|
Name |
Accession |
Description |
Interval |
E-value |
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
184-711 |
0e+00 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 679.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 184 ELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQVLMERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQEETFRLEA 263
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 264 AKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKLLEEK 343
Cdd:pfam05622 81 ARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLGDLRRQVKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 344 NTVYMQNTVSLEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKET 423
Cdd:pfam05622 161 NAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRET 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 424 IEELRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKLNQEGSDNEKIALLQSLLDDANLRK 503
Cdd:pfam05622 241 NEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLGQEGSYRERLTELQQLLEDANRRK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 504 NELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDaiSVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFN-NSS 582
Cdd:pfam05622 321 NELETQNRLANQRILELQQQVEELQKALQEQGSKAED--SSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDsNLA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 583 LKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQLQERDRLFHSLEKEYEKTKSQREM 662
Cdd:pfam05622 399 QKIDELQEALRKKDEDMKAMEERYKKYVEKAKSVIKTLDPKQNPASPPEIQALKNQLLEKDKKIEHLERDFEKSKLQREQ 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1622960294 663 EEKYIVSAWYNMGMTLHKKAAEDRLASTGS-GQSFLARQRQATSSRRSYP 711
Cdd:pfam05622 479 EEKLIVTAWYNMGMALHRKAIEERLAGLSSpGQSFLARQRQATNARRGLS 528
|
|
| HkD_Hook3 |
cd22226 |
Hook domain found in protein Hook 3 (Hook3) and similar proteins; Hook3 is an adaptor protein ... |
8-160 |
9.32e-103 |
|
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: 311.13 E-value: 9.32e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 8 ERAELCESLLTWIQTFNVDAPWQTVEDLTNGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYN 87
Cdd:cd22226 1 DRAELCESLLTWIQTFNVDAPCQTVEDLTSGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622960294 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 |
7.72e-95 |
|
HOOK domain; This domain is found at the N-terminus of HOOK proteins.
Pssm-ID: 465958 Cd Length: 151 Bit Score: 290.46 E-value: 7.72e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 11 ELCESLLTWIQTFNVDAPWQTVEDLTNGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEI 90
Cdd:pfam19047 1 ELCDSLLTWLQTFNVPAPCATVEDLTDGVAMAQVLHQIDPSWFTEAWLSRIKEDVGDNWRLKVSNLKKILQSVVDYYQDV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622960294 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 |
4.37e-90 |
|
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: 277.98 E-value: 4.37e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 13 CESLLTWIQTFNVDAPWQTVEDLTNGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEILG 92
Cdd:cd22222 1 CDSLLQWLQTFNLIAPHATAEDLSDGVAIAQVLNQIDPEYFSDSWLSKIKPDVGDNWRLKVSNLKKILKGIVDYYSEVLG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622960294 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 |
1.78e-80 |
|
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: 252.85 E-value: 1.78e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 12 LCESLLTWIQTFNVDAPWQTVEDLTNGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEIL 91
Cdd:cd22225 1 LCDSLIIWLQTFNTAAPCQTVQDLTSGVAMAQVLHQIDSSWFDESWLSRIKEDVGDNWRIKMSNLKKILQGIVDYYHEFL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 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 |
9.98e-71 |
|
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: 227.45 E-value: 9.98e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 11 ELCESLLTWIQTFNVDAPWQTVEDLTNGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEI 90
Cdd:cd22227 1 ELCDSLLTWLQTFQVPSPCSSYQDLTSGVAIAQVLNRIDPSWFNEAWLGRIKEDTGDNWRLKVSNLKKILQSLLEYYQDV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 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 |
4.93e-53 |
|
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: 179.78 E-value: 4.93e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 14 ESLLTWIQTFNVDAPWQTVEDLTNGVVMAQVLQKIDPAYFDENWLNriKTEVGDNWRLKISNLKKILKGILDYNHEILGQ 93
Cdd:cd22211 2 AALLAWINTFPLSSPVESLDDLSDGVVLAEILSQIDPSYFDSEWLE--SRDSSDNWVLKLNNLKKLYRSLSKYYREVLGQ 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622960294 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 |
3.76e-26 |
|
Hook domain found in the Hook-related protein (HkRP) family; The HkRP family includes Daple, Girdin and Gipie. Daple, also called Dvl-associating protein with a high frequency of leucine residues, or coiled-coil domain-containing protein 88C (CCDC88C), or Hook-related protein 2 (HkRP2), is a novel non-receptor nucleotide exchange factor (GEF) required for activation of guanine nucleotide-binding proteins (G-proteins) during non-canonical Wnt signaling. Girdin, also called Akt phosphorylation enhancer (APE), or coiled-coil domain-containing protein 88A (CCDC88A), or G alpha-interacting vesicle-associated protein (GIV), or Girders of actin filament, or Hook-related protein 1 (HkRP1), is a bifunctional modulator of guanine nucleotide-binding proteins (G proteins). It acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein G(i) alpha subunits. It also acts as a guanine nucleotide dissociation inhibitor for guanine nucleotide-binding protein G(s) subunit alpha GNAS. In addition, Girdin plays an essential role in cell migration. Gipie, also called GRP78-interacting protein induced by ER stress, or coiled-coil domain-containing protein 88B (CCDC88B), or brain leucine zipper domain-containing protein, or Hook-related protein 3 (HkRP3), is a novel actin cytoskeleton-binding protein and Akt substrate that regulates cell migratory responses in various biological contexts. It acts as a positive regulator of T-cell maturation and inflammatory function. As a microtubule-binding protein, Gipie regulates lytic granule clustering and NK cell killing. All family members contain a conserved globular Hook domain which folds as a variant of the helical calponin homology (CH) domain.
Pssm-ID: 411794 Cd Length: 149 Bit Score: 104.59 E-value: 3.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 12 LCESLLTWIQTFNVDAPWQ-TVEDLTNGVVMAQVLQKIDPAYFDEnwlnRIKTEVGDNWRLKISNLKKILKGILDYNHEI 90
Cdd:cd22223 2 LSSPLVTWAKTFADDGSAElSYTDLVDGVFLNNVMLQIDPRPFSE----VSNRNVDDDVNARIQNLDLLLRNIKSFYQEV 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622960294 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 |
1.09e-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: 77.66 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 16 LLTWIQTFNV-----DAPWQTVEDLTNGVVMAQVLQKIDPAYFDEnwlnRIKTEVGDNWRLKISNLKKILKGILDYNHEI 90
Cdd:cd22228 6 LVTWVKTFGPlgfgsEDKLSMYMDLVDGVFLNKIMLQIDPRPTNQ----RVNKHVNNDVNLRIQNLTILVRHIKTYYQEV 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622960294 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 |
1.11e-12 |
|
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: 66.35 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 16 LLTWIQTFNVDAPWQTVE-----DLTNGVVMAQVLQKIDPAYFDEnwlnRIKTEVGDNWRLKISNLKKILKGILDYNHEI 90
Cdd:cd22229 9 LVTWVKTFGPLATGNGTPldeyvALVDGVFLNEVMLQINPKSSNQ----RVNKKVNNDASLRIQNLSILVKQIKLYYQET 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622960294 91 LgQQINDFTLPDVNLIGEH--SDAA--ELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQEL 157
Cdd:cd22229 85 L-QQLIMMSLPNVLVLGRNplSEQGteEMKKLLLLLLGCAVQCERKEEFIERIQTLDFDTKAAVAAHIQEV 154
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
260-635 |
8.02e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 8.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 260 RLEAAKDDY---RIRCEELEKEISELRQQndelTTLADEAQSLKDEIDVLrhssdkvsKLEGQVESYKKKLEDLGDLRRQ 336
Cdd:COG1196 180 KLEATEENLerlEDILGELERQLEPLERQ----AEKAERYRELKEELKEL--------EAELLLLKLRELEAELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 337 VKLLEEKNTVYMQNTVSLEEELRKANAARSQLEtykRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTE 416
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELE---LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 417 RDSLKETIEELrcvQAQEGQLTTQGLMplgSQESSDSLAAEIVtpEIREKLIRLQHENKMLKLNQEGSDNEKIALLQSLL 496
Cdd:COG1196 325 LAELEEELEEL---EEELEELEEELEE---AEEELEEAEAELA--EAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 497 DDANLRKNELETENRLvNQRLLEVQSQVEELQKSLQDQGSKAEDAisvllKKKLEEHLEKLHEANNELQKKRAIIEDLEP 576
Cdd:COG1196 397 ELAAQLEELEEAEEAL-LERLERLEEELEELEEALAELEEEEEEE-----EEALEEAAEEEAELEEEEEALLELLAELLE 470
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622960294 577 RFNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQAL 635
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL 529
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
130-665 |
1.18e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.17 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 130 EQKQEYIQAIMMMEESVQHVVMTAIQELMSKESPVSAGNDAYVDLDRQLKKTTEELNEALSAKEEIAqrchELDMQVAAL 209
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIE----ELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 210 QEEKSSLLAENQVLMERLNQSDS-IEDPNSPAGR---------RHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEI 279
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKeIEELEEKVKElkelkekaeEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 280 SELRQQNDELTTLADEAQSLKDEIDVLRHSS---DKVSKLEGQVESYKKKLEDL--GDLRRQVKLLEEKNTvymqntvSL 354
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEELEERHelyEEAKAKKEELERLKKRLTGLtpEKLEKELEELEKAKE-------EI 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 355 EEELRKANAARSQLET----YKRQVVELQ-------------------NRLSEESKKADKLDFEYKRLKEKVDSLQKEKD 411
Cdd:PRK03918 404 EEEISKITARIGELKKeikeLKKAIEELKkakgkcpvcgrelteehrkELLEEYTAELKRIEKELKEIEEKERKLRKELR 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 412 RLRTERD------SLKETIEELRCVQAQegqlttqglmpLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKlnqegSD 485
Cdd:PRK03918 484 ELEKVLKkeseliKLKELAEQLKELEEK-----------LKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLK-----KE 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 486 NEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQ-SQVEELQKSLQDQGSKAEDAISVL-LKKKLEEHLEKLHEANNE 563
Cdd:PRK03918 548 LEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKdAEKELEREEKELKKLEEE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 564 LQKKRAIIEDLEPRFNNSSLKIEELQealrkKEEEMKQMEERYKKYLEKAKSVirtldpkqnQGAAPEIQALKNQLQERD 643
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELEELE-----KKYSEEEYEELREEYLELSREL---------AGLRAELEELEKRREEIK 693
|
570 580
....*....|....*....|..
