|
Name |
Accession |
Description |
Interval |
E-value |
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
184-546 |
2.03e-166 |
|
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: 483.04 E-value: 2.03e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 184 ELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQEETFRLEA 263
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 264 AKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKLLEEK 343
Cdd:pfam05622 81 ARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLGDLRRQVKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 344 NTMYMQNTVSLEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKET 423
Cdd:pfam05622 161 NAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRET 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 424 IEELRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKINQEGSDNEKIALLQSLLDDANLRK 503
Cdd:pfam05622 241 NEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLGQEGSYRERLTELQQLLEDANRRK 320
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1958684022 504 NELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDHGSRNS 546
Cdd:pfam05622 321 NELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSLLKQ 363
|
|
| HkD_Hook3 |
cd22226 |
Hook domain found in protein Hook 3 (Hook3) and similar proteins; Hook3 is an adaptor protein ... |
8-160 |
4.97e-105 |
|
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: 311.90 E-value: 4.97e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 8 ERVELCESLLTWIQTFNVDTPCQTVEDLTNGVVMSQVLQKIDPAYFDDNWLNRIKTEVGDNWRLKISNLKKILKGILDYN 87
Cdd:cd22226 1 DRAELCESLLTWIQTFNVDAPCQTVEDLTSGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958684022 88 HEILGQQINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQELMSK 160
Cdd:cd22226 81 HEILGQQINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMSK 153
|
|
| HOOK_N |
pfam19047 |
HOOK domain; This domain is found at the N-terminus of HOOK proteins. |
11-161 |
1.30e-96 |
|
HOOK domain; This domain is found at the N-terminus of HOOK proteins.
Pssm-ID: 465958 Cd Length: 151 Bit Score: 290.08 E-value: 1.30e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 11 ELCESLLTWIQTFNVDTPCQTVEDLTNGVVMSQVLQKIDPAYFDDNWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEI 90
Cdd:pfam19047 1 ELCDSLLTWLQTFNVPAPCATVEDLTDGVAMAQVLHQIDPSWFTEAWLSRIKEDVGDNWRLKVSNLKKILQSVVDYYQDV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958684022 91 LGQQINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQELMSKE 161
Cdd:pfam19047 81 LGQQISDFLLPDVNLIGEHSDPAELGRLLQLILGCAVNCEKKQEYIQQIMTLEESVQHVVMTAIQELMSKD 151
|
|
| HkD_Hook |
cd22222 |
Hook domain found in Hook family of microtubule-binding proteins; The Hook family includes ... |
13-159 |
1.07e-91 |
|
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: 277.59 E-value: 1.07e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 13 CESLLTWIQTFNVDTPCQTVEDLTNGVVMSQVLQKIDPAYFDDNWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEILG 92
Cdd:cd22222 1 CDSLLQWLQTFNLIAPHATAEDLSDGVAIAQVLNQIDPEYFSDSWLSKIKPDVGDNWRLKVSNLKKILKGIVDYYSEVLG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958684022 93 QQINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQELMS 159
Cdd:cd22222 81 QQISGFTMPDVNAIAEKEDPKELGRLLQLVLGCAVNCERKEEYIQAIMGLEESVQHVVMEAIQELMS 147
|
|
| HkD_Hook1 |
cd22225 |
Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a ... |
12-161 |
3.42e-82 |
|
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: 253.23 E-value: 3.42e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 12 LCESLLTWIQTFNVDTPCQTVEDLTNGVVMSQVLQKIDPAYFDDNWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEIL 91
Cdd:cd22225 1 LCDSLIIWLQTFNTAAPCQTVQDLTSGVAMAQVLHQIDSSWFDESWLSRIKEDVGDNWRIKMSNLKKILQGIVDYYHEFL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 92 GQQINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQELMSKE 161
Cdd:cd22225 81 DQQISEFLLPDLNRIAEHSDPVELGRLLQLILGCAVNCEKKQEHIQNIMTLEESVQHVVMTAIQELMSKE 150
|
|
| HkD_Hook2 |
cd22227 |
Hook domain found in protein Hook 2 (Hook2) and similar proteins; Hook2 is a ... |
11-160 |
6.34e-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: 6.34e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 11 ELCESLLTWIQTFNVDTPCQTVEDLTNGVVMSQVLQKIDPAYFDDNWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEI 90
Cdd:cd22227 1 ELCDSLLTWLQTFQVPSPCSSYQDLTSGVAIAQVLNRIDPSWFNEAWLGRIKEDTGDNWRLKVSNLKKILQSLLEYYQDV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 91 LGQQINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQELMSK 160
Cdd:cd22227 81 LGHQVSEDHLPDVNLIGEFSDDTELGKLLQLVLGCAISCEKKQEHIQQIMTLEESVQHVVMEAIQELLTK 150
|
|
| HkD_SF |
cd22211 |
Hook domain-containing proteins superfamily; The Hook domain superfamily includes Hook adaptor ... |
14-159 |
2.65e-55 |
|
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: 182.86 E-value: 2.65e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 14 ESLLTWIQTFNVDTPCQTVEDLTNGVVMSQVLQKIDPAYFDDNWLNriKTEVGDNWRLKISNLKKILKGILDYNHEILGQ 93
Cdd:cd22211 2 AALLAWINTFPLSSPVESLDDLSDGVVLAEILSQIDPSYFDSEWLE--SRDSSDNWVLKLNNLKKLYRSLSKYYREVLGQ 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958684022 94 QINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQELMS 159
Cdd:cd22211 80 QLSDLPLPDLSAIARDGDEEEIVKLLELVLGAAVQCENKEEYIARIQQLDESTQAELMLIIQEVLE 145
|
|
| HkD_HkRP |
cd22223 |
Hook domain found in the Hook-related protein (HkRP) family; The HkRP family includes Daple, ... |
12-157 |
3.21e-25 |
|
Hook domain found in the Hook-related protein (HkRP) family; The HkRP family includes Daple, Girdin and Gipie. Daple, also called Dvl-associating protein with a high frequency of leucine residues, or coiled-coil domain-containing protein 88C (CCDC88C), or Hook-related protein 2 (HkRP2), is a novel non-receptor nucleotide exchange factor (GEF) required for activation of guanine nucleotide-binding proteins (G-proteins) during non-canonical Wnt signaling. Girdin, also called Akt phosphorylation enhancer (APE), or coiled-coil domain-containing protein 88A (CCDC88A), or G alpha-interacting vesicle-associated protein (GIV), or Girders of actin filament, or Hook-related protein 1 (HkRP1), is a bifunctional modulator of guanine nucleotide-binding proteins (G proteins). It acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein G(i) alpha subunits. It also acts as a guanine nucleotide dissociation inhibitor for guanine nucleotide-binding protein G(s) subunit alpha GNAS. In addition, Girdin plays an essential role in cell migration. Gipie, also called GRP78-interacting protein induced by ER stress, or coiled-coil domain-containing protein 88B (CCDC88B), or brain leucine zipper domain-containing protein, or Hook-related protein 3 (HkRP3), is a novel actin cytoskeleton-binding protein and Akt substrate that regulates cell migratory responses in various biological contexts. It acts as a positive regulator of T-cell maturation and inflammatory function. As a microtubule-binding protein, Gipie regulates lytic granule clustering and NK cell killing. All family members contain a conserved globular Hook domain which folds as a variant of the helical calponin homology (CH) domain.
