLNDLR 337
Cdd:TIGR04523 148 KKKEKELEKLNNKYNDLKKQKEELE---NELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKnkslESQISELK 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 338 KQVKTLQETNMMYMHNTVSLEEELKKA----NAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEK 413
Cdd:TIGR04523 225 KQNNQLKDNIEKKQQEINEKTTEISNTqtqlNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 414 ERlieqrDTLKETNEELRCsqvQQDHLNQTDASATKSYENLAaeimpveyrevfiRLQHENKMLRLQQEGSENERiEELQ 493
Cdd:TIGR04523 305 EQ-----DWNKELKSELKN---QEKKLEEIQNQISQNNKIIS-------------QLNEQISQLKKELTNSESEN-SEKQ 362
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 578799215 494 EQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQ 534
Cdd:TIGR04523 363 RELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQ 403
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
170-533 |
3.96e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.11 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 170 NDAVGELEQQLKRALEELQEALAEKEELRQRCEELD---MQVTTLQDEKNSLVSENEMMNEKLDQLDgsfddpntvvakk 246
Cdd:pfam05557 110 KNELSELRRQIQRAELELQSTNSELEELQERLDLLKakaSEAEQLRQNLEKQQSSLAEAEQRIKELE------------- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 247 YFHAQLQLEQLQEENFRLEAAKddyrvhCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRA-------TSDKANKL 319
Cdd:pfam05557 177 FEIQSQEQDSEIVKNSKSELAR------IPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRklereekYREEAATL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 320 ESTVEIYRQKLQD---------LN-----DLRKQVKTLQETNMMYMHNTVSLEEELKKANAARTQLETYKRQVQdlhvkl 385
Cdd:pfam05557 251 ELEKEKLEQELQSwvklaqdtgLNlrspeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYL------ 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 386 ssesKRADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKETNEELrcsqvqQDHLNQTDASATKSYENLAAEIMPVEYRE 465
Cdd:pfam05557 325 ----KKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESY------DKELTMSNYSPQLLERIEEAEDMTQKMQA 394
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578799215 466 VFIRLQHENKMLrLQQEGSENERIEELQEQLeqKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQE 533
Cdd:pfam05557 395 HNEEMEAQLSVA-EEELGGYKQQAQTLEREL--QALRQQESLADPSYSKEEVDSLRRKLETLELERQR 459
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
398-520 |
4.23e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.84 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 398 EMKRLEEKHEALLKEKERLIEQRDTLKETNEELRcsqvqqdhlnqtdasaTKSYENLAAEIMPVEYREVFIRLQHENKML 477
Cdd:COG2433 414 EIRRLEEQVERLEAEVEELEAELEEKDERIERLE----------------RELSEARSEERREIRKDREISRLDREIERL 477
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 578799215 478 RLQQEgSENERIEELQEQLEqKHRKMNELETEQR---------LSKERIREL 520
Cdd:COG2433 478 ERELE-EERERIEELKRKLE-RLKELWKLEHSGElvpvkvvekFTKEAIRRL 527
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
176-429 |
4.50e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 39.89 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 176 LEQQLKRALEELQEALAEKEELRQRCEELDMQVTTlQDEKNSLVSEN----EMMNEKLDQLDGSFDDPNTVVAKKYFHAQ 251
Cdd:PLN02939 147 LNQARLQALEDLEKILTEKEALQGKINILEMRLSE-TDARIKLAAQEkihvEILEEQLEKLRNELLIRGATEGLCVHSLS 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 252 LQLEQLQEENFRLeaaKDDyrvhCEELEKQLIEFQHRNDELTSLAEEtRALKD------EIDVLRATSDKANKLESTVEI 325
Cdd:PLN02939 226 KELDVLKEENMLL---KDD----IQFLKAELIEVAETEERVFKLEKE-RSLLDaslrelESKFIVAQEDVSKLSPLQYDC 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 326 YRQKLQDLNDLRKQVKTLQETNMMYMHNTVSLEEELKKANAARTQLETYkrqvqdlhvKLSSEskRADTLAFEMKRLEEK 405
Cdd:PLN02939 298 WWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVS---------KFSSY--KVELLQQKLKLLEER 366
|
250 260 270
....*....|....*....|....*....|..
gi 578799215 406 HEALLKE--------KERLIEQRDTLKETNEE 429
Cdd:PLN02939 367 LQASDHEihsyiqlyQESIKEFQDTLSKLKEE 398
|
|
| Med21 |
pfam11221 |
Subunit 21 of Mediator complex; Med21 has been known as Srb7 in yeasts, hSrb7 in humans and ... |
173-210 |
4.92e-03 |
|
Subunit 21 of Mediator complex; Med21 has been known as Srb7 in yeasts, hSrb7 in humans and Trap 19 in Drosophila. The heterodimer of the two subunits Med7 and Med21 appears to act as a hinge between the middle and the tail regions of Mediator.