gi 1622960294 644 RLFHSLEKEYEKTKSQREMEEK 665
Cdd:PRK03918 694 KTLEKLKEELEEREKAKKELEK 715
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
153-661 |
2.60e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.99 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 153 AIQELMSKESPVSAGNDAYVDLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQVLMERLNQSDS 232
Cdd:PRK02224 207 RLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 233 IEDpnspagrrhlqlqtqleqlqeetfRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQslkdeiDVLRHSSDK 312
Cdd:PRK02224 287 RLE------------------------ELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELR------DRLEECRVA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 313 VSKLEGQVESYKKKLEDLgdlrrqvkllEEKNTVYMQNTVSLEEELRkanAARSQLETYKRQVVELQNRLSEESKKADKL 392
Cdd:PRK02224 337 AQAHNEEAESLREDADDL----------EERAEELREEAAELESELE---EAREAVEDRREEIEELEEEIEELRERFGDA 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 393 DFEYKRLKEKVDSLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTpEIREKLIRLQH 472
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIE-EDRERVEELEA 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 473 ENKMLKLNQEGSDN--EKIALLQSLLDDANLRKNELETENRLVNQR---LLEVQSQVEELQKSLQDQGSKAEDAISVLLK 547
Cdd:PRK02224 483 ELEDLEEEVEEVEErlERAEDLVEAEDRIERLEERREDLEELIAERretIEEKRERAEELRERAAELEAEAEEKREAAAE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 548 KKL--EEHLEKLHEANNELQKKRAIIEDLEpRFNNSSLKIEELQ---EALRKKEEEMKQMEERYKKYLEKAKSVIRTLDP 622
Cdd:PRK02224 563 AEEeaEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEdeiERLREKREALAELNDERRERLAEKRERKRELEA 641
|
490 500 510
....*....|....*....|....*....|....*....
gi 1622960294 623 KQNQGAAPEIQalknqlQERDRLFHSLEKEYEKTKSQRE 661
Cdd:PRK02224 642 EFDEARIEEAR------EDKERAEEYLEQVEEKLDELRE 674
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
260-593 |
8.03e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.85 E-value: 8.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 260 RLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDK-VSKLEGQVESYKKKLEDL----GDLR 334
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdLARLEAEVEQLEERIAQLskelTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 335 RQVKLLEEKNTVYMQNTVSLEEEL----RKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEK 410
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIeeleAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 411 DRLRTERDSLKETIEELRCVQAQEGQLTTQglmplgSQESSDSLAAEIVTPEIREKLIRLQHENKMLKLNQEGSDN---- 486
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEE------LESELEALLNERASLEEALALLRSELEELSEELRELESKRselr 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 487 EKIALLQSLLDDANLRKNELETENRLVNQRLLEVQS----QVEELQKSLQDQGSKAEDAIsvllkKKLEEHLEKLHEANN 562
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSltleEAEALENKIEDDEEEARRRL-----KRLENKIKELGPVNL 989
|
330 340 350
....*....|....*....|....*....|...
gi 1622960294 563 ElqkkrAI--IEDLEPRFNNSSLKIEELQEALR 593
Cdd:TIGR02168 990 A-----AIeeYEELKERYDFLTAQKEDLTEAKE 1017
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
371-661 |
5.34e-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: 5.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 371 YKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDR------LRTERDSLKETIEELRCVQAQEGQLTTQGLMp 444
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKaerykeLKAELRELELALLVLRLEELREELEELQEEL- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 445 LGSQESSDSLAAEIVTPEIREKLIRLQHenkmlklnqeGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQV 524
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEV----------SELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 525 EELQKSLQDQGSKAED--AISVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLKIEELQEALRKKEEEMKQM 602
Cdd:TIGR02168 319 EELEAQLEELESKLDElaEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622960294 603 EERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQLQERDRLFHSLEKEYEKTKSQRE 661
Cdd:TIGR02168 399 NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE 457
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
153-657 |
1.24e-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: 62.00 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 153 AIQELMSKESPVSAGNDAYVDLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQVLMERLNQSds 232
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL-- 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 233 iEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQ----SLKDEIDVLRH 308
Cdd:TIGR02168 315 -ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEeqleTLRSKVAQLEL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 309 ssdKVSKLEGQVESYKKKLEDLGdlRRQVKLLEEKNTVYMqntvslEEELRKANAARSQLETYKRQVVELQNRLSEESKK 388
Cdd:TIGR02168 394 ---QIASLNNEIERLEARLERLE--DRRERLQQEIEELLK------KLEEAELKELQAELEELEEELEELQEELERLEEA 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 389 ADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTQ-----GLMPLGSQ----ESSDSLAAEIV 459
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNqsglsGILGVLSElisvDEGYEAAIEAA 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 460 TPEIREKLI---------------------------------RLQHENKMLKLNQEG----------SDNEKIALLQSLL 496
Cdd:TIGR02168 543 LGGRLQAVVvenlnaakkaiaflkqnelgrvtflpldsikgtEIQGNDREILKNIEGflgvakdlvkFDPKLRKALSYLL 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 497 ---------DDANLRKNELETENRLV--------------------NQRLLEVQSQVEELQKSLQDQGSKAEDaisvlLK 547
Cdd:TIGR02168 623 ggvlvvddlDNALELAKKLRPGYRIVtldgdlvrpggvitggsaktNSSILERRREIEELEEKIEELEEKIAE-----LE 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 548 KKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLKIEEL---QEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQ 624
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLeaeVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777
|
570 580 590
....*....|....*....|....*....|....*....
gi 1622960294 625 NQGAA------PEIQALKNQLQERDRLFHSLEKEYEKTK 657
Cdd:TIGR02168 778 AEAEAeieeleAQIEQLKEELKALREALDELRAELTLLN 816
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
168-577 |
6.56e-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: 59.69 E-value: 6.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 168 NDAYVDLDRQLKKtteelneaLSAKEEIAQRCHELDMQVAALQeeKSSLLAENQVLMERLNQSDSIEDpnspagrrhlql 247
Cdd:TIGR02168 192 EDILNELERQLKS--------LERQAEKAERYKELKAELRELE--LALLVLRLEELREELEELQEELK------------ 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 248 qtqleQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSlkdeidvlrhssdKVSKLEGQVESYKKKL 327
Cdd:TIGR02168 250 -----EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN-------------EISRLEQQKQILRERL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 328 EdlgDLRRQVKLLEEkntvymqntvSLEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQ 407
Cdd:TIGR02168 312 A---NLERQLEELEA----------QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 408 KEKDRLRTERDSLKETIEelrcvqaqegqlttqglmplgsqessdSLAAEIVtpEIREKLIRLQHENKMLKLNQEGSDNE 487
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIA---------------------------SLNNEIE--RLEARLERLEDRRERLQQEIEELLKK 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 488 ----KIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDAISVL-LKKKLEEHLEKLHEANN 562
Cdd:TIGR02168 430 leeaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLdSLERLQENLEGFSEGVK 509
|
410
....*....|....*
gi 1622960294 563 ELQKKRAIIEDLEPR 577
Cdd:TIGR02168 510 ALLKNQSGLSGILGV 524
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
130-654 |
1.29e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 58.59 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 130 EQKQEYIQAIMMMEESVQHVVMT--AIQELMSKEspvsagNDAYVDLDRQLKKTTEELNEALSAKEEIaqrcheLDMQVA 207
Cdd:pfam15921 103 KQKFYLRQSVIDLQTKLQEMQMErdAMADIRRRE------SQSQEDLRNQLQNTVHELEAAKCLKEDM------LEDSNT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 208 ALQEEKSSLLAENQVLMERLNQSDSIEDPNSPAGRRHlqlqtqlEQLQEETFRLEAAKDDYRIRceELEKEISELRQQ-- 285
Cdd:pfam15921 171 QIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEH-------DSMSTMHFRSLGSAISKILR--ELDTEISYLKGRif 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 286 --NDELTTLADEAQSlKDEIdVLRHSSDKVSKLEGQVEsykkkLEDLGDLRRQVKLLEEKNTVYMQNTVSLEEelrkana 363
Cdd:pfam15921 242 pvEDQLEALKSESQN-KIEL-LLQQHQDRIEQLISEHE-----VEITGLTEKASSARSQANSIQSQLEIIQEQ------- 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 364 ARSQLETYKRQVVELQNRLSEESKKADkldfEYKRLKE-KVDSLQK-------EKDRLRTERDSLketieelrcvqaqeg 435
Cdd:pfam15921 308 ARNQNSMYMRQLSDLESTVSQLRSELR----EAKRMYEdKIEELEKqlvlansELTEARTERDQF--------------- 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 436 qlttqglmplgSQES---SDSLAAEIVTPEIREKLIRLQHENKMLKLNQEGSDNEKIALLQSLLDDANLRKNELETenrL 512
Cdd:pfam15921 369 -----------SQESgnlDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEA---L 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 513 VNQRLLEVQSQVEELQKSLQDQGSKAEDAISvlLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLKIEELQEAL 592
Cdd:pfam15921 435 LKAMKSECQGQMERQMAAIQGKNESLEKVSS--LTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAI 512
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622960294 593 RKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNqgAAPEIQALKNQLQERDRLFHSLEKEYE 654
Cdd:pfam15921 513 EATNAEITKLRSRVDLKLQELQHLKNEGDHLRN--VQTECEALKLQMAEKDKVIEILRQQIE 572
|
|
| HkD_Gipie |
cd22230 |
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar ... |
35-157 |
1.79e-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: 54.45 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 35 LTNGVVMAQVLQKIDPAYFDENWLNRikteVGDNWRLKISNLKKILKGILDYNHEILgQQINDFTLPDVNLIGEH----S 110
Cdd:cd22230 47 LSNGDLLNRVMGIIDPSPRGGPRMRG----DDGPAAHRVQNLHILWGRLRDFYQEEL-QQLILSPPPDLQVMGRDpfteE 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1622960294 111 DAAELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQEL 157
Cdd:cd22230 122 AVQELEKLLRLLLGAAVQCERRELFIRHIQGLDLDVQAELAEAIQEV 168
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
173-532 |
1.82e-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: 58.16 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 173 DLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLaENQVLMERLnqsdsIEDPNSPAGRRHLQLQTQLE 252
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEK-----REYEGYELLKEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 253 QLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTT-----LADEAQSLKDEIDVLrhsSDKVSKLEGQVESYKKKL 327
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKkikdlGEEEQLRVKEKIGEL---EAEIASLERSIAEKEREL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 328 EDLGdlRRQVKLLEEKNTVYMQNTvSLEEELRKANAARSQLET----YKRQVVELQNRLSEESKKADKLDFEYKRLKEKV 403
Cdd:TIGR02169 318 EDAE--ERLAKLEAEIDKLLAEIE-ELEREIEEERKRRDKLTEeyaeLKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 404 DSLQKEKDRLRTERDSLKETIEELRCVQAQ-EGQLTTQGLMPLGSQESSDSLAAEIvtPEIREKLIRLQheNKMLKLNQE 482