Pssm-ID: 411794 Cd Length: 149 Bit Score: 101.51 E-value: 3.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 12 LCESLLTWIQTFNVDTPCQ-TVEDLTNGVVMSQVLQKIDPAYFDDnwlnRIKTEVGDNWRLKISNLKKILKGILDYNHEI 90
Cdd:cd22223 2 LSSPLVTWAKTFADDGSAElSYTDLVDGVFLNNVMLQIDPRPFSE----VSNRNVDDDVNARIQNLDLLLRNIKSFYQEV 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958684022 91 LGQQINdFTLPDVNLIGEHSDA----AELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQEL 157
Cdd:cd22223 78 LQQLIV-MKLPDILTIGREPESeqslEELEKLLLLLLGCAVQCERKEEFIERIKNLDLEVQHALVACIQEV 147
|
|
| HkD_Daple |
cd22228 |
Hook domain found in Daple (Dvl-associating protein with a high frequency of leucine residues) ... |
16-157 |
1.21e-16 |
|
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: 77.27 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 16 LLTWIQTFNV-----DTPCQTVEDLTNGVVMSQVLQKIDPAYFDdnwlNRIKTEVGDNWRLKISNLKKILKGILDYNHEI 90
Cdd:cd22228 6 LVTWVKTFGPlgfgsEDKLSMYMDLVDGVFLNKIMLQIDPRPTN----QRVNKHVNNDVNLRIQNLTILVRHIKTYYQEV 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958684022 91 LgQQINDFTLPDVNLIGEH----SDAAELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQEL 157
Cdd:cd22228 82 L-QQLIVMNLPNVLMIGKDplsgKSMEEIKKMLLLVLGCAVQCERKEEFIERIKQLDIETQAAIVSHIQEV 151
|
|
| HkD_Girdin |
cd22229 |
Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation ... |
16-157 |
4.86e-13 |
|
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: 66.74 E-value: 4.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 16 LLTWIQTF-----NVDTPCQTVEDLTNGVVMSQVLQKIDPAYFDdnwlNRIKTEVGDNWRLKISNLKKILKGILDYNHEI 90
Cdd:cd22229 9 LVTWVKTFgplatGNGTPLDEYVALVDGVFLNEVMLQINPKSSN----QRVNKKVNNDASLRIQNLSILVKQIKLYYQET 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958684022 91 LgQQINDFTLPDVNLIGEH--SDAA--ELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQEL 157
Cdd:cd22229 85 L-QQLIMMSLPNVLVLGRNplSEQGteEMKKLLLLLLGCAVQCERKEEFIERIQTLDFDTKAAVAAHIQEV 154
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
260-532 |
2.89e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.15 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 260 RLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDK-VSKLEGQVESYKKKLEDL----GDLR 334
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdLARLEAEVEQLEERIAQLskelTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 335 RQVKLLEEKNTMYMQNTVSLEEEL----RKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEK 410
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIeeleAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 411 DRLRTERDSLKETIEELRCVQAQEGQLTTQglmplgSQESSDSLAAEIVTPEIREKLIRLQHENKMLKINQEGSDN---- 486
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEE------LESELEALLNERASLEEALALLRSELEELSEELRELESKRselr 914
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1958684022 487 EKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQ 532
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALE 960
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
153-428 |
6.49e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.00 E-value: 6.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 153 AIQELMSKESPVSAGNDAYVDLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSds 232
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL-- 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 233 iEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQ----SLKDEIDVLRH 308
Cdd:TIGR02168 315 -ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEeqleTLRSKVAQLEL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 309 ssdKVSKLEGQVESYKKKLEDLGdlRRQVKLLEEkntmymQNTVSLEEELRKANAARGQLETYKRQVVELQNRLSDESKK 388
Cdd:TIGR02168 394 ---QIASLNNEIERLEARLERLE--DRRERLQQE------IEELLKKLEEAELKELQAELEELEEELEELQEELERLEEA 462
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1958684022 389 ADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEELR 428
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
184-533 |
1.73e-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: 60.84 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 184 ELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQ-SDSIEDPNSPAGRRHLQLQTQLEQLQEETFRLE 262
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEElSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 263 AAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQV-ESYKKKLEDLGDLRRQVKLLE 341
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLnEEAANLRERLESLERRIAATE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 342 EKNTMYMQNTVSLEEELRKANAARGQLETY----KRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTER 417
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEELieelESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 418 DSLKETIEELRCVQAQ--------EGQLTTQGLMPLGSQESSdSLAAEIVTPEIREKLIRLQhenkmLKINQEGSDNEki 489
Cdd:TIGR02168 918 EELREKLAQLELRLEGlevridnlQERLSEEYSLTLEEAEAL-ENKIEDDEEEARRRLKRLE-----NKIKELGPVNL-- 989
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1958684022 490 allqsllddanlrknELETENRLVNQRLLEVQSQVEELQKSLQD 533
Cdd:TIGR02168 990 ---------------AAIEEYEELKERYDFLTAQKEDLTEAKET 1018
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
173-532 |
2.22e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.47 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 173 DLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLaENQILMERLnqsdsIEDPNSPAGRRHLQLQTQLE 252
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEK-----REYEGYELLKEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 253 QLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTT-----LADEAQSLKDEIDVLrhsSDKVSKLEGQVESYKKKL 327
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKkikdlGEEEQLRVKEKIGEL---EAEIASLERSIAEKEREL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 328 EDLGDLRRQVKLLEEKNTMYMQNtvsLEEELRKANAARGQLET----YKRQVVELQNRLSDESKKADKLDFEYKRLKEKV 403
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEE---LEREIEEERKRRDKLTEeyaeLKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 404 DGLQKEKDRLRTERDSLKETIEELRCVQAQ-EGQLTTQGLMPLGSQESSDSLAAEIvtPEIREKLIRLQheNKMLKINQE 482
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADlNAAIAGIEAKINELEEEKEDKALEI--KKQEWKLEQLA--ADLSKYEQE 470
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1958684022 483 GSD-NEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQ 532
Cdd:TIGR02169 471 LYDlKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
153-541 |
9.37e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.13 E-value: 9.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 153 AIQELMSKESPVSAGNDAYVDLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDS 232
Cdd:PRK02224 207 RLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 233 IEDpnspagrrhlqlqtqleqlqeetfRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQslkdeiDVLRHSSDK 312
Cdd:PRK02224 287 RLE------------------------ELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELR------DRLEECRVA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 313 VSKLEGQVESYKKKLEDLgdlrrqvkllEEKNTMYMQNTVSLEEELRkanAARGQLETYKRQVVELQNRLSDESKKADKL 392
Cdd:PRK02224 337 AQAHNEEAESLREDADDL----------EERAEELREEAAELESELE---EAREAVEDRREEIEELEEEIEELRERFGDA 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 393 DFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTpEIREKLIRLQH 472
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIE-EDRERVEELEA 482
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958684022 473 ENKMLKINQEgSDNEKIALLQSLLDDANlRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDH 541
Cdd:PRK02224 483 ELEDLEEEVE-EVEERLERAEDLVEAED-RIERLEERREDLEELIAERRETIEEKRERAEELRERAAEL 549
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
174-471 |
1.53e-08 |
|
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: 57.77 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 174 LDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDsiedpnspagRRHLQLQTQLEQ 253
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK----------ERLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 254 LQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTtlADEAQSLKDEI-DVLRHSSDKVSKLEGQVESYKKKLEDLgD 332
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE--ARLSHSRIPEIqAELSKLEEEVSRIEARLREIEQKLNRL-T 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 333 LRRQvkLLEEKntmyMQNTVSLEEEL---RKANAAR-----GQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVD 404
Cdd:TIGR02169 826 LEKE--YLEKE----IQELQEQRIDLkeqIKSIEKEienlnGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958684022 405 GLQKEKDRLRTERDSLKETIEELRC-VQAQEGQLTTQG-LMPLGSQESSDSLAAEIVTPEIREKLIRLQ 471
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAkLEALEEELSEIEdPKGEDEEIPEEELSLEDVQAELQRVEEEIR 968
|
|
| HkD_Gipie |
cd22230 |
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar ... |
35-157 |
2.07e-08 |
|
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar proteins; Gipie, also called coiled-coil domain-containing protein 88B (CCDC88B), or brain leucine zipper domain-containing protein, or Hook-related protein 3 (HkRP3), is a novel actin cytoskeleton-binding protein and Akt substrate that regulates cell migratory responses in various biological contexts. It acts as a positive regulator of T-cell maturation and inflammatory function. As a microtubule-binding protein, Gipie regulates lytic granule clustering and NK cell killing.