Pssm-ID: 463241 Cd Length: 134 Bit Score: 37.57 E-value: 4.92e-03
10 20 30
....*....|....*....|....*....|....*...
gi 578799215 173 VGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTT 210
Cdd:pfam11221 97 IKELEEELREAEEERQEAVKEKEELLKKLDELIRSVAR 134
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
476-533 |
5.64e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 39.68 E-value: 5.64e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 578799215 476 MLRLQQEgSENERIEELQEQLEQKHRKMNELETEQRL-SKERIRELQQQIEDLQKSLQE 533
Cdd:COG0542 401 RVRMEID-SKPEELDELERRLEQLEIEKEALKKEQDEaSFERLAELRDELAELEEELEA 458
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
263-431 |
5.68e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 263 RLEAAKDDYRVHCEELEKQLIEFQHR-----NDELTSLAEETRALKDEIDVLRATSDKANKLESTVE--IYRQKLQDLND 335
Cdd:COG4913 263 RYAAARERLAELEYLRAALRLWFAQRrlellEAELEELRAELARLEAELERLEARLDALREELDELEaqIRGNGGDRLEQ 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 336 LRKQVKTLQETNMMYMHNTVSLEEELK----KANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKR----LEEKHE 407
Cdd:COG4913 343 LEREIERLERELEERERRRARLEALLAalglPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAalrdLRRELR 422
|
170 180
....*....|....*....|....
gi 578799215 408 ALLKEKERLIEQRDTLKETNEELR 431
Cdd:COG4913 423 ELEAEIASLERRKSNIPARLLALR 446
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
277-534 |
5.80e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 39.55 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 277 ELEKQLIEFQhrnDELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRqklqdLNDLRKQVKTLQETNMMYMHNTVS 356
Cdd:COG3096 847 ELERELAQHR---AQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADR-----LEELREELDAAQEAQAFIQQHGKA 918
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 357 LEEELKKANAART---QLETYKRQVQDLHVKLSSESKRADTLAFEMKRLE----EKHEALLKE--------KERLIEQRD 421
Cdd:COG3096 919 LAQLEPLVAVLQSdpeQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhfsyEDAVGLLGEnsdlneklRARLEQAEE 998
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 422 TLKETNEELRCSQVQQDHLNQTDASATKSYEnlAAEIMPVEYREVFIRLQhenkmLRLQQEGSENERIE--ELQEQLEQK 499
Cdd:COG3096 999 ARREAREQLRQAQAQYSQYNQVLASLKSSRD--AKQQTLQELEQELEELG-----VQADAEAEERARIRrdELHEELSQN 1071
|
250 260 270
....*....|....*....|....*....|....*
gi 578799215 500 HRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQ 534
Cdd:COG3096 1072 RSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQE 1106
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
302-534 |
6.25e-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: 39.57 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 302 LKDEIDVLRATSDKANKLESTVEIYRQKLQDLNDLRKQVKTLQETNMMYMHNTVSLEEEL-KKANAARTQLETYKRQVQD 380
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLaKEEEELKSELLKLERRKVD 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 381 LHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKETNEELRCSQVQQDHLNQTDASATKSYEnlaaeimp 460
Cdd:pfam02463 312 DEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES-------- 383
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578799215 461 vEYREVFIRLQHENKMLRLQQEGSENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQ 534
Cdd:pfam02463 384 -ERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQ 456
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
276-533 |
6.35e-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: 39.62 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 276 EELEKQLIEFQHRNDELTSLAEE--TRALKDEIDvlratsDKANKLESTVEIYRQKLQDLNDLRKQVKTLQETNMMYMHN 353
Cdd:TIGR04523 284 KELEKQLNQLKSEISDLNNQKEQdwNKELKSELK------NQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 354 TVSLEEELKKANAA-----------RTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLIEQRDT 422
Cdd:TIGR04523 358 NSEKQRELEEKQNEieklkkenqsyKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIK 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 423 LKETNEElrcsqvqqdhLNQTDASATKSYENLaaeimpveyrEVFIRLQHENKMLRLQQEGSENERIEELQEQLEQKHRK 502
Cdd:TIGR04523 438 NNSEIKD----------LTNQDSVKELIIKNL----------DNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE 497
|
250 260 270
....*....|....*....|....*....|.