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADlNAAIAGIEAKINELEEEKEDKALEI--KKQEWKLEQLA--ADLSKYEQE 470
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1622960294 483 GSD-NEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQ 532
Cdd:TIGR02169 471 LYDlKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
260-708 |
4.04e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 4.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 260 RLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLkdeidvLRHSSDKVSKLEGQVESYKKKLEDLgdLRRQVKL 339
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAE------EYELLAELARLEQDIARLEERRREL--EERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 340 LEEkntvymqntvsLEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDS 419
Cdd:COG1196 322 EEE-----------LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 420 LKETIEELRcvqaqegqlttqglmplgSQESSDSLAAEivtpEIREKLIRLQHENKMLKLNQEGSDNEKIALLQSLLDDA 499
Cdd:COG1196 391 ALRAAAELA------------------AQLEELEEAEE----ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 500 NLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDAISVLLKKKLEEHLE-------KLHEANNELQKKRAIIE 572
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgflegvkAALLLAGLRGLAGAVAV 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 573 DLEPRFNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQN-QGAAPEIQALKNQLQERDRLFHSLEK 651
Cdd:COG1196 529 LIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKiRARAALAAALARGAIGAAVDLVASDL 608
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 652 EYEKTKSQREME---EKYIVSAWYNMGMTLHKKAAEDRLASTGSGQSFLARQRQATSSRR 708
Cdd:COG1196 609 READARYYVLGDtllGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR 668
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
304-605 |
4.17e-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: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 304 DVLRHSSDKVSKLEGQVES------YKKKLEDL------GDLRRQVKLLEEKNTVYMQNTVSLEEELRKANAARSQLETY 371
Cdd:TIGR02168 193 DILNELERQLKSLERQAEKaerykeLKAELRELelallvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 372 KRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTQglmplgSQESS 451
Cdd:TIGR02168 273 RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE------LEEKL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 452 DSLAAEIVtpEIREKLIRLQHENKMLKlnqegsdnEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSL 531
Cdd:TIGR02168 347 EELKEELE--SLEAELEELEAELEELE--------SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR 416
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622960294 532 QDQGSKAEDAISVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLKIEELQEALRKKEEEMKQMEER 605
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
174-471 |
8.31e-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: 55.84 E-value: 8.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 174 LDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQVLMERLNQSDsiedpnspagRRHLQLQTQLEQ 253
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK----------ERLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 254 LQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTtlADEAQSLKDEI-DVLRHSSDKVSKLEGQVESYKKKLEDLgD 332
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE--ARLSHSRIPEIqAELSKLEEEVSRIEARLREIEQKLNRL-T 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 333 LRRQvkLLEEKntvyMQNTVSLEEELR-KANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKD 411
Cdd:TIGR02169 826 LEKE--YLEKE----IQELQEQRIDLKeQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622960294 412 RLRTERDSLKETIEELRC--------VQAQEGQLTTQG-LMPLGSQESSDSLAAEIVTPEIREKLIRLQ 471
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKrlselkakLEALEEELSEIEdPKGEDEEIPEEELSLEDVQAELQRVEEEIR 968
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
173-664 |
8.93e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 8.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 173 DLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAEnqvLMERLNQSDSIEDPNSPAGRRHLQLQTQLE 252
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE---LARLEQDIARLEERRRELEERLEELEEELA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 253 QLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEI--DVLRHSSDKVSKLEGQVESYKKKLEDL 330
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAeeELEELAEELLEALRAAAELAAQLEELE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 331 GDLRRQVKLLEEKNTVYMQNTVSLEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEK 410
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 411 DRLRTERDSLKETIEE----LRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPE---------IREKLIRLQHENKML 477
Cdd:COG1196 487 AEAAARLLLLLEAEADyegfLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAalaaalqniVVEDDEVAAAAIEYL 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 478 KLNQEGsdneKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDAISVLLKKKLEEHLEKL 557
Cdd:COG1196 567 KAAKAG----RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTL 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 558 HEANNELQKKRAIIEDLEPRFNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKN 637
Cdd:COG1196 643 AGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELE 722
|
490 500
....*....|....*....|....*..
gi 1622960294 638 QLQERDRLFHSLEKEYEKTKSQREMEE 664
Cdd:COG1196 723 EEALEEQLEAEREELLEELLEEEELLE 749
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
269-667 |
1.38e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 269 RIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHS----SDKVSKLEGQVESYKKKLEDLGDLRRQVKLLEEKN 344
Cdd:PRK03918 213 SSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSkrklEEKIRELEERIEELKKEIEELEEKVKELKELKEKA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 345 TVYMQNTVSLEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLdfeyKRLKEKVDSLQKEKDRLRT---ERDSLK 421
Cdd:PRK03918 293 EEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL----EELKKKLKELEKRLEELEErheLYEEAK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 422 ETIEELRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKLN---------------QEGSDN 486
Cdd:PRK03918 369 AKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAieelkkakgkcpvcgRELTEE 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 487 EKIALLQS-LLDDANLRKNELETENRL--VNQRLLEVQSQVEEL-----QKSLQDQGSKAEDAISVLLKKKLE---EHLE 555
Cdd:PRK03918 449 HRKELLEEyTAELKRIEKELKEIEEKErkLRKELRELEKVLKKEselikLKELAEQLKELEEKLKKYNLEELEkkaEEYE 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 556 KLHEANNELQKKRAIIED----LEPRFNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQ----- 626
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKelekLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEylelk 608
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1622960294 627 GAAPEIQALKNQLQERDRLFHSLEKEYEKTKSQREMEEKYI 667
Cdd:PRK03918 609 DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL 649
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
238-668 |
2.28e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 238 SPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSD------ 311
Cdd:COG4717 60 KPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQElealea 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 312 KVSKLEGQVESYKKKLEDLGDLRRQVKLLEEKntvYMQNTVSLEEELRK-ANAARSQLETYKRQVVELQNRLSEESKKAD 390
Cdd:COG4717 140 ELAELPERLEELEERLEELRELEEELEELEAE---LAELQEELEELLEQlSLATEEELQDLAEELEELQQRLAELEEELE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 391 KLDFEYKRLKEKVDSLQKEKdrlrtERDSLKETIEELR----------CVQAQEGQLTTQGLMPLGSQESSDSLAAEIVT 460
Cdd:COG4717 217 EAQEELEELEEELEQLENEL-----EAAALEERLKEARlllliaaallALLGLGGSLLSLILTIAGVLFLVLGLLALLFL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 461 PEIREKLIRLQHENKMLKLN-QEGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGskAE 539
Cdd:COG4717 292 LLAREKASLGKEAEELQALPaLEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE--LE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 540 DAISVLLKK---KLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLKIEELQEALrkkeeemkqMEERYKKYLEKAKSV 616
Cdd:COG4717 370 QEIAALLAEagvEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL---------DEEELEEELEELEEE 440
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1622960294 617 IRTLDPKQNQgAAPEIQALKNQLQ--ERDRLFHSLEKEYEKTKSQ-REMEEKYIV 668
Cdd:COG4717 441 LEELEEELEE-LREELAELEAELEqlEEDGELAELLQELEELKAElRELAEEWAA 494
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
173-427 |
3.45e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.92 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 173 DLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAE-------------NQVLMERLNQSDSIEDPNSP 239
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlshsripeiqaelSKLEEEVSRIEARLREIEQK 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 240 AGRRHLQLQTQLEQLQEETFRLEAAKDdyriRCEELEKEISELRQQNDELTTLADEAQ-SLKDEIDVLRHSSDKVSKLEG 318
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQRIDLKE----QIKSIEKEIENLNGKKEELEEELEELEaALRDLESRLGDLKKERDELEA 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 319 QVESYKKKLEDLG----DLRRQVKLLEEKNTVYMQNTVSLEEELRK---ANAARSQLETYKRQVVELQNRLSEESKKADK 391
Cdd:TIGR02169 897 QLRELERKIEELEaqieKKRKRLSELKAKLEALEEELSEIEDPKGEdeeIPEEELSLEDVQAELQRVEEEIRALEPVNML 976
|
250 260 270
....*....|....*....|....*....|....*.
gi 1622960294 392 LDFEYKRLKEKVDSLQKEKDRLRTERDSLKETIEEL 427
Cdd:TIGR02169 977 AIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
304-593 |
9.39e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 9.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 304 DVLRHSSDKVSKLEGQVESYKkkleDLGDLRRQVK--LLEEKNTvyMQNTVSLEEELRKANAARSQLETYKRQV------ 375
Cdd:COG4913 184 RRLGIGSEKALRLLHKTQSFK----PIGDLDDFVReyMLEEPDT--FEAADALVEHFDDLERAHEALEDAREQIellepi 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 376 VELQNRLSEESKKADKLD-----FEYKRLKEKVDSLQKEKDRLRTERDSLKETIEELrcvQAQEGQLttqglmplgsqes 450
Cdd:COG4913 258 RELAERYAAARERLAELEylraaLRLWFAQRRLELLEAELEELRAELARLEAELERL---EARLDAL------------- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 451 sdslaaeivtpeiREKLIRLQHEnkmlklnQEGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKS 530
Cdd:COG4913 322 -------------REELDELEAQ-------IRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622960294 531 LQDQGSKAEDAISVL------LKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLKIEELQEALR 593
Cdd:COG4913 382 FAALRAEAAALLEALeeeleaLEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
354-540 |
1.11e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 354 LEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKETIEELrcVQAQ 433
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL--LRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 434 EGQLTTQGLMPLGSQESSDSLAA-----EIVTPEIREKLIRLQHENKMLKLNQEGSDNEKiALLQSLLDDANLRKNELET 508
Cdd:COG4942 114 YRLGRQPPLALLLSPEDFLDAVRrlqylKYLAPARREQAEELRADLAELAALRAELEAER-AELEALLAELEEERAALEA 192
|
170 180 190
....*....|....*....|....*....|..