Pssm-ID: 411801 Cd Length: 170 Bit Score: 54.07 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 35 LTNGVVMSQVLQKIDPAyfddNWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEILgQQINDFTLPDVNLIGEH----S 110
Cdd:cd22230 47 LSNGDLLNRVMGIIDPS----PRGGPRMRGDDGPAAHRVQNLHILWGRLRDFYQEEL-QQLILSPPPDLQVMGRDpfteE 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1958684022 111 DAAELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQEL 157
Cdd:cd22230 122 AVQELEKLLRLLLGAAVQCERRELFIRHIQGLDLDVQAELAEAIQEV 168
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
168-544 |
2.40e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 168 NDAYVDLDRQLKKtteelneaLSAKEEIAQRCHELDMQVAALQeeKSSLLAENQILMERLNQSDSIEDpnspagrrhlql 247
Cdd:TIGR02168 192 EDILNELERQLKS--------LERQAEKAERYKELKAELRELE--LALLVLRLEELREELEELQEELK------------ 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 248 qtqleQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSlkdeidvlrhssdKVSKLEGQVESYKKKL 327
Cdd:TIGR02168 250 -----EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN-------------EISRLEQQKQILRERL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 328 EdlgDLRRQVKLLEEkntmymqntvSLEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQ 407
Cdd:TIGR02168 312 A---NLERQLEELEA----------QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 408 KEKDRLRTERDSLKETIEelrcvqaqegqlttqglmplgsqessdSLAAEIVtpEIREKLIRLQHENKMLKINQEGSDNE 487
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIA---------------------------SLNNEIE--RLEARLERLEDRRERLQQEIEELLKK 429
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958684022 488 ----KIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDHGSR 544
Cdd:TIGR02168 430 leeaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
154-540 |
1.08e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 154 IQELMSKESPVSAGNDAYVDLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSI 233
Cdd:PRK03918 209 INEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 234 EdpnsPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSS--- 310
Cdd:PRK03918 289 K----EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHely 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 311 DKVSKLEGQVESYKKKLEDL--GDLRRQVKLLEEKNTmymqntvSLEEELRKANAARGQLET----YKRQVVELQ----- 379
Cdd:PRK03918 365 EEAKAKKEELERLKKRLTGLtpEKLEKELEELEKAKE-------EIEEEISKITARIGELKKeikeLKKAIEELKkakgk 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 380 ----NRLSDESKKADKLdfeyKRLKEKVDGLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTQglmplgsqessDSLA 455
Cdd:PRK03918 438 cpvcGRELTEEHRKELL----EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKL-----------KELA 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 456 AEIVtpEIREKLIRLQHEnkmlKINQEGSDNEKI--------ALLQSLLDDANlRKNELETENRLVNQRLLEVQSQVEEL 527
Cdd:PRK03918 503 EQLK--ELEEKLKKYNLE----ELEKKAEEYEKLkekliklkGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAEL 575
|
410
....*....|...
gi 1958684022 528 QKSLQDQGSKAED 540
Cdd:PRK03918 576 LKELEELGFESVE 588
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
173-427 |
1.69e-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: 54.30 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 173 DLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAE-------------NQILMERLNQSDSIEDPNSP 239
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlshsripeiqaelSKLEEEVSRIEARLREIEQK 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 240 AGRRHLQLQTQLEQLQEETFRLEAAKDdyriRCEELEKEISELRQQNDELTTLADEAQ-SLKDEIDVLRHSSDKVSKLEG 318
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQRIDLKE----QIKSIEKEIENLNGKKEELEEELEELEaALRDLESRLGDLKKERDELEA 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 319 QVESYKKKLEDLG----DLRRQVKLLEEKNTMYMQNTVSLEEELRK---ANAARGQLETYKRQVVELQNRLSDESKKADK 391
Cdd:TIGR02169 897 QLRELERKIEELEaqieKKRKRLSELKAKLEALEEELSEIEDPKGEdeeIPEEELSLEDVQAELQRVEEEIRALEPVNML 976
|
250 260 270
....*....|....*....|....*....|....*.
gi 1958684022 392 LDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEEL 427
Cdd:TIGR02169 977 AIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
130-532 |
2.62e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 130 EQKQEYIQAIMMMEESVQHVVMTAIQELMSKESPVSAGNDAYVDLDRQLKKTTEELNEALSAKEEIAqrchELDMQVAAL 209
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIE----ELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 210 QEEKSSLLAENQILMERLNQSDS-IEDPNSPAGR---------RHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEI 279
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKeIEELEEKVKElkelkekaeEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 280 SELRQQNDELTTLADEAQSLKDEIDVLRHSS---DKVSKLEGQVESYKKKLEDL--GDLRRQVKLLEEKNTmymqntvSL 354
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEELEERHelyEEAKAKKEELERLKKRLTGLtpEKLEKELEELEKAKE-------EI 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 355 EEELRKANAARGQLET----YKRQVVELQ---------NRLSDESKKAD----------KLDFEYKRLKEKVDGLQKEKD 411
Cdd:PRK03918 404 EEEISKITARIGELKKeikeLKKAIEELKkakgkcpvcGRELTEEHRKElleeytaelkRIEKELKEIEEKERKLRKELR 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 412 RLRTERD------SLKETIEELRCVQAQegqlttqglmpLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKinqegSD 485
Cdd:PRK03918 484 ELEKVLKkeseliKLKELAEQLKELEEK-----------LKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLK-----KE 547
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1958684022 486 NEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQ-SQVEELQKSLQ 532
Cdd:PRK03918 548 LEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLK 595
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
260-540 |
2.64e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 260 RLEAAKDDY---RIRCEELEKEISELRQQndelTTLADEAQSLKDEIDVLrhssdkvsKLEGQVESYKKKLEDLGDLRRQ 336
Cdd:COG1196 180 KLEATEENLerlEDILGELERQLEPLERQ----AEKAERYRELKEELKEL--------EAELLLLKLRELEAELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 337 VKLLEEKNTMYMQNTVSLEEELRKANAARGQLEtykRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTE 416
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELE---LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 417 RDSLKETIEELrcvQAQEGQLTTQGLMplgSQESSDSLAAEIVtpEIREKLIRLQHENKMLKINQEGSDNEKIALLQSLL 496
Cdd:COG1196 325 LAELEEELEEL---EEELEELEEELEE---AEEELEEAEAELA--EAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1958684022 497 DDANLRKNELETENRLvNQRLLEVQSQVEELQKSLQDQGSKAED 540
Cdd:COG1196 397 ELAAQLEELEEAEEAL-LERLERLEEELEELEEALAELEEEEEE 439
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
318-540 |
3.14e-07 |
|
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: 52.84 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 318 GQVESYKKKLEDLGDLRRQVKLLEEKntmymqntvsLEEELRKANAARGQLETYKRQVVELQNRLsdeskkaDKLDFEYK 397
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKE----------LAALKKEEKALLKQLAALERRIAALARRI-------RALEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 398 RLKEKVDGLQKEKDRLRTERDSLKETIEELrcVQAQEGQLTTQGLMPLGSQESSDSLAA-----EIVTPEIREKLIRLQH 472
Cdd:COG4942 80 ALEAELAELEKEIAELRAELEAQKEELAEL--LRALYRLGRQPPLALLLSPEDFLDAVRrlqylKYLAPARREQAEELRA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958684022 473 ENKMLKINQEGSDNEKiALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAED 540
Cdd:COG4942 158 DLAELAALRAELEAER-AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
174-428 |
9.03e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 9.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 174 LDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDPNSpagRRHLQLQTQLEQ 253
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE---ERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 254 LQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELttLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDL 333
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEA--EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 334 RRQVKLLEEKNTMYMQNTVSLEEELRKANAARGQLEtykRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRL 413