gi 578799215 503 MNELETEQRLSKERIRELQQQIEDLQKSLQE 533
Cdd:TIGR04523 498 LKKLNEEKKELEEKVKDLTKKISSLKEKIEK 528
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
179-431 |
6.72e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 6.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 179 QLKRALEELQEALAEKEELRQRCEELDMQVttlqdEKNSLVSENEMMNEKLDQLDGSFDDPNTV-VAKKYFHAQLQLEQL 257
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVL-----KKESELIKLKELAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKL 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 258 QEENFRLEAAKDDYRvHCEELEKQLIEFQHrndELTSLAEETRALKDEIDVLRATS--DKANKLESTVEIYRQKL----- 330
Cdd:PRK03918 535 IKLKGEIKSLKKELE-KLEELKKKLAELEK---KLDELEEELAELLKELEELGFESveELEERLKELEPFYNEYLelkda 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 331 -QDLNDLRKQVKTLQETnmmymhntvsLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRadTLAFEMKRLEEKHEAL 409
Cdd:PRK03918 611 eKELEREEKELKKLEEE----------LDKAFEELAETEKRLEELRKELEELEKKYSEEEYE--ELREEYLELSRELAGL 678
|
250 260
....*....|....*....|..
gi 578799215 410 LKEKERLIEQRDTLKETNEELR 431
Cdd:PRK03918 679 RAELEELEKRREEIKKTLEKLK 700
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
292-534 |
6.82e-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: 39.32 E-value: 6.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 292 LTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKLQDLNDLRKQVKTLQETNMMYMHNTVS----LEEELKKANAA 367
Cdd:pfam05483 246 LIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMStqkaLEEDLQIATKT 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 368 RTQL-ETYKRQVQDLHVKLSSESKRADTLAFEMKRLEekhEALLKEKERLIEQRDTLKETNEELRCSQVQQDHLNQTDAS 446
Cdd:pfam05483 326 ICQLtEEKEAQMEELNKAKAAHSFVVTEFEATTCSLE---ELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNN 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 447 ATKSYENLAAEIMPVEyrevfiRLQHENKML-RLQQEGSENEriEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIE 525
Cdd:pfam05483 403 KEVELEELKKILAEDE------KLLDEKKQFeKIAEELKGKE--QELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVE 474
|
....*....
gi 578799215 526 DLQKSLQEQ 534
Cdd:pfam05483 475 DLKTELEKE 483
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
306-517 |
8.14e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 8.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 306 IDVLRATSDKANKLESTVEIYRQKLQDLNDLRKQVKTlqetnmmymhntvsLEEELKKANAARTQLETYKrQVQDLHVKL 385
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEE--------------LEAELEELREELEKLEKLL-QLLPLYQEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 386 SSESKRADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKETNEELrcsqvqQDHLNQTDASATKSYENLAAeimpvEYRE 465
Cdd:COG4717 135 EALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEEL------EELLEQLSLATEEELQDLAE-----ELEE 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 578799215 466 VFIRLQHENKMLRLQQegsenERIEELQEQLEQKHRKMNELETEQRLSKERI 517
Cdd:COG4717 204 LQQRLAELEEELEEAQ-----EELEELEEELEQLENELEAAALEERLKEARL 250
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
171-528 |
9.44e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 39.17 E-value: 9.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 171 DAVGELEQqlkrALEELQEALAEKEELRQRCEEldmQVTTLQDEKNSLVSENEMMNEKLDQLDGSfddpntvvAKKYFHA 250
Cdd:COG3096 354 EDLEELTE----RLEEQEEVVEEAAEQLAEAEA---RLEAAEEEVDSLKSQLADYQQALDVQQTR--------AIQYQQA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 251 QLqleqlqeenfRLEAAK---DDYRVHCEELEKQLIEFQHRNDELTslaEETRALKDEIDVLRATS---DKANKLESTV- 323
Cdd:COG3096 419 VQ----------ALEKARalcGLPDLTPENAEDYLAAFRAKEQQAT---EEVLELEQKLSVADAARrqfEKAYELVCKIa 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 324 ---------EIYRQKLQDLNDLRKQVKTLQetnmmymhntvSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADT 394
Cdd:COG3096 486 geversqawQTARELLRRYRSQQALAQRLQ-----------QLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEE 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578799215 395 LAFEMKRLEEKHEALLKEKERLIEQRDTLKETNEELRcSQVQQdhlnqtdaSATKSYENLAAeimpveyREVFIRLQhen 474
Cdd:COG3096 555 LEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLR-ARIKE--------LAARAPAWLAA-------QDALERLR--- 615
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 578799215 475 kmlrlQQEGSENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQ 528
Cdd:COG3096 616 -----EQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLS 664
|
|
| |