gi 1622960294 509 ENRLVNQRLLEVQSQVEELQKSLQDQGSKAED 540
Cdd:COG4942 193 LKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
350-592 |
1.26e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 350 NTVSLEEELRKANAarsQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKETIEELRc 429
Cdd:TIGR02169 668 FSRSEPAELQRLRE---RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELE- 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 430 vqaQEGQLTTQGLmpLGSQESSDSLAAEIvtPEIREKLIRLQHE-----------------NKMLKLNQEGSDNE----- 487
Cdd:TIGR02169 744 ---EDLSSLEQEI--ENVKSELKELEARI--EELEEDLHKLEEAlndlearlshsripeiqAELSKLEEEVSRIEarlre 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 488 -----------------KIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDaisvlLKKKL 550
Cdd:TIGR02169 817 ieqklnrltlekeylekEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD-----LKKER 891
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1622960294 551 EEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLKIEELQEAL 592
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
260-511 |
1.92e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 260 RLEAAKDDYRIRCEELEKEISELRQQNDELTTLAD-------------EAQSLKDEIDVLRHSSDKVSKLEGQVESYKKK 326
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeidvasaerEIAELEAELERLDASSDDLAALEEQLEELEAE 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 327 LEDL----GDLRRQVKLLEEKNTvymqntvSLEEELRKANAARSQLETYKRQVV--ELQNRLSEESKKAdkldfeykRLK 400
Cdd:COG4913 701 LEELeeelDELKGEIGRLEKELE-------QAEEELDELQDRLEAAEDLARLELraLLEERFAAALGDA--------VER 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 401 EKVDSLQKEKDRLRTERDSLKETIEELRcvqaqegqLTTQGLMPLGSQESSDSLAAEivtPEIREKLIRLQ------HEN 474
Cdd:COG4913 766 ELRENLEERIDALRARLNRAEEELERAM--------RAFNREWPAETADLDADLESL---PEYLALLDRLEedglpeYEE 834
|
250 260 270
....*....|....*....|....*....|....*..
gi 1622960294 475 KMLKLNQEGSDNEKIALLQSLLDDANLRKNELETENR 511
Cdd:COG4913 835 RFKELLNENSIEFVADLLSKLRRAIREIKERIDPLND 871
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
273-593 |
2.05e-06 |
|
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: 51.27 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 273 EELEKEISELRQQNDELTTLADEAQSLKDE-------IDVLRHSSD----KVSKLEGQVESYKKKLEdlGDLRRQVKLLE 341
Cdd:pfam15921 377 DQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDdrnmEVQRLEALLKAMKSECQ--GQMERQMAAIQ 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 342 EKN------TVYMQNTVSLEEELRKA----NAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKD 411
Cdd:pfam15921 455 GKNeslekvSSLTAQLESTKEMLRKVveelTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQ 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 412 RLRTERDSLKETieelrcvqaqegqlttqglmplgsQESSDSLAAEIVTPEIREKLIRLQHENKMLKLNQEGSDNEKI-- 489
Cdd:pfam15921 535 HLKNEGDHLRNV------------------------QTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMqv 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 490 --ALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQ---KSLQDQGSKAEDAISVlLKKKLEEHLEKLHEANNEL 564
Cdd:pfam15921 591 ekAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLElekVKLVNAGSERLRAVKD-IKQERDQLLNEVKTSRNEL 669
|
330 340
....*....|....*....|....*....
gi 1622960294 565 QKKRAIIEDLEPRFNNSSLKIEELQEALR 593
Cdd:pfam15921 670 NSLSEDYEVLKRNFRNKSEEMETTTNKLK 698
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
269-616 |
2.15e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.22 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 269 RIRCEELEKEISELRQQNDELTTLADEA-QSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLgdlRRQVKLLEEKNTVY 347
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELsQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL---EEDLSSLEQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 348 MQNTVSLEEELrkaNAARSQLETYKRQVVELQNRLSEE-----SKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKE 422
Cdd:TIGR02169 757 KSELKELEARI---EELEEDLHKLEEALNDLEARLSHSripeiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEK 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 423 TIEELRCVQAQegqlttqglmpLGSQESSDSLAAEIVTPEIREKLIRL-QHENKMLKLNQEGSDNEK-IALLQSLLDDAN 500
Cdd:TIGR02169 834 EIQELQEQRID-----------LKEQIKSIEKEIENLNGKKEELEEELeELEAALRDLESRLGDLKKeRDELEAQLRELE 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 501 LRKNELETENRLVNQRLLEVQSQVEELQkslqDQGSKAEDAISVLLKKKLEE-HLEKLHEannELQKKRAIIEDLEP--- 576
Cdd:TIGR02169 903 RKIEELEAQIEKKRKRLSELKAKLEALE----EELSEIEDPKGEDEEIPEEElSLEDVQA---ELQRVEEEIRALEPvnm 975
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1622960294 577 ----RFNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSV 616
Cdd:TIGR02169 976 laiqEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
183-658 |
4.11e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 50.29 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 183 EELNEaLSAKEEIAQRcheLDMQVAALQEEKSSLLAENQVLMERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQEETFRLE 262
Cdd:PRK01156 239 SALNE-LSSLEDMKNR---YESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQIL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 263 AAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDlgdlrrqvkllEE 342
Cdd:PRK01156 315 SNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEE-----------YS 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 343 KNTVYMQNTVSLEEELRKANAArsqletykrqvvELQNRLSEESKKADKLDfeykrlkEKVDSLQKEKDRLRTERDSLKE 422
Cdd:PRK01156 384 KNIERMSAFISEILKIQEIDPD------------AIKKELNEINVKLQDIS-------SKVSSLNQRIRALRENLDELSR 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 423 TIEelrcvqaqegQLTTQGLMPLGSQESSDSLAAEIVTpEIREKLIRLqhENKMLKLNQEGSD-NEKIALLQSLLDDANL 501
Cdd:PRK01156 445 NME----------MLNGQSVCPVCGTTLGEEKSNHIIN-HYNEKKSRL--EEKIREIEIEVKDiDEKIVDLKKRKEYLES 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 502 RK-NELETENRLVNQRLLEVQSQVEELQKsLQDQGSKAEDAISVLLKKKLEEHLEKLHEANNELQKKRAI-IEDLEPRFN 579
Cdd:PRK01156 512 EEiNKSINEYNKIESARADLEDIKIKINE-LKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVISLIdIETNRSRSN 590
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622960294 580 NSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNqgaapEIQALKNQLQERDRLFHSLEKEYEKTKS 658
Cdd:PRK01156 591 EIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYN-----EIQENKILIEKLRGKIDNYKKQIAEIDS 664
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
355-670 |
4.64e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 4.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 355 EEELRKANAARSQLETYKRQVVEL---QNRLSEESKKADKldfeYKRLKEKVDSLQK-----EKDRLRTERDSLKETIEE 426
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELerqLKSLERQAEKAER----YKELKAELRELELallvlRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 427 LrcvqaqegqlttqglmplgsQESSDSLAAEIVTPEIREKLIRLQHenkmlklnqeGSDNEKIALLQSLLDDANLRKNEL 506
Cdd:TIGR02168 251 A--------------------EEELEELTAELQELEEKLEELRLEV----------SELEEEIEELQKELYALANEISRL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 507 ETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEdaisvllkkkleehleklhEANNELQKKRAIIEDLEPRFNNSSLKIE 586
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLD-------------------ELAEELAELEEKLEELKEELESLEAELE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 587 ELQEALRkkeeemkQMEERYKKYLEKAKSVIRTLDPKQNQgaapeIQALKNQLQERDRLFHSLEKEYEKTKSQREMEEKY 666
Cdd:TIGR02168 362 ELEAELE-------ELESRLEELEEQLETLRSKVAQLELQ-----IASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429
|
....