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELE---EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
250
....*....|....*
gi 1958684022 414 RTERDSLKETIEELR 428
Cdd:COG1196 476 EAALAELLEELAEAA 490
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
173-462 |
1.66e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 173 DLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLA-----ENQILMERLNQSDSIEDpnspAGRRHLQL 247
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAelarlEQDIARLEERRRELEER----LEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 248 QTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRhsSDKVSKLEGQVESYKKKL 327
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA--EELLEALRAAAELAAQLE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 328 EDLGDLRRQVKLLEEKNTMYMQNTVSLEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQ 407
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958684022 408 KEKDRLRTERDSLKETIEE----LRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPE 462
Cdd:COG1196 484 EELAEAAARLLLLLEAEADyegfLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEA 542
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
260-534 |
2.42e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 260 RLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLkdeidvLRHSSDKVSKLEGQVESYKKKLEDLgdLRRQVKL 339
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAE------EYELLAELARLEQDIARLEERRREL--EERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 340 LEEkntmymqntvsLEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDS 419
Cdd:COG1196 322 EEE-----------LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 420 LKETIEELRcVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKINQEGSDNEKIALLQSLLDDa 499
Cdd:COG1196 391 ALRAAAELA-AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL- 468
|
250 260 270
....*....|....*....|....*....|....*
gi 1958684022 500 nLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQ 534
Cdd:COG1196 469 -LEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
273-427 |
3.06e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 273 EELEKEISELRQqndELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESykkkLEDLGDLRRQVklleekntmymqntV 352
Cdd:COG4913 613 AALEAELAELEE---ELAEAEERLEALEAELDALQERREALQRLAEYSWD----EIDVASAEREI--------------A 671
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958684022 353 SLEEELRKANAARGQLETYKRQVVELQNRLsdeskkaDKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEEL 427
Cdd:COG4913 672 ELEAELERLDASSDDLAALEEQLEELEAEL-------EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
260-499 |
4.00e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 260 RLEAAKDDYRIRCEELEKEISELRQQNDELTTLAD-------------EAQSLKDEIDVLRHSSDKVSKLEGQVESYKKK 326
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeidvasaerEIAELEAELERLDASSDDLAALEEQLEELEAE 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 327 LEDL----GDLRRQVKLLEEKNTmymqntvSLEEELRKANAARGQLETYKRQVV--ELQNRLSDESKKAdkldfeykRLK 400
Cdd:COG4913 701 LEELeeelDELKGEIGRLEKELE-------QAEEELDELQDRLEAAEDLARLELraLLEERFAAALGDA--------VER 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 401 EKVDGLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTQGLMP-LGSQESSDSLAAEIVT---PEIREKLIRLQHENKm 476
Cdd:COG4913 766 ELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDAdLESLPEYLALLDRLEEdglPEYEERFKELLNENS- 844
|
250 260
....*....|....*....|...
gi 1958684022 477 lkinqegsdNEKIALLQSLLDDA 499
Cdd:COG4913 845 ---------IEFVADLLSKLRRA 858
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
260-426 |
4.96e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 4.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 260 RLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDV-LRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVK 338
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKeIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 339 LLEEKNTMYMQNTVsLEEELRKANAargQLETYKRQVVELQNRLSdesKKADKLDFEYKRLKEKVDGLQKEKDRLRTERD 418
Cdd:COG1579 94 LQKEIESLKRRISD-LEDEILELME---RIEELEEELAELEAELA---ELEAELEEKKAELDEELAELEAELEELEAERE 166
|
....*...
gi 1958684022 419 SLKETIEE 426
Cdd:COG1579 167 ELAAKIPP 174
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
260-531 |
7.55e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 7.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 260 RLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLrhsSDKVSKLEGQVESYKKKLEDLGDLRRQVKL 339
Cdd:PRK03918 166 NLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEI---SSELPELREELEKLEKEVKELEELKEEIEE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 340 LEEKNTMYMQNTVSLEEELRKANAARGQLETYKRQVVELQNRLSDESKKAD---KLDFEYKRLKEKVDGLQKEKDRLRTE 416
Cdd:PRK03918 243 LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEeyiKLSEFYEEYLDELREIEKRLSRLEEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 417 RDSLKETIEELRCVQAQEGQLTTQglmplgSQESSDSLAAEIVTPEIREKLIRLQHENKMLKINQEGSDNEKIAllqSLL 496
Cdd:PRK03918 323 INGIEERIKELEEKEERLEELKKK------LKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLE---KEL 393
|
250 260 270
....*....|....*....|....*....|....*
gi 1958684022 497 DDANLRKNELETENRLVNQRLLEVQSQVEELQKSL 531
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKAI 428
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
283-544 |
8.02e-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: 48.91 E-value: 8.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 283 RQQNDELTTLADEAQSLKDEIDVLRhssDKVSKLEGQVESYKKKLED----LGDLRRQVKLLEEKNTMYMQNTVSLEEEL 358
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQ---SELRRIENRLDELSQELSDasrkIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 359 RKANAARgqlETYKRQVVELQNRLSDESKKADKL-----DFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEELrcvqaq 433
Cdd:TIGR02169 747 SSLEQEI---ENVKSELKELEARIEELEEDLHKLeealnDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREI------ 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 434 EGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENkmlkinqegsDNEKIALLQSLLDDANLRKNELETENRLV 513
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN----------LNGKKEELEEELEELEAALRDLESRLGDL 887
|
250 260 270
....*....|....*....|....*....|.
gi 1958684022 514 NQRLLEVQSQVEELQKSLQDQGSKAEDHGSR 544
Cdd:TIGR02169 888 KKERDELEAQLRELERKIEELEAQIEKKRKR 918
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
179-431 |
1.14e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 179 KKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIedpnspagRRHLQLQTQLEQLQEET 258
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEK--------KKAEEAKKAEEDKNMAL 1580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 259 FRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDL----- 333
Cdd:PTZ00121 1581 RKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAeeenk 1660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 334 --RRQVKLLEEKNTMYMQNTVSLEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKD 411
Cdd:PTZ00121 1661 ikAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE 1740
|
250 260
....*....|....*....|
gi 1958684022 412 RLRTERDSLKETIEELRCVQ 431
Cdd:PTZ00121 1741 EDKKKAEEAKKDEEEKKKIA 1760
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
173-427 |
1.33e-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: 48.13 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 173 DLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQ-----------SDSIEDPNSPAG 241
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaanlrerLESLERRIAATE 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 242 RRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDE-IDVLRHSSDKVSKLEGQV 320
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEElSEELRELESKRSELRREL 917
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 321 ESYKKKLEDLgDLRRQ---VKLLEEKNTMYMQNTVSLEEELRKANAARGQLETYKRQVVELQNRLSD---------Eskk 388
Cdd:TIGR02168 918 EELREKLAQL-ELRLEgleVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaaiE--- 993
|
250 260 270
....*....|....*....|....*....|....*....
gi 1958684022 389 adkldfEYKRLKEKVDGLQKEKDRLRTERDSLKETIEEL 427
Cdd:TIGR02168 994 ------EYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
154-425 |
2.11e-05 |
|
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: 47.43 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 154 IQELMSKESPVSAGNDAYVDLDRQLKKTTEELNEALSAKE-----------EIAQRCHELDMQVAALQEEKSSLLAENQI 222
Cdd:pfam05557 57 IRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKEsqladarevisCLKNELSELRRQIQRAELELQSTNSELEE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 223 LMERLNQSDS----IEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRI---------RCEELEKEISELRQQNDEL 289
Cdd:pfam05557 137 LQERLDLLKAkaseAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIvknskselaRIPELEKELERLREHNKHL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 290 TTLADEAQSLKDEIDVLRHSSDKV--------------SKLEGQVESYKKKLEDLG-------DLRRQVKLLEEKNTMYM 348
Cdd:pfam05557 217 NENIENKLLLKEEVEDLKRKLEREekyreeaatlelekEKLEQELQSWVKLAQDTGlnlrspeDLSRRIEQLQQREIVLK 296
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958684022 349 QNTVSLEEELRKANAARGQLETYKRQvveLQNRLSDESKKadkldfeYKRLKEKVDGLQKEKDRLRTERDSLKETIE 425
Cdd:pfam05557 297 EENSSLTSSARQLEKARRELEQELAQ---YLKKIEDLNKK-------LKRHKALVRRLQRRVLLLTKERDGYRAILE 363
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
360-540 |
3.12e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 360 KANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEELRCV-------QA 432
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElgeraraLY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 433 QEGQLTTQGLMPLGSQESSD----SLAAEIVTPEIREKLIRLQHENKMLKiNQEGSDNEKIALLQSLLDDANLRKNELET 508
Cdd:COG3883 97 RSGGSVSYLDVLLGSESFSDfldrLSALSKIADADADLLEELKADKAELE-AKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190
....*....|....*....|....*....|....*
gi 1958684022 509 ---ENRLVNQRLLEVQSQVEELQKSLQDQGSKAED 540
Cdd:COG3883 176 qqaEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
273-541 |
4.79e-05 |
|
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: 46.26 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 273 EELEKEISELRQQNDELTTLADEAQSLKDE-------IDVLRHSSD----KVSKLEGQVESYKKKLEdlGDLRRQVKLLE 341
Cdd:pfam15921 377 DQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDdrnmEVQRLEALLKAMKSECQ--GQMERQMAAIQ 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 342 EKN------TMYMQNTVSLEEELRKA----NAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKD 411
Cdd:pfam15921 455 GKNeslekvSSLTAQLESTKEMLRKVveelTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQ 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 412 RLRTERDSLKETIEELRCVQAQEGQ---------LTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKINQE 482
Cdd:pfam15921 535 HLKNEGDHLRNVQTECEALKLQMAEkdkvieilrQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKD 614
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958684022 483 GSDnEKIALLQSLLDDANLRKNELETEN----RLVNQRLLEVQSQVEELQKSLQDQGSKAEDH 541
Cdd:pfam15921 615 KKD-AKIRELEARVSDLELEKVKLVNAGserlRAVKDIKQERDQLLNEVKTSRNELNSLSEDY 676
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
261-428 |
6.38e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 6.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 261 LEAAKDDYRIRCEELEKEISELRQQNDeLTTLADEAQSLKDEIDVLRhssDKVSKLEGQVESYKKKLEdlgDLRRQVKLL 340
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNG-LVDLSEEAKLLLQQLSELE---SQLAEARAELAEAEARLA---ALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 341 EEKNTMYMQNTV--SLEEELRKANAARGQLET-----------YKRQVVELQNRLSDESKKA-DKLDFEYKRLKEKVDGL 406
Cdd:COG3206 253 PDALPELLQSPViqQLRAQLAELEAELAELSArytpnhpdviaLRAQIAALRAQLQQEAQRIlASLEAELEALQAREASL 332
|
170 180
....*....|....*....|..
gi 1958684022 407 QKEKDRLRTERDSLKETIEELR 428
Cdd:COG3206 333 QAQLAQLEARLAELPELEAELR 354
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
193-439 |
9.65e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 9.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 193 EEIAQRCHELDMQVAALQEEKSSL---LAENQILMERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDDYR 269
Cdd:PRK02224 471 EEDRERVEELEAELEDLEEEVEEVeerLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELE 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 270 IRCEELEKEISELRQQNDE----LTTLADEAQSLKDEIDVL---RHSSDKVSKLEGQVESYKKKLEDLGDLRRQVK-LLE 341
Cdd:PRK02224 551 AEAEEKREAAAEAEEEAEEareeVAELNSKLAELKERIESLeriRTLLAAIADAEDEIERLREKREALAELNDERReRLA 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 342 EKNTMYMQNTVSLEEE-LRKANAARGQLETYKRQVVElqnrlsdeskKADKLDFEYKRLKEKVDGLQ---KEKDRLRTER 417
Cdd:PRK02224 631 EKRERKRELEAEFDEArIEEAREDKERAEEYLEQVEE----------KLDELREERDDLQAEIGAVEnelEELEELRERR 700
|
250 260
....*....|....*....|..
gi 1958684022 418 DSLKETIEELRCVQAQEGQLTT 439
Cdd:PRK02224 701 EALENRVEALEALYDEAEELES 722
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
276-428 |
1.57e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 276 EKEISELRQQNDE--------LTTLADEAQSLKDEIDVLrhsSDKVSKLEGQVESYKKKLEDLG----DLRRQVKLLEEK 343
Cdd:PHA02562 201 NKNIEEQRKKNGEniarkqnkYDELVEEAKTIKAEIEEL---TDELLNLVMDIEDPSAALNKLNtaaaKIKSKIEQFQKV 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 344 NTMYMQNTV-----------------------SLEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLK 400
Cdd:PHA02562 278 IKMYEKGGVcptctqqisegpdritkikdklkELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLV 357
|
170 180
....*....|....*....|....*...
gi 1958684022 401 EKVDGLQKEKDRLRTERDSLKETIEELR 428
Cdd:PHA02562 358 DKAKKVKAAIEELQAEFVDNAEELAKLQ 385
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
334-428 |
1.69e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 334 RRQVKLLEEKNTMYMQNTVSLEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLK----------EKV 403
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARseerreirkdREI 467
|
90 100
....*....|....*....|....*
gi 1958684022 404 DGLQKEKDRLRTERDSLKETIEELR 428
Cdd:COG2433 468 SRLDREIERLERELEEERERIEELK 492
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
174-413 |
1.76e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 174 LDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDPnspAGRRHLQLQTQLEQ 253
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE---LRAELTLLNEEAAN 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 254 LQEETFRLEAAKDDYRIRCEELEKEISELRQQndeLTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLED-LGD 332
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSED---IESLAAEIEELEELIEELESELEALLNERASLEEALALLRSeLEE 898
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 333 LRRQVKLLEEKNTMYMQNTVSLEEELRKANAARGQLETykrQVVELQNRLSDE--------SKKADKLDFEYKRLKEKVD 404
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLELRLEGLEV---RIDNLQERLSEEysltleeaEALENKIEDDEEEARRRLK 975
|
....*....