gi 1622960294 667 IVSA 670
Cdd:TIGR02168 430 LEEA 433
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
259-670 |
4.87e-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: 4.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 259 FRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEI--DVLRHSSDKVSKLEGQVESYKKKLEDLGDLRRQ 336
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELeaQIRGNGGDRLEQLEREIERLERELEERERRRAR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 337 vklleekntvYMQNTVSLEEElrkANAARSQLETYKRQVVELQNRLSEESKKA----DKLDFEYKRLKEKVDSLQKEKDR 412
Cdd:COG4913 364 ----------LEALLAALGLP---LPASAEEFAALRAEAAALLEALEEELEALeealAEAEAALRDLRRELRELEAEIAS 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 413 LRTERDSLKETIEELRCVQAQE---------------------------------------------------------- 434
Cdd:COG4913 431 LERRKSNIPARLLALRDALAEAlgldeaelpfvgelievrpeeerwrgaiervlggfaltllvppehyaaalrwvnrlhl 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 435 -GQLTTQGLMPLGSQE-----SSDSLAAEIVT------PEIREKLIR------------LQHENK------MLKLNQE-- 482
Cdd:COG4913 511 rGRLVYERVRTGLPDPerprlDPDSLAGKLDFkphpfrAWLEAELGRrfdyvcvdspeeLRRHPRaitragQVKGNGTrh 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 483 --------------GSDN-EKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKsLQDQGSKAEDAISVLLK 547
Cdd:COG4913 591 ekddrrrirsryvlGFDNrAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQR-LAEYSWDEIDVASAERE 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 548 -KKLEEHLEKLHEANNELQKKRAIIEDLEprfnnssLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQ 626
Cdd:COG4913 670 iAELEAELERLDASSDDLAALEEQLEELE-------AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1622960294 627 GAAPEIQALKNQLQE------RDRLFHSLEKEYEKTKSQREMEEKYIVSA 670
Cdd:COG4913 743 ARLELRALLEERFAAalgdavERELRENLEERIDALRARLNRAEEELERA 792
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
364-643 |
6.84e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 6.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 364 ARSQLETYKRQVVELQNRLSEeskkadkldfeykrLKEKVDSLQKEKDRLRTERDSLkETIEELRcvqaqegqlttqglm 443
Cdd:COG4913 608 NRAKLAALEAELAELEEELAE--------------AEERLEALEAELDALQERREAL-QRLAEYS--------------- 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 444 plgsqessdslAAEIVTPEIREKLIRLQHENKMLKlnqegSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQ 523
Cdd:COG4913 658 -----------WDEIDVASAEREIAELEAELERLD-----ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE 721
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 524 V---EELQKSLQDQGSKAEDAISVLLKKKLEEHLEKLHEANNELQKKRAI---IEDLEPRFNNSSLKIEELQEAlrkkee 597
Cdd:COG4913 722 LeqaEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLeerIDALRARLNRAEEELERAMRA------ 795
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1622960294 598 emkqmeerykkYLEKAKSVIRTLDPkqNQGAAPEIQALKNQLQERD 643
Cdd:COG4913 796 -----------FNREWPAETADLDA--DLESLPEYLALLDRLEEDG 828
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
359-670 |
7.03e-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: 49.68 E-value: 7.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 359 RKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEyKRLKEKVDSLQKEKDRLR-TERDSLKETIEELRcvQAQEGQL 437
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE-REKAERYQALLKEKREYEgYELLKEKEALERQK--EAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 438 TTQGLMPLGSQESSDSLAAEIVTPEIR----EKLIRLQHENKMLKLNQE-GSDNEKIALLQSLLDDANLRKNELETENRL 512
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLleelNKKIKDLGEEEQLRVKEKiGELEAEIASLERSIAEKERELEDAEERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 513 VNQRLLEVQSQVEELQKSLQDQGSKAEDAISVL---------LKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSL 583
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYaelkeeledLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 584 KIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNqgaapEIQALKNQLQERDRLFHSLEKEYEKTKSQREME 663
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL-----EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
|
....*..
gi 1622960294 664 EKYIVSA 670
Cdd:TIGR02169 482 EKELSKL 488
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
299-587 |
8.29e-06 |
|
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: 49.58 E-value: 8.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 299 LKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKLLEEKNTVYMQNTVSLEEEL-RKANAARSQLETYKRQVVE 377
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLaKEEEELKSELLKLERRKVD 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 378 LQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKETIEELRCVQAQEgqlttqglmplgSQESSDSLAAE 457
Cdd:pfam02463 312 DEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKL------------EQLEEELLAKK 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 458 IVTPEIREKLIRLQHENKMLKLNQEGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSK 537
Cdd:pfam02463 380 KLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELK 459
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1622960294 538 AEDAISVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLKIEE 587
Cdd:pfam02463 460 LLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGL 509
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
154-425 |
9.44e-06 |
|
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: 48.97 E-value: 9.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 154 IQELMSKESPVSAGNDAYVDLDRQLKKTTEELNEALSAKE-----------EIAQRCHELDMQVAALQEEKSSLLAENQV 222
Cdd:pfam05557 57 IRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKEsqladarevisCLKNELSELRRQIQRAELELQSTNSELEE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 223 LMERLNQSDS----IEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRI---------RCEELEKEISELRQQNDEL 289
Cdd:pfam05557 137 LQERLDLLKAkaseAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIvknskselaRIPELEKELERLREHNKHL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 290 TTLADEAQSLKDEIDVLRHSSDKV--------------SKLEGQVESYKKKLEDLG-------DLRRQVKLLEEKNTVYM 348
Cdd:pfam05557 217 NENIENKLLLKEEVEDLKRKLEREekyreeaatlelekEKLEQELQSWVKLAQDTGlnlrspeDLSRRIEQLQQREIVLK 296
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622960294 349 QNTVSLEEELRKANAARSQLETYKRQVVelqnrlseesKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKETIE 425
Cdd:pfam05557 297 EENSSLTSSARQLEKARRELEQELAQYL----------KKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILE 363
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
173-641 |
9.75e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 9.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 173 DLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQVLMERLNQSDSIEDpnsPAGRRHLQLQTQLE 252
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA---EAEEELEELAEELL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 253 QLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDEL-TTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLG 331
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELeEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 332 DLRRQVKLLEEKNTVYMQNTVSLEEELRKANAARSQLE--TYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKE 409
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLegVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 410 KDRLRTERDsLKETIEELRcvQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKmLKLNQEGSDNEKI 489
Cdd:COG1196 550 NIVVEDDEV-AAAAIEYLK--AAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREAD-ARYYVLGDTLLGR 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 490 ALLQSLLDDANLRKNELETENRLVNQ--RLLEVQSQVEELQKSLQDQGSKAEDAISVLLKKKLEEHLEKLHEANNELQKK 567
Cdd:COG1196 626 TLVAARLEAALRRAVTLAGRLREVTLegEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEE 705
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622960294 568 RAIIEDLEPRFNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQgAAPEIQALKNQLQE 641
Cdd:COG1196 706 ERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEE-LERELERLEREIEA 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
171-685 |
1.12e-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: 48.90 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 171 YVDLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQVLMERLNQSDsiedpnspagrrHLQLQTQ 250
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE------------DRRERLQ 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 251 LEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEI-DVLRHSSDKVSKLEGQVESYKKKLED 329
Cdd:TIGR02168 421 QEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAeQALDAAERELAQLQARLDSLERLQEN 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 330 LGDLRRQVKLLEEKNTVY------MQNTVSLEEELRKA-----------------NAARSQLETYKRQVVELQNRLSEES 386
Cdd:TIGR02168 501 LEGFSEGVKALLKNQSGLsgilgvLSELISVDEGYEAAieaalggrlqavvvenlNAAKKAIAFLKQNELGRVTFLPLDS 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 387 KKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKETIEEL--RCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTP--- 461
Cdd:TIGR02168 581 IKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLlgGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPggv 660
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 462 ----EIREKLIRLQHENKMLKLNQEGSDNE-KIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGS 536
Cdd:TIGR02168 661 itggSAKTNSSILERRREIEELEEKIEELEeKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA 740
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 537 KAE----------------DAISVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLKIEELQEALRKKEEEMK 600
Cdd:TIGR02168 741 EVEqleeriaqlskeltelEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 601 QMEERYKKYLEKAKSVIRTLDPKQNQgaapeiqaLKNQLQERDRLFHSLEK-EYEKTKSQREMEEKYIVSAWYNMGMTLH 679
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQ--------IEELSEDIESLAAEIEElEELIEELESELEALLNERASLEEALALL 892
|
....*.
gi 1622960294 680 KKAAED 685
Cdd:TIGR02168 893 RSELEE 898
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
179-431 |
1.20e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 179 KKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQVLMERLNQSDSIedpnspagRRHLQLQTQLEQLQEET 258
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEK--------KKAEEAKKAEEDKNMAL 1580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 259 FRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDL----- 333
Cdd:PTZ00121 1581 RKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAeeenk 1660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 334 --RRQVKLLEEKNTVYMQNTVSLEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKD 411
Cdd:PTZ00121 1661 ikAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE 1740
|
250 260
....*....|....*....|
gi 1622960294 412 RLRTERDSLKETIEELRCVQ 431
Cdd:PTZ00121 1741 EDKKKAEEAKKDEEEKKKIA 1760
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
260-661 |
1.25e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 260 RLEAAKDdyriRCEELEKEISELRQQNDELTTLADE---AQSLKDEIDVLRHSSDKVSKLEG---QVESYKKKLEDLGDL 333
Cdd:PTZ00121 1358 EAEAAEE----KAEAAEKKKEEAKKKADAAKKKAEEkkkADEAKKKAEEDKKKADELKKAAAakkKADEAKKKAEEKKKA 1433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 334 RRQVKLLEEKNTVymQNTVSLEEELRKANAARSQLETyKRQVVELQNRlSEESKKADKLDFEYKRLKEKVDSLQKeKDRL 413
Cdd:PTZ00121 1434 DEAKKKAEEAKKA--DEAKKKAEEAKKAEEAKKKAEE-AKKADEAKKK-AEEAKKADEAKKKAEEAKKKADEAKK-AAEA 1508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 414 RTERDSLKETIEELRCVQAQEGQLTTQglmplgsqessdslAAEIVTPEIREKLIRLQHENKMLKLNQEGSDNEKiallQ 493
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAEEAKK--------------ADEAKKAEEKKKADELKKAEELKKAEEKKKAEEA----K 1570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 494 SLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDA-ISVLLKKKLEEHLEKLHEANNELQKKRAIIE 572
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAkIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE 1650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 573 DLEPRFNNSSLKIEELQ----------EALRKKEEEMKQMEERYKKYLEKAKSVIRTldPKQNQGAAPEIQALKNQLQER 642
Cdd:PTZ00121 1651 ELKKAEEENKIKAAEEAkkaeedkkkaEEAKKAEEDEKKAAEALKKEAEEAKKAEEL--KKKEAEEKKKAEELKKAEEEN 1728
|
410
....*....|....*....
gi 1622960294 643 DRLFHSLEKEYEKTKSQRE 661
Cdd:PTZ00121 1729 KIKAEEAKKEAEEDKKKAE 1747
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
360-543 |
2.80e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 360 KANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKETIEELRCV-------QA 432
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElgeraraLY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 433 QEGQLTTQGLMPLGSQESSD----SLAAEIVTPEIREKLIRLQHENKMLKlNQEGSDNEKIALLQSLLDDANLRKNELET 508
Cdd:COG3883 97 RSGGSVSYLDVLLGSESFSDfldrLSALSKIADADADLLEELKADKAELE-AKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622960294 509 ---ENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDAIS 543
Cdd:COG3883 176 qqaEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
173-427 |
2.89e-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: 47.74 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 173 DLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQVLMERLNQ-----------SDSIEDPNSPAG 241
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaanlrerLESLERRIAATE 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 242 RRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDV-LRHSSDKVSKLEGQV 320
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEeLRELESKRSELRREL 917
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 321 ESYKKKLEDLgDLRRQ---VKLLEEKNTVYMQNTVSLEEELRKANAARSQLETYKRQVVELQNRLSE---------Eskk 388
Cdd:TIGR02168 918 EELREKLAQL-ELRLEgleVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaaiE--- 993
|
250 260 270
....*....|....*....|....*....|....*....