gi 1958684022 405 GLQKEKDRL 413
Cdd:TIGR02168 976 RLENKIKEL 984
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
213-417 |
2.50e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 213 KSSLLA-ENQILMERLNQSdsIEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTT 291
Cdd:COG4717 36 KSTLLAfIRAMLLERLEKE--ADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 292 LADEAQSLKDEIDVLRHSSD------KVSKLEGQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEELRkaNAAR 365
Cdd:COG4717 114 LREELEKLEKLLQLLPLYQElealeaELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLS--LATE 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958684022 366 GQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTER 417
Cdd:COG4717 192 EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
260-533 |
2.75e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 260 RLEAAKDDY---RIRCEELEKEISELRQQNDELTTLADEA------QSLKDEIDVLRHSSDK-------------VSKLE 317
Cdd:TIGR02169 171 KKEKALEELeevEENIERLDLIIDEKRQQLERLRREREKAeryqalLKEKREYEGYELLKEKealerqkeaierqLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 318 GQVESYKKKLEDLGD-LRRQVKLLEEKNTMYMQNT----VSLEEELRKANAARGQLEtykRQVVELQNRLSDESKKADKL 392
Cdd:TIGR02169 251 EELEKLTEEISELEKrLEEIEQLLEELNKKIKDLGeeeqLRVKEKIGELEAEIASLE---RSIAEKERELEDAEERLAKL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 393 DFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEELRcvqaqegqlttqglmplgsqessdslaaeivtPEIREKLIRLQH 472
Cdd:TIGR02169 328 EAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK--------------------------------EELEDLRAELEE 375
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958684022 473 ENKMLKINQEGSDNEKIALlqsllDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQD 533
Cdd:TIGR02169 376 VDKEFAETRDELKDYREKL-----EKLKREINELKRELDRLQEELQRLSEELADLNAAIAG 431
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
273-428 |
2.82e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 273 EELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLG-----DLRRQVKLLEEKNTMY 347
Cdd:PRK03918 525 EEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfesveELEERLKELEPFYNEY 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 348 M------QNTVSLEEELRK----ANAARGQLETYKRQVVELQNRLSDESKKADKLDFE-----YKRLKEKVDGLQKEKDR 412
Cdd:PRK03918 605 LelkdaeKELEREEKELKKleeeLDKAFEELAETEKRLEELRKELEELEKKYSEEEYEelreeYLELSRELAGLRAELEE 684
|
170
....*....|....*.
gi 1958684022 413 LRTERDSLKETIEELR 428
Cdd:PRK03918 685 LEKRREEIKKTLEKLK 700
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
260-531 |
3.34e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.67 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 260 RLEAAKDDYRIRCEELEKEISELRQQ-NDELTTLADEAQSLKDEIDVLrhSSDKVSKLEGQVESYKKKLEDLGDLRRQVK 338
Cdd:pfam12128 280 ERQETSAELNQLLRTLDDQWKEKRDElNGELSAADAAVAKDRSELEAL--EDQHGAFLDADIETAAADQEQLPSWQSELE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 339 LLEEKNTMYMQNTVSLEEELRKANAARGQletykrqvvelqnrlsdeskkadkldfeykRLKEKVDGLQKEKDRLRTERD 418
Cdd:pfam12128 358 NLEERLKALTGKHQDVTAKYNRRRSKIKE------------------------------QNNRDIAGIKDKLAKIREARD 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 419 SLKETIEELrcVQAQEGQLTTQ---GLMPLGSQESSDSLAAE-----IVTPEIREKLIrLQHENKMLKIN----QEGSDN 486
Cdd:pfam12128 408 RQLAVAEDD--LQALESELREQleaGKLEFNEEEYRLKSRLGelklrLNQATATPELL-LQLENFDERIErareEQEAAN 484
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1958684022 487 EKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSL 531
Cdd:pfam12128 485 AEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQL 529
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
173-427 |
4.48e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.09 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 173 DLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQ---------------SDSIEDPN 237
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEkqneieklkkenqsyKQEIKNLE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 238 SPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSD----KV 313
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTREsletQL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 314 SKLEGQVESYKKKLED-----------LGDLRRQVKLLEEKNTMYMQNTVSLEEELRKANAARGQLEtykrqvvelqNRL 382
Cdd:TIGR04523 471 KVLSRSINKIKQNLEQkqkelkskekeLKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKE----------SKI 540
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1958684022 383 SDESKKADKLDFEYKR--LKEKVDGLQKEKDRLRTERDSLKETIEEL 427
Cdd:TIGR04523 541 SDLEDELNKDDFELKKenLEKEIDEKNKEIEELKQTQKSLKKKQEEK 587
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
273-426 |
5.11e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 273 EELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDKVSKLEG-QVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNT 351
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKkKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELK 1708
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958684022 352 VSLEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRlKEKVDGLQKEKDRLRTERDSLKETIEE 426
Cdd:PTZ00121 1709 KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE-KKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
130-528 |
6.03e-04 |
|
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: 42.80 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 130 EQKQEYI-QAIMMMEESVQHVVMT--AIQELMSKEspvsagNDAYVDLDRQLKKTTEELNEALSAKEEIAQRCHELDMQV 206
Cdd:pfam15921 102 EKQKFYLrQSVIDLQTKLQEMQMErdAMADIRRRE------SQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 207 --------AALQEEKSSLLAENQILMERLNQSDSI-----EDPNSPAGRRHLQLQTQLEQLQEETF----RLEAAKDDYR 269
Cdd:pfam15921 176 rkmmlsheGVLQEIRSILVDFEEASGKKIYEHDSMstmhfRSLGSAISKILRELDTEISYLKGRIFpvedQLEALKSESQ 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 270 IRCEEL----EKEISELRQQND-ELTTLADEAQSLKDEIDVLRHSSDKVS-KLEGQVESYKKKLEDLGDLRRQVKL-LEE 342
Cdd:pfam15921 256 NKIELLlqqhQDRIEQLISEHEvEITGLTEKASSARSQANSIQSQLEIIQeQARNQNSMYMRQLSDLESTVSQLRSeLRE 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 343 KNTMYMQNTVSLEEELRKANAARGQLETYKRQVV--------ELQNRLSDESKKADKLDFEY---KRLKEKVDGLQKEKD 411
Cdd:pfam15921 336 AKRMYEDKIEELEKQLVLANSELTEARTERDQFSqesgnlddQLQKLLADLHKREKELSLEKeqnKRLWDRDTGNSITID 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 412 RLRTERDSLKETIEELRCVQAQ-----EGQLTTQGLMPLGSQESSD---SLAAEI-VTPEIREKLIRLQHENKMLKINQE 482
Cdd:pfam15921 416 HLRRELDDRNMEVQRLEALLKAmksecQGQMERQMAAIQGKNESLEkvsSLTAQLeSTKEMLRKVVEELTAKKMTLESSE 495
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1958684022 483 GSDNEKIALLQSllddanlRKNELETENRLVNQRLLEVQSQVEELQ 528
Cdd:pfam15921 496 RTVSDLTASLQE-------KERAIEATNAEITKLRSRVDLKLQELQ 534
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
169-428 |
7.11e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 7.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 169 DAYVDLDRQLKKTTEELnEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENqilmerlnqsdsiedpnspAGRRHLQLQ 248
Cdd:COG4913 235 DDLERAHEALEDAREQI-ELLEPIRELAERYAAARERLAELEYLRAALRLWF-------------------AQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 249 TQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTlaDEAQSLKDEIDVLRhssDKVSKLEGQVESYKKKLE 328
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGG--DRLEQLEREIERLE---RELEERERRRARLEALLA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 329 DLGdlrrqvklleekntmyMQNTVSLEEELRKANAARGQLETYKRQVVELQNRLsdeskkaDKLDFEYKRLKEKVDGLQK 408
Cdd:COG4913 370 ALG----------------LPLPASAEEFAALRAEAAALLEALEEELEALEEAL-------AEAEAALRDLRRELRELEA 426
|
250 260
....*....|....*....|
gi 1958684022 409 EKDRLRTERDSLKETIEELR 428
Cdd:COG4913 427 EIASLERRKSNIPARLLALR 446
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
261-422 |
7.87e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.50 E-value: 7.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 261 LEAAKDDYRIRCEE----LEKEISELRQQNDELTTLADEAQSLKDEIDVlrhSSDKVSKLEGQVESYKKKLED----LGD 332
Cdd:pfam10174 343 LQTEVDALRLRLEEkesfLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDV---KERKINVLQKKIENLQEQLRDkdkqLAG 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 333 LRRQVKLLEEKNTMYMQNTVSLEEELRKANAArgqLETYKRQVVELQNRLSDESKKADKldfEYKRLKEKVDGLQKEKDR 412
Cdd:pfam10174 420 LKERVKSLQTDSSNTDTALTTLEEALSEKERI---IERLKEQREREDRERLEELESLKK---ENKDLKEKVSALQPELTE 493
|
170
....*....|
gi 1958684022 413 LRTERDSLKE 422
Cdd:pfam10174 494 KESSLIDLKE 503
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
190-428 |
8.80e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.22 E-value: 8.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 190 SAKEEIAQRCHELD-MQVAALQEEKSSLLAENQI-LMERLNQ-SDSIEDPNSPAGrrhlqlQTQLEQLQEETFRLEAAKD 266
Cdd:PRK05771 16 SYKDEVLEALHELGvVHIEDLKEELSNERLRKLRsLLTKLSEaLDKLRSYLPKLN------PLREEKKKVSVKSLEELIK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 267 DYRIRCEELEKEISELrqqNDELTTLADEAQSLKDEIDVLrhssdkvsklegqvesykKKLEDLG-DLRRqvkLLEEKNT 345
Cdd:PRK05771 90 DVEEELEKIEKEIKEL---EEEISELENEIKELEQEIERL------------------EPWGNFDlDLSL---LLGFKYV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 346 MYMQNTVSLE-EELRKANAARGQLETYKRQ-------VVELQNRLSDESKKADKLDF------EYKRLKEKVDGLQKEKD 411
Cdd:PRK05771 146 SVFVGTVPEDkLEELKLESDVENVEYISTDkgyvyvvVVVLKELSDEVEEELKKLGFerleleEEGTPSELIREIKEELE 225
|
250
....*....|....*..
gi 1958684022 412 RLRTERDSLKETIEELR 428
Cdd:PRK05771 226 EIEKERESLLEELKELA 242
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
270-428 |
9.47e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 9.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 270 IRCEELEKEISELRQ--QNDELTTLADEAQSLKDEIDVLRhssDKVSKLEGQVEsykkKLEDL-GDLRRQVKLLEEKNTM 346
Cdd:COG2433 373 IRGLSIEEALEELIEkeLPEEEPEAEREKEHEERELTEEE---EEIRRLEEQVE----RLEAEvEELEAELEEKDERIER 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 347 ymqntvsLEEELRKAnaargqletykrqvvelqnrlSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEE 426
Cdd:COG2433 446 -------LERELSEA---------------------RSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLER 497
|
..
gi 1958684022 427 LR 428
Cdd:COG2433 498 LK 499
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
182-438 |
1.07e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 182 TEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQsdsiedpnspagrrhlqlqtqleqlqeetfrL 261
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA-------------------------------L 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 262 EAAKDDYRIRCEELEKEISELRQQNDELTT-LADEAQSLKDEIDVL-RHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKL 339
Cdd:COG4942 68 ARRIRALEQELAALEAELAELEKEIAELRAeLEAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 340 LEEKNTMYMQNTVSLEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLdfeYKRLKEKVDGLQKEKDRLRTERDS 419
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL---LARLEKELAELAAELAELQQEAEE 224
|
250
....*....|....*....
gi 1958684022 420 LKETIEELRCVQAQEGQLT 438
Cdd:COG4942 225 LEALIARLEAEAAAAAERT 243
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
355-540 |
1.30e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.58 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 355 EEELRKANAARGQLETYKRQVVEL---QNRLSDESKKADKldfeYKRLKEKVDGLQK-----EKDRLRTERDSLKETIEE 426
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELerqLKSLERQAEKAER----YKELKAELRELELallvlRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 427 LrcvqaqegqlttqglmplgsQESSDSLAAEIVTPEIREKLIRLQHenkmlkinqeGSDNEKIALLQSLLDDANLRKNEL 506
Cdd:TIGR02168 251 A--------------------EEELEELTAELQELEEKLEELRLEV----------SELEEEIEELQKELYALANEISRL 300
|
170 180 190
....*....|....*....|....*....|....
gi 1958684022 507 ETENRLVNQRLLEVQSQVEELQKSLQDQGSKAED 540
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDE 334
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
299-537 |
1.49e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.50 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 299 LKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEEL-RKANAARGQLETYKRQVVE 377
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLaKEEEELKSELLKLERRKVD 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 378 LQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEELRCVQAQEgqlttqglmplgSQESSDSLAAE 457
Cdd:pfam02463 312 DEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKL------------EQLEEELLAKK 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 458 IVTPEIREKLIRLQHENKMLKINQEGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSK 537
Cdd:pfam02463 380 KLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELK 459
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
311-423 |
1.51e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 311 DKVSKLEGQVESYKKKLEDLGDLRRQvklLEEKNTMYMQNTVSLEEELRKANAARGQLETYKRQV-------VELQNRLS 383
Cdd:PHA02562 299 DRITKIKDKLKELQHSLEKLDTAIDE---LEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAkkvkaaiEELQAEFV 375
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1958684022 384 DESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKET 423
Cdd:PHA02562 376 DNAEELAKLQDELDKIVKTKSELVKEKYHRGIVTDLLKDS 415
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
260-437 |
1.91e-03 |
|
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: 41.26 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 260 RLEAAKDdyrIRcEELEKEISELRQQNDELTTLADEAQSLKDEidvLRHSSDKV----SKLEGQVESYKKKLEDLgdlRR 335
Cdd:pfam15921 644 RLRAVKD---IK-QERDQLLNEVKTSRNELNSLSEDYEVLKRN---FRNKSEEMetttNKLKMQLKSAQSELEQT---RN 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 336 QVKLLEEKNTMYMQNTVSLEEELrkaNAARGQLETYKRQVVELQNRLSDESKkadkldfEYKRLKEKVDGLQKEKDRLRT 415
Cdd:pfam15921 714 TLKSMEGSDGHAMKVAMGMQKQI---TAKRGQIDALQSKIQFLEEAMTNANK-------EKHFLKEEKNKLSQELSTVAT 783
|
170 180
....*....|....*....|..