gi 1622960294 389 adkldfEYKRLKEKVDSLQKEKDRLRTERDSLKETIEEL 427
Cdd:TIGR02168 994 ------EYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
261-428 |
3.28e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 261 LEAAKDDYRIRCEELEKEISELRQQNDeLTTLADEAQSLKDEIDVLRhssDKVSKLEGQVESYKKKLEDLgdlRRQVKLL 340
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNG-LVDLSEEAKLLLQQLSELE---SQLAEARAELAEAEARLAAL---RAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 341 EEKNTVYMQNTV--SLEEELRKANAARSQLET-----------YKRQVVELQNRLSEESKKA-DKLDFEYKRLKEKVDSL 406
Cdd:COG3206 253 PDALPELLQSPViqQLRAQLAELEAELAELSArytpnhpdviaLRAQIAALRAQLQQEAQRIlASLEAELEALQAREASL 332
|
170 180
....*....|....*....|..
gi 1622960294 407 QKEKDRLRTERDSLKETIEELR 428
Cdd:COG3206 333 QAQLAQLEARLAELPELEAELR 354
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
354-428 |
3.90e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.16 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 354 LEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLK----------EKVDSLQKEKDRLRTERDSLKET 423
Cdd:COG2433 408 LTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARseerreirkdREISRLDREIERLERELEEERER 487
|
....*
gi 1622960294 424 IEELR 428
Cdd:COG2433 488 IEELK 492
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
260-426 |
5.00e-05 |
|
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: 45.30 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 260 RLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDV-LRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVK 338
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKeIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 339 LLEEKNTVYMQNTVsLEEELRKANAarsQLETYKRQVVELQNRLSEeskKADKLDFEYKRLKEKVDSLQKEKDRLRTERD 418
Cdd:COG1579 94 LQKEIESLKRRISD-LEDEILELME---RIEELEEELAELEAELAE---LEAELEEKKAELDEELAELEAELEELEAERE 166
|
....*...
gi 1622960294 419 SLKETIEE 426
Cdd:COG1579 167 ELAAKIPP 174
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
351-593 |
5.77e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.67 E-value: 5.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 351 TVSLEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTE----RDSLKETIEE 426
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKvkelKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 427 LRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIvtpeirEKLIRlQHENKMLKLNQEGSDNEKIALLQSLLDDAnLRKNEL 506
Cdd:COG1340 87 LNELREELDELRKELAELNKAGGSIDKLRKEI------ERLEW-RQQTEVLSPEEEKELVEKIKELEKELEKA-KKALEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 507 ETENRLVNQRLLEVQSQVEELQKSLQDQGSKAE--DAISVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLK 584
Cdd:COG1340 159 NEKLKELRAELKELRKEAEEIHKKIKELAEEAQelHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKE 238
|
....*....
gi 1622960294 585 IEELQEALR 593
Cdd:COG1340 239 LRELRKELK 247
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
260-667 |
7.03e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 7.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 260 RLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKL 339
Cdd:PTZ00121 1225 KAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKA 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 340 LEEKNTVymqntvsleEELRKANAARSQLETYKRQVVELQNRlSEESKKAD--------KLDFEYKRLKEKVDSLQKEKD 411
Cdd:PTZ00121 1305 DEAKKKA---------EEAKKADEAKKKAEEAKKKADAAKKK-AEEAKKAAeaakaeaeAAADEAEAAEEKAEAAEKKKE 1374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 412 RLRTERDSLKETIEELRcvQAQEGQLTTQGLMPlGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKLNQEGSDNEKIAL 491
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEKK--KADEAKKKAEEDKK-KADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKK 1451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 492 LQSLLDDA-NLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDAisvllkKKLEEHLEKLHEANNELQKKRAI 570
Cdd:PTZ00121 1452 KAEEAKKAeEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEA------KKAAEAKKKADEAKKAEEAKKAD 1525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 571 iedlEPRFNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQLQERDRLFHSLE 650
Cdd:PTZ00121 1526 ----EAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLY 1601
|
410
....*....|....*....
gi 1622960294 651 KEYEKTKSQ--REMEEKYI 667
Cdd:PTZ00121 1602 EEEKKMKAEeaKKAEEAKI 1620
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
263-428 |
8.08e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 8.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 263 AAKDDYRIRCEELEKEISELRQQNDELTT-LADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKK--KLEDLGDL----RR 335
Cdd:PHA02562 213 ENIARKQNKYDELVEEAKTIKAEIEELTDeLLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKviKMYEKGGVcptcTQ 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 336 QVKLLEEKNTVYMQNTVSLEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRT 415
Cdd:PHA02562 293 QISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQA 372
|
170
....*....|...
gi 1622960294 416 ERDSLKETIEELR 428
Cdd:PHA02562 373 EFVDNAEELAKLQ 385
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
301-592 |
8.70e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 8.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 301 DEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKLLEEKNTVYMQNTVSLEEELRKANAarsQLETYKRQVVELQN 380
Cdd:PRK03918 138 DAILESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEK---ELEEVLREINEISS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 381 RLSEESKKADKLDFEYKRL---KEKVDSLQKEKDRLRTERDSLKETIEELRCVQAQegqlTTQGLMPLGSQESSDSLAAE 457
Cdd:PRK03918 215 ELPELREELEKLEKEVKELeelKEEIEELEKELESLEGSKRKLEEKIRELEERIEE----LKKEIEELEEKVKELKELKE 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 458 IVTPEIREKLIRLQHENKMLKLNQEGSD-NEKIALLQSLLDDANLRKNEL-ETENRL--VNQRLLEVQSQVEELQ--KSL 531
Cdd:PRK03918 291 KAEEYIKLSEFYEEYLDELREIEKRLSRlEEEINGIEERIKELEEKEERLeELKKKLkeLEKRLEELEERHELYEeaKAK 370
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622960294 532 QDQGSKAEDAISVLLKKKLEEHLEKLHEANNELQKKraiIEDLEPRFNNSSLKIEELQEAL 592
Cdd:PRK03918 371 KEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEE---ISKITARIGELKKEIKELKKAI 428
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
193-439 |
1.79e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 193 EEIAQRCHELDMQVAALQEEKSSL---LAENQVLMERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDDYR 269
Cdd:PRK02224 471 EEDRERVEELEAELEDLEEEVEEVeerLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELE 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 270 IRCEELEKEISELRQQNDE----LTTLADEAQSLKDEIDVL---RHSSDKVSKLEGQVESYKKKLEDLGDLRRQVK-LLE 341
Cdd:PRK02224 551 AEAEEKREAAAEAEEEAEEareeVAELNSKLAELKERIESLeriRTLLAAIADAEDEIERLREKREALAELNDERReRLA 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 342 EKNTVYMQNTVSLEEE-LRKANAARSQLETYKRQVvelqnrlseeskkADKLDfeykRLKEKVDSLQ----------KEK 410
Cdd:PRK02224 631 EKRERKRELEAEFDEArIEEAREDKERAEEYLEQV-------------EEKLD----ELREERDDLQaeigavenelEEL 693
|
250 260
....*....|....*....|....*....
gi 1622960294 411 DRLRTERDSLKETIEELRCVQAQEGQLTT 439
Cdd:PRK02224 694 EELRERREALENRVEALEALYDEAEELES 722
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
290-427 |
2.34e-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: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 290 TTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKlEDLGDLRRQVKLLEEKNtvymqntVSLEEELRKANAARSQLE 369
Cdd:COG2433 376 LSIEEALEELIEKELPEEEPEAEREKEHEERELTEEE-EEIRRLEEQVERLEAEV-------EELEAELEEKDERIERLE 447
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622960294 370 TYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKETIEEL 427
Cdd:COG2433 448 RELSEARSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLE 505
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
273-574 |
2.47e-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: 44.63 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 273 EELEKEISELRQQNDELTTLADEAQSLKDEIDVLRH--SSDKVSKLEGQVESYKKKLEDL-----------GDLRRQVKL 339
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNqkEQDWNKELKSELKNQEKKLEEIqnqisqnnkiiSQLNEQISQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 340 LEEKNTVYMQNTVSLEEELRKANAA-----------RSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQK 408
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEieklkkenqsyKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 409 EKDRLRTERDSLKETIEELRcVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHE-----NKMLKLNQEG 483
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLT-NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKElkskeKELKKLNEEK 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 484 SD-NEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEdaisvllKKKLEEHLEKLHEANN 562
Cdd:TIGR04523 506 KElEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKE-------IDEKNKEIEELKQTQK 578
|
330
....*....|..
gi 1622960294 563 ELQKKRAIIEDL 574
Cdd:TIGR04523 579 SLKKKQEEKQEL 590
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
190-440 |
2.63e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.15 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 190 SAKEEIAQRCHELD-MQVAALQEEKSS-----LLAENQVLMERLNQSDSIEDPNSpagrrhlqlQTQLEQLQEETFRLEA 263
Cdd:PRK05771 16 SYKDEVLEALHELGvVHIEDLKEELSNerlrkLRSLLTKLSEALDKLRSYLPKLN---------PLREEKKKVSVKSLEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 264 AKDDYRIRCEELEKEISELrqqNDELTTLADEAQSLKDEIDVLR------------HSSDKVSKLEGQVESYKKKLEDLG 331
Cdd:PRK05771 87 LIKDVEEELEKIEKEIKEL---EEEISELENEIKELEQEIERLEpwgnfdldlsllLGFKYVSVFVGTVPEDKLEELKLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 332 DLRRQVKLLEE-KNTVYM------QNTVSLEEELRKANAARSQLEtykrqvvelqnrlseESKKADKLdfeYKRLKEKVD 404
Cdd:PRK05771 164 SDVENVEYISTdKGYVYVvvvvlkELSDEVEEELKKLGFERLELE---------------EEGTPSEL---IREIKEELE 225
|
250 260 270
....*....|....*....|....*....|....*.