gi 1958684022 416 ERDSLKETIEELRcvqAQEGQL 437
Cdd:pfam15921 784 EKNKMAGELEVLR---SQERRL 802
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
266-376 |
2.03e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 266 DDYRIRCEELEKEISELRQQNDELTtlADEAQSLKDEIDVLRhssDKVSKLEGQVESYKKKLEDLGDLRRQvklLEEKNt 345
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEQDEAS--FERLAELRDELAELE---EELEALKARWEAEKELIEEIQELKEE---LEQRY- 484
|
90 100 110
....*....|....*....|....*....|.
gi 1958684022 346 mymQNTVSLEEELRKANAARGQLETYKRQVV 376
Cdd:COG0542 485 ---GKIPELEKELAELEEELAELAPLLREEV 512
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
301-428 |
2.51e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 301 DEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEELRKANAargQLETYKRQVVELQN 380
Cdd:PRK03918 138 DAILESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEK---ELEEVLREINEISS 214
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1958684022 381 RLSDESKKADKLDFEYKRL---KEKVDGLQKEKDRLRTERDSLKETIEELR 428
Cdd:PRK03918 215 ELPELREELEKLEKEVKELeelKEEIEELEKELESLEGSKRKLEEKIRELE 265
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
261-540 |
2.81e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.59 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 261 LEAAKDDYRIRCEELEKEISELRQQNDELTT-LADEAQSLKDEIDVLR-----HSSDKVSKLEGQVESYKKKLEDLGDLR 334
Cdd:pfam12128 609 AEEALQSAREKQAAAEEQLVQANGELEKASReETFARTALKNARLDLRrlfdeKQSEKDKKNKALAERKDSANERLNSLE 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 335 RQVKLLEEKNTMYmqntvsLEEELRKANAARGQLETYKRQVVELQNRLSDESKKAdkLDFEYKRLKEKVDGLQKEKDR-- 412
Cdd:pfam12128 689 AQLKQLDKKHQAW------LEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAA--IAARRSGAKAELKALETWYKRdl 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 413 ------------LRTERDSLKETIEELrcvqAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKIN 480
Cdd:pfam12128 761 aslgvdpdviakLKREIRTLERKIERI----AVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIAD 836
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958684022 481 QEgSDNEKIALLQSLLDDANLRKNELETENRLVNQRL--LEVQSQVEELQKSLQDQGSKAED 540
Cdd:pfam12128 837 TK-LRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLatLKEDANSEQAQGSIGERLAQLED 897
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
175-411 |
2.81e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 175 DRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSiedpnspagrrhlqlqtqleql 254
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA---------------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 255 qeetfRLEAAKDDYRIRCEELEKEISELRQQNDELTTLAD--EAQSLKDEIDvlrhssdKVSKLEGQVESYKKKLEDLGD 332
Cdd:COG3883 73 -----EIAEAEAEIEERREELGERARALYRSGGSVSYLDVllGSESFSDFLD-------RLSALSKIADADADLLEELKA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958684022 333 LRRQVKLLEEKntmymqntvsLEEELRKANAARGQLETYKRqvvELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKD 411
Cdd:COG3883 141 DKAELEAKKAE----------LEAKLAELEALKAELEAAKA---ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
273-427 |
3.34e-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: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 273 EELEKEISELRQQNDELTTLADEAQSLKDEIDVLRH--SSDKVSKLEGQVESYKKKLEDL-----------GDLRRQVKL 339
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNqkEQDWNKELKSELKNQEKKLEEIqnqisqnnkiiSQLNEQISQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 340 LEEKNTMYMQNTVSLEEELRKANAA-----------RGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQK 408
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEieklkkenqsyKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
170
....*....|....*....
gi 1958684022 409 EKDRLRTERDSLKETIEEL 427
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDL 445
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
168-427 |
3.43e-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: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 168 NDAYVDLDRQLKKTTEELNEALSAKEEIAQrchELDMQVAALQEEKSSLLAENQILM-ERLNQSDSIEDPNSPAGRRHLQ 246
Cdd:TIGR04523 379 NQSYKQEIKNLESQINDLESKIQNQEKLNQ---QKDEQIKKLQQEKELLEKEIERLKeTIIKNNSEIKDLTNQDSVKELI 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 247 LQTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKK 326
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 327 LED-LGDLRRQVKLLEEKNTMYMQNTVSLE-----EELRKANAA----------------------RGQLETYKRQVVEL 378
Cdd:TIGR04523 536 KESkISDLEDELNKDDFELKKENLEKEIDEknkeiEELKQTQKSlkkkqeekqelidqkekekkdlIKEIEEKEKKISSL 615
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1958684022 379 QNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEEL 427
Cdd:TIGR04523 616 EKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEI 664
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
260-428 |
3.95e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.51 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 260 RLEAAKDDYRIRCEELEKEISELRQQNDELT----TLADEAQSLKDEID------------------VLRHSSDKVSKLE 317
Cdd:COG1340 19 ELREEIEELKEKRDELNEELKELAEKRDELNaqvkELREEAQELREKRDelnekvkelkeerdelneKLNELREELDELR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 318 GQVESYKKKLEDLGDLRRQVKLLEEKntmyMQNTV--------------SLEEELRKANAARGQLETYKR---QVVELQN 380
Cdd:COG1340 99 KELAELNKAGGSIDKLRKEIERLEWR----QQTEVlspeeekelvekikELEKELEKAKKALEKNEKLKElraELKELRK 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958684022 381 RLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEELR 428
Cdd:COG1340 175 EAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQ 222
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
166-422 |
5.48e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 39.89 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 166 AGNDAYVDLDRQLKKTTEELNEALSA-KEEIAQR-------CHELDMQVAALQEEKSSLLAENQILMERLnqsDSIEDPN 237
Cdd:PLN02939 180 SETDARIKLAAQEKIHVEILEEQLEKlRNELLIRgateglcVHSLSKELDVLKEENMLLKDDIQFLKAEL---IEVAETE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 238 SPAGRRHLQLQTQLEQLQEETFRLEAAKDDYR----IRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRhssDKV 313
Cdd:PLN02939 257 ERVFKLEKERSLLDASLRELESKFIVAQEDVSklspLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLR---DKV 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 314 SKLEGQVES---YKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSleeelrkanaargQLETYKRQVVELQ---NRLSDESK 387
Cdd:PLN02939 334 DKLEASLKEanvSKFSSYKVELLQQKLKLLEERLQASDHEIHS-------------YIQLYQESIKEFQdtlSKLKEESK 400
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958684022 388 K------ADKLDFEY-KRLKEKVDGLQKEKDRLRTERDSLKE 422
Cdd:PLN02939 401 KrslehpADDMPSEFwSRILLLIDGWLLEKKISNNDAKLLRE 442
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
273-426 |
7.41e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 38.74 E-value: 7.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 273 EELEKEISEL--RQQNDELTTlaDEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQN 350
Cdd:COG1340 112 DKLRKEIERLewRQQTEVLSP--EEEKELVEKIKELEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEE 189
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958684022 351 TVSLEEELrkaNAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEE 426
Cdd:COG1340 190 AQELHEEM---IELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEK 262
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
183-365 |
9.26e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 9.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 183 EELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDPNSPAGRRHlqlqtqleqlqeetfRLE 262
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELE---------------ALE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958684022 263 AAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVL--RHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKLL 340
Cdd:COG4717 139 AELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELleQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
170 180
....*....|....*....|....*
gi 1958684022 341 EEKNTMYMQNTVSLEEELRKANAAR 365
Cdd:COG4717 219 QEELEELEEELEQLENELEAAALEE 243
|
|
| |