gi 1622960294 405 SLQKEKDRLRTERDSLKETIEELrcVQAQEGQLTTQ 440
Cdd:PRK05771 226 EIEKERESLLEELKELAKKYLEE--LLALYEYLEIE 259
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
273-667 |
2.98e-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: 44.24 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 273 EELEKEI----SELRQQNDELTTLADeaqSLKDEIDVLRHSSDKVSKLEGQVESYKKKLED----LGDLRRQVKLLEEKN 344
Cdd:TIGR04523 36 KQLEKKLktikNELKNKEKELKNLDK---NLNKDEEKINNSNNKIKILEQQIKDLNDKLKKnkdkINKLNSDLSKINSEI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 345 TVYMQNTVSLEEELRKAnaaRSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKETI 424
Cdd:TIGR04523 113 KNDKEQKNKLEVELNKL---EKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 425 EELRcvqAQEGQLTTQGLMPLGSQESSDSLAAEIVtpEIREKLIRLqhENKMLKLNQEgsDNEKIALLQSLLDDANLRKN 504
Cdd:TIGR04523 190 DKIK---NKLLKLELLLSNLKKKIQKNKSLESQIS--ELKKQNNQL--KDNIEKKQQE--INEKTTEISNTQTQLNQLKD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 505 ELETENRLVNQRLLEVQsQVEELQKSLQDQGSKAEDAISVLLKKKLEEHLEKLHEannELQKKRAIIEDLEPRFNNSSLK 584
Cdd:TIGR04523 261 EQNKIKKQLSEKQKELE-QNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKS---ELKNQEKKLEEIQNQISQNNKI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 585 IEELQEA---LRKKEEEMKQMEERYKKYLEKAKSVIRTLDpKQNQGAAPEIQALKNQLQERDRLF--------------- 646
Cdd:TIGR04523 337 ISQLNEQisqLKKELTNSESENSEKQRELEEKQNEIEKLK-KENQSYKQEIKNLESQINDLESKIqnqeklnqqkdeqik 415
|
410 420
....*....|....*....|....*..
gi 1622960294 647 ------HSLEKEYEKTKSQREMEEKYI 667
Cdd:TIGR04523 416 klqqekELLEKEIERLKETIIKNNSEI 442
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
298-577 |
3.29e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.15 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 298 SLKDEID-VLR--HSSDKVsklegQVESYKKKLEDLgdlrrQVKLLEEKNTVYMQNTVSLEEELRKANAARSQLETYKrq 374
Cdd:PRK05771 13 TLKSYKDeVLEalHELGVV-----HIEDLKEELSNE-----RLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVS-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 375 VVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLK--ETIE-ELRCVQAQEGQLTTQGLMPLGSQESS 451
Cdd:PRK05771 81 VKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwGNFDlDLSLLLGFKYVSVFVGTVPEDKLEEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 452 DSLAAEIVTPEIREKlirlqHENKMLKLNQEGSDNEKIAllqSLLDDANLRKNELETENRL------VNQRLLEVQSQVE 525
Cdd:PRK05771 161 KLESDVENVEYISTD-----KGYVYVVVVVLKELSDEVE---EELKKLGFERLELEEEGTPselireIKEELEEIEKERE 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622960294 526 ELQKSLQDQGSKAEDAISVL------LKKKLE--------------------EHLEKLHEANNELQKKRAIIEDLEPR 577
Cdd:PRK05771 233 SLLEELKELAKKYLEELLALyeyleiELERAEalskflktdktfaiegwvpeDRVKKLKELIDKATGGSAYVEFVEPD 310
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
274-617 |
4.93e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.81 E-value: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 274 ELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLgdlrrQVKLLEEKNTVYMQNTVS 353
Cdd:pfam02463 663 EVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEA-----EELLADRVQEAQDKINEE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 354 LEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKETIEELRCVQAQ 433
Cdd:pfam02463 738 LKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELL 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 434 EGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKLNQEGSDNEKIALLQSLLDDANLRKNELETENRLV 513
Cdd:pfam02463 818 EEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 514 NQRLLEVQSQVEELQKSLQDQGSKAEDAISVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLKIEELQEALR 593
Cdd:pfam02463 898 EKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNL 977
|
330 340
....*....|....*....|....
gi 1622960294 594 KKEEEMKQMEERYKKYLEKAKSVI 617
Cdd:pfam02463 978 MAIEEFEEKEERYNKDELEKERLE 1001
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
271-674 |
5.52e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 271 RCEELEKEISELRQQNDELTTLADE---AQSLKDEIDVLRHSSDKVSKLE--GQVESYKKKLEDLGDLRRQVKLLEEKNT 345
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKAAAAkkkADEAKKKAEEKKKADEAKKKAEeaKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 346 VymQNTVSLEEELRKANAARSQLETYKRQVVELQN-----------RLSEESKKADKLdfEYKRLKEKVDSLQKEKDRLR 414
Cdd:PTZ00121 1472 A--DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKaaeakkkadeaKKAEEAKKADEA--KKAEEAKKADEAKKAEEKKK 1547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 415 TERDSLKETIEELRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKLNQEGSDNEKIALLQS 494
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK 1627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 495 LLDD----ANLRKNELETENRLVNQRLLEVQSQV--EELQKSLQDQGSKAEDAisvllkKKLEEHLEKLHEANNELQKKR 568
Cdd:PTZ00121 1628 AEEEkkkvEQLKKKEAEEKKKAEELKKAEEENKIkaAEEAKKAEEDKKKAEEA------KKAEEDEKKAAEALKKEAEEA 1701
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 569 AIIEDLEPRFNNSSLKIEELQ----------EALRKKEEEMKQMEERYKKYLEKAKSVIRTldPKQNQGAAPEIQALKNQ 638
Cdd:PTZ00121 1702 KKAEELKKKEAEEKKKAEELKkaeeenkikaEEAKKEAEEDKKKAEEAKKDEEEKKKIAHL--KKEEEKKAEEIRKEKEA 1779
|
410 420 430
....*....|....*....|....*....|....*.
gi 1622960294 639 LQERDrlfhsLEKEYEKTKSQREMEEKYIVSAWYNM 674
Cdd:PTZ00121 1780 VIEEE-----LDEEDEKRRMEVDKKIKDIFDNFANI 1810
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
260-438 |
9.03e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 9.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 260 RLEAAKDDYRIRCEELEKEISELRQQ----NDELTTLADEAQSLKDEIDVLRhssdkvSKLEGQVESYKKKL-------- 327
Cdd:COG4942 45 ALKKEEKALLKQLAALERRIAALARRiralEQELAALEAELAELEKEIAELR------AELEAQKEELAELLralyrlgr 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 328 ----------EDLGDLRRQVKLLEEKNTVYMQNTVSLEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKL----D 393
Cdd:COG4942 119 qpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALkaerQ 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622960294 394 FEYKRLKEKVDSLQKEKDRLRTERDSLKETIEELRCVQAQEGQLT 438
Cdd:COG4942 199 KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
265-531 |
9.44e-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: 42.90 E-value: 9.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 265 KDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEidvlrhssdkvskLEGQVESYKkklEDLGDLRRQVKLLEEKN 344
Cdd:pfam12128 268 KSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDE-------------LNGELSAAD---AAVAKDRSELEALEDQH 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 345 TVYmqntvsLEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDS-LQKEKDRLRTERDSLKET 423
Cdd:pfam12128 332 GAF------LDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEqNNRDIAGIKDKLAKIREA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 424 IEELRCV-----QAQEGQLTTQ---GLMPLGSQESSDSLAAE---------IVTPEIREKLIRLQHENKMLKLNQEGSdN 486
Cdd:pfam12128 406 RDRQLAVaeddlQALESELREQleaGKLEFNEEEYRLKSRLGelklrlnqaTATPELLLQLENFDERIERAREEQEAA-N 484
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1622960294 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 ... |
173-579 |
9.54e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 9.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 173 DLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQVLMERLNQ---------------SDSIEDPN 237
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEkqneieklkkenqsyKQEIKNLE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 238 SPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSD----KV 313
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTREsletQL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 314 SKLEGQVESYKKKLED-----------LGDLRRQVKLLEEKNTVYMQNTVSLEEELRKANAARSQLEtykrqvvelqNRL 382
Cdd:TIGR04523 471 KVLSRSINKIKQNLEQkqkelkskekeLKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKE----------SKI 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 383 SEESKKADKLDFEYKR--LKEKVDSLQKEKDRLRTERDSLKETIEELrcvqaqegqlttqglmplgsQESSDSLAAEI-- 458
Cdd:TIGR04523 541 SDLEDELNKDDFELKKenLEKEIDEKNKEIEELKQTQKSLKKKQEEK--------------------QELIDQKEKEKkd 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 459 VTPEIREKLIRLQHENKMLKLNQEgsDNEKialLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKA 538
Cdd:TIGR04523 601 LIKEIEEKEKKISSLEKELEKAKK--ENEK---LSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKI 675
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622960294 539 EDAISVLLK----------------------KKLEEHLEKLHEANNELQKKRAIIEDLEPRFN 579
Cdd:TIGR04523 676 DDIIELMKDwlkelslhykkyitrmirikdlPKLEEKYKEIEKELKKLDEFSKELENIIKNFN 738
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
360-639 |
9.76e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 9.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 360 KANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKETIEELrcvQAQEGQLtt 439
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL---EKEIAEL-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 440 qglmplgsqessdslaaeivtpeiREKLIRLQHE-NKMLKLNQEGSDNEKIALL--QSLLDDANLRKNELETENRLVNQR 516
Cdd:COG4942 96 ------------------------RAELEAQKEElAELLRALYRLGRQPPLALLlsPEDFLDAVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 517 LLEVQSQVEELQKslqdqgskaedaisvlLKKKLEEHLEKLHEANNELQKKRAIIEDLEprfNNSSLKIEELQEALRKKE 596
Cdd:COG4942 152 AEELRADLAELAA----------------LRAELEAERAELEALLAELEEERAALEALK---AERQKLLARLEKELAELA 212
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1622960294 597 EEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQL 639
Cdd:COG4942 213 AELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
262-665 |
1.07e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 262 EAAKDDYRIRCEELEKEISELRQQnDELTTLADEAQSLKDEIDvlRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKLLE 341
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKKA-DEAKKKAEEAKKKADAAK--KKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 342 EKNtvymqntvslEEELRKANAARSQLETyKRQVVELQNRLSEESKKADKLDfEYKRLKEKVDSLQKEKDRLRtERDSLK 421
Cdd:PTZ00121 1371 KKK----------EEAKKKADAAKKKAEE-KKKADEAKKKAEEDKKKADELK-KAAAAKKKADEAKKKAEEKK-KADEAK 1437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 422 ETIEELRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKLNQEGSDNEKIALLQSLLDDA-- 499
Cdd:PTZ00121 1438 KKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAkk 1517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 500 --NLRKNE----LETENRLVNQRLLEVQSQVEELQKSlqDQGSKAEDAISVLLKKKLEEHLEKLHEANNELQK--KRAII 571
Cdd:PTZ00121 1518 aeEAKKADeakkAEEAKKADEAKKAEEKKKADELKKA--EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaeEARIE 1595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 572 EDLEPRFNNSSLKIEELQEALRK--------KEEEMKQMEERYKKYLEKAKSVIRTLDpKQNQGAAPEIQALKNQLQERD 643
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKKAEEAkikaeelkKAEEEKKKVEQLKKKEAEEKKKAEELK-KAEEENKIKAAEEAKKAEEDK 1674
|
410 420
....*....|....*....|..
gi 1622960294 644 RLFHSLEKEYEKTKSQREMEEK 665
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEALKK 1696
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
501-665 |
1.99e-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: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 501 LRKNELETENRLVN-----QRLLEVQSQVEELQKSLQDQGSKAEDAISV----------LLKKKLEEHLEKLHEANNELQ 565
Cdd:TIGR02168 170 YKERRKETERKLERtrenlDRLEDILNELERQLKSLERQAEKAERYKELkaelrelelaLLVLRLEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 566 KKRAIIEDLEPRFNNSSLKIEELQEALRKKEEEMKQMEERY----------KKYLEKAKSVIRTLDPKQNQGAApEIQAL 635
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELyalaneisrlEQQKQILRERLANLERQLEELEA-QLEEL 328
|
170 180 190
....*....|....*....|....*....|
gi 1622960294 636 KNQLQERDRLFHSLEKEYEKTKSQREMEEK 665
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEA 358
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
168-427 |
2.11e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.54 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 168 NDAYVDLDRQLKKTTEELNEALSAKEEIAQrchELDMQVAALQEEKSSLLAENQVLM-ERLNQSDSIEDPNSPAGRRHLQ 246
Cdd:TIGR04523 379 NQSYKQEIKNLESQINDLESKIQNQEKLNQ---QKDEQIKKLQQEKELLEKEIERLKeTIIKNNSEIKDLTNQDSVKELI 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 247 LQTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKK 326
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 327 LED-LGDLRRQVKLLEEKNTVYMQNTVSLE-----EELRKANAA----------------------RSQLETYKRQVVEL 378
Cdd:TIGR04523 536 KESkISDLEDELNKDDFELKKENLEKEIDEknkeiEELKQTQKSlkkkqeekqelidqkekekkdlIKEIEEKEKKISSL 615
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1622960294 379 QNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKETIEEL 427
Cdd:TIGR04523 616 EKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEI 664
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
266-376 |
2.77e-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: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 266 DDYRIRCEELEKEISELRQQNDELTtlADEAQSLKDEIDVLRhssDKVSKLEGQVESYKKKLEDLGDLRRQvklLEEKNt 345
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEQDEAS--FERLAELRDELAELE---EELEALKARWEAEKELIEEIQELKEE---LEQRY- 484
|
90 100 110
....*....|....*....|....*....|.
gi 1622960294 346 vymQNTVSLEEELRKANAARSQLETYKRQVV 376
Cdd:COG0542 485 ---GKIPELEKELAELEEELAELAPLLREEV 512
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
488-665 |
3.26e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 488 KIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDaisvlLKKKLEEHLEKLHEANNELQKK 567
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE-----LELELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 568 RAIIEDLEPRFNNSSLKIEELQEALRKKEEEMKQMEERykkyLEKAKSVIRTLDPKQNQGAApEIQALKNQLQERDRLFH 647
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEE----LEELEEELEEAEEELEEAEA-ELAEAEEALLEAEAELA 375
|
170
....*....|....*...
gi 1622960294 648 SLEKEYEKTKSQREMEEK 665
Cdd:COG1196 376 EAEEELEELAEELLEALR 393
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
273-663 |
3.86e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.80 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 273 EELEKEISELRQQNDELTTLADEAQSLKD----EIDVLRHSSDKVS----KLEGQVESYKKKLEDLGDLRRQVKLLEEKN 344
Cdd:TIGR00606 712 KSTESELKKKEKRRDEMLGLAPGRQSIIDlkekEIPELRNKLQKVNrdiqRLKNDIEEQETLLGTIMPEEESAKVCLTDV 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 345 TVYMQNTVSLEEELRKANAARSQLetykrQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKETI 424
Cdd:TIGR00606 792 TIMERFQMELKDVERKIAQQAAKL-----QGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKT 866
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 425 EELRCVQAQEGQLTTQglmplgsqessdslaAEIVTPEIREKLIRLQHENKMLKlnqegSDNEKIALLQSLLDDANLRKN 504
Cdd:TIGR00606 867 NELKSEKLQIGTNLQR---------------RQQFEEQLVELSTEVQSLIREIK-----DAKEQDSPLETFLEKDQQEKE 926
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 505 EL----ETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDAISVLLKKKlEEHLEKLHEANNELQKKRAIIEDlEPRFNN 580
Cdd:TIGR00606 927 ELisskETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQK-ETELNTVNAQLEECEKHQEKINE-DMRLMR 1004
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 581 SSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQLQERDR---LFHSLEKEYEKTK 657
Cdd:TIGR00606 1005 QDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRnhvLALGRQKGYEKEI 1084
|
....*.
gi 1622960294 658 SQREME 663
Cdd:TIGR00606 1085 KHFKKE 1090
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
269-580 |
4.66e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 40.34 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 269 RIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKLLEEKNTVYM 348
Cdd:pfam02463 711 ELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEE 790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 349 QNTVSLEEELRKANAARSQLEtYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKETIEELR 428
Cdd:pfam02463 791 EKEEKLKAQEEELRALEEELK-EEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELL 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 429 CVQAQEGQLTTQglmplgsQESSDSLAAEIVTPEIREKLIRLQHENKMLKLNQEGSDNEKIALLQSLLDDANLRKNELET 508
Cdd:pfam02463 870 QELLLKEEELEE-------QKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLL 942
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622960294 509 ENRLVNQRLLEVQSQVEELQKSLQDQGSKAE-------DAISVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNN 580
Cdd:pfam02463 943 EEADEKEKEENNKEEEEERNKRLLLAKEELGkvnlmaiEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| Taf7 |
COG5414 |
TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation ... |
380-575 |
4.67e-03 |
|
TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation complex [Transcription];
Pssm-ID: 227701 Cd Length: 392 Bit Score: 40.07 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 380 NRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKETIEE------LRCVQAQEGQLTTQGLMPLGSQESSDS 453
Cdd:COG5414 200 IEIEEVEKKVDDLLEKDMKAESVSVVLKDEKELARQERVSSWENFKEepgeplSRPALKKEKQGAEEEGEEGMSEEDLDV 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 454 LAAEIVTPEIREKLIRLQHENKMlklNQEGSDNEKiallQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQD 533
Cdd:COG5414 280 GAAEIENKEVSEGDKEQQQEEVE---NAEAHKEEV----QSDRPDEIGEEKEEDDENEENERHTELLADELNELEKGIEE 352
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622960294 534 QGSKAEDAISVLLKKKLEEHLEKLHEannELQKKRAIIEDLE 575
Cdd:COG5414 353 KRRQMESATNPILQKRFESQLNVLLK---ELELKRKQLEMEE 391
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
284-559 |
5.78e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.27 E-value: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 284 QQNDELTTLADEAQ----SLKDEIDVLRHSSDKVSKLEgqvesyKKKLEDLGDLRrqvKLLEEKNTVYMQNTVsLEEELR 359
Cdd:PLN02939 111 IDNEQQTNSKDGEQlsdfQLEDLVGMIQNAEKNILLLN------QARLQALEDLE---KILTEKEALQGKINI-LEMRLS 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 360 KANAaRSQLETYKRQVVELQNRLSEesKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKETIEELRcVQAQEGQLTT 439
Cdd:PLN02939 181 ETDA-RIKLAAQEKIHVEILEEQLE--KLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLK-AELIEVAETE 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 440 QGLMPLGSQESsdslAAEIVTPEIREKLIRLQHEnkMLKLNQEGSDN--EKIALLQSLLDDAnlrKNELEtENRLVNQRL 517
Cdd:PLN02939 257 ERVFKLEKERS----LLDASLRELESKFIVAQED--VSKLSPLQYDCwwEKVENLQDLLDRA---TNQVE-KAALVLDQN 326
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1622960294 518 LEVQSQVEELQKSLQDQG-SKAEDAISVLLKKK---LEEHLEKLHE 559
Cdd:PLN02939 327 QDLRDKVDKLEASLKEANvSKFSSYKVELLQQKlklLEERLQASDH 372
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
166-409 |
6.09e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 39.89 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 166 AGNDAYVDLDRQLKKTTEELNEALSA-KEEIAQR-------CHELDMQVAALQEEKSSLLAENQVLMERLnqsDSIEDPN 237
Cdd:PLN02939 180 SETDARIKLAAQEKIHVEILEEQLEKlRNELLIRgateglcVHSLSKELDVLKEENMLLKDDIQFLKAEL---IEVAETE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 238 SPAGRRHLQLQTQLEQLQEETFRLEAAKDDYR----IRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRhssDKV 313
Cdd:PLN02939 257 ERVFKLEKERSLLDASLRELESKFIVAQEDVSklspLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLR---DKV 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960294 314 SKLEGQVES---YKKKLEDLGDLRRQVKLLEEKNTVYMQNTvsleeelrkanaaRSQLETYKRQVVELQ---NRLSEESK 387
Cdd:PLN02939 334 DKLEASLKEanvSKFSSYKVELLQQKLKLLEERLQASDHEI-------------HSYIQLYQESIKEFQdtlSKLKEESK 400
|
250 260
....*....|....*....|..
gi 1622960294 388 KadkldfeyKRLKEKVDSLQKE 409
Cdd:PLN02939 401 K--------RSLEHPADDMPSE 414
|
|
| |
