|
Name |
Accession |
Description |
Interval |
E-value |
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
184-709 |
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: 672.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 184 ELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQEETFRLEA 263
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 264 AKDDYRIRCEELEKEIAELRQQTEELTTLAEEAQSLKDEIDVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQVKLLEEK 343
Cdd:pfam05622 81 ARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLGDLRRQVKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 344 NTMYMQNTVSLEEELRKANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERDSLKET 423
Cdd:pfam05622 161 NAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRET 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 424 IEELRCVQAQEGQLTTTGLMPLGTQEPSDSLAAEIVTPEIKEKLIRLQHENKILKLNQEGSDNEKIALLQSLLDDANLRK 503
Cdd:pfam05622 241 NEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLGQEGSYRERLTELQQLLEDANRRK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 504 NELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDSILLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRCN-NSSLK 582
Cdd:pfam05622 321 NELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDsNLAQK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 583 IEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQLQERDRMFHSLEKEYEKTKSQREMEE 662
Cdd:pfam05622 401 IDELQEALRKKDEDMKAMEERYKKYVEKAKSVIKTLDPKQNPASPPEIQALKNQLLEKDKKIEHLERDFEKSKLQREQEE 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1865265942 663 KFIVSAWYNMGMTLHKKAAEDRLASTGS-GQSFLARQRQATSTRRSYP 709
Cdd:pfam05622 481 KLIVTAWYNMGMALHRKAIEERLAGLSSpGQSFLARQRQATNARRGLS 528
|
|
| HkD_Hook3 |
cd22226 |
Hook domain found in protein Hook 3 (Hook3) and similar proteins; Hook3 is an adaptor protein ... |
8-160 |
4.62e-102 |
|
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: 309.21 E-value: 4.62e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 8 ERAELGESLLTWIQTFNVEAPCQTVEDLTSGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKVSNLKKILKGILDYN 87
Cdd:cd22226 1 DRAELCESLLTWIQTFNVDAPCQTVEDLTSGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1865265942 88 HEILGQQINDFTLPDVNLIGEHADAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMSK 160
Cdd:cd22226 81 HEILGQQINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMSK 153
|
|
| HOOK_N |
pfam19047 |
HOOK domain; This domain is found at the N-terminus of HOOK proteins. |
11-161 |
6.86e-94 |
|
HOOK domain; This domain is found at the N-terminus of HOOK proteins.
Pssm-ID: 465958 Cd Length: 151 Bit Score: 287.77 E-value: 6.86e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 11 ELGESLLTWIQTFNVEAPCQTVEDLTSGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKVSNLKKILKGILDYNHEI 90
Cdd:pfam19047 1 ELCDSLLTWLQTFNVPAPCATVEDLTDGVAMAQVLHQIDPSWFTEAWLSRIKEDVGDNWRLKVSNLKKILQSVVDYYQDV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1865265942 91 LGQQINDFTLPDVNLIGEHADAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMSKE 161
Cdd:pfam19047 81 LGQQISDFLLPDVNLIGEHSDPAELGRLLQLILGCAVNCEKKQEYIQQIMTLEESVQHVVMTAIQELMSKD 151
|
|
| HkD_Hook |
cd22222 |
Hook domain found in Hook family of microtubule-binding proteins; The Hook family includes ... |
14-159 |
2.21e-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: 278.75 E-value: 2.21e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 14 ESLLTWIQTFNVEAPCQTVEDLTSGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKVSNLKKILKGILDYNHEILGQ 93
Cdd:cd22222 2 DSLLQWLQTFNLIAPHATAEDLSDGVAIAQVLNQIDPEYFSDSWLSKIKPDVGDNWRLKVSNLKKILKGIVDYYSEVLGQ 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1865265942 94 QINDFTLPDVNLIGEHADAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMS 159
Cdd:cd22222 82 QISGFTMPDVNAIAEKEDPKELGRLLQLVLGCAVNCERKEEYIQAIMGLEESVQHVVMEAIQELMS 147
|
|
| HkD_Hook1 |
cd22225 |
Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a ... |
12-161 |
1.90e-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: 1.90e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 12 LGESLLTWIQTFNVEAPCQTVEDLTSGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKVSNLKKILKGILDYNHEIL 91
Cdd:cd22225 1 LCDSLIIWLQTFNTAAPCQTVQDLTSGVAMAQVLHQIDSSWFDESWLSRIKEDVGDNWRIKMSNLKKILQGIVDYYHEFL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 92 GQQINDFTLPDVNLIGEHADAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMSKE 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 |
4.93e-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: 228.22 E-value: 4.93e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 11 ELGESLLTWIQTFNVEAPCQTVEDLTSGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKVSNLKKILKGILDYNHEI 90
Cdd:cd22227 1 ELCDSLLTWLQTFQVPSPCSSYQDLTSGVAIAQVLNRIDPSWFNEAWLGRIKEDTGDNWRLKVSNLKKILQSLLEYYQDV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 91 LGQQINDFTLPDVNLIGEHADAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMSK 160
Cdd:cd22227 81 LGHQVSEDHLPDVNLIGEFSDDTELGKLLQLVLGCAISCEKKQEHIQQIMTLEESVQHVVMEAIQELLTK 150
|
|
| HkD_SF |
cd22211 |
Hook domain-containing proteins superfamily; The Hook domain superfamily includes Hook adaptor ... |
13-159 |
3.90e-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: 3.90e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 13 GESLLTWIQTFNVEAPCQTVEDLTSGVVMAQVLQKIDPAYFDENWLNriKTEVGDNWRLKVSNLKKILKGILDYNHEILG 92
Cdd:cd22211 1 EAALLAWINTFPLSSPVESLDDLSDGVVLAEILSQIDPSYFDSEWLE--SRDSSDNWVLKLNNLKKLYRSLSKYYREVLG 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1865265942 93 QQINDFTLPDVNLIGEHADAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMS 159
Cdd:cd22211 79 QQLSDLPLPDLSAIARDGDEEEIVKLLELVLGAAVQCENKEEYIARIQQLDESTQAELMLIIQEVLE 145
|
|
| HkD_HkRP |
cd22223 |
Hook domain found in the Hook-related protein (HkRP) family; The HkRP family includes Daple, ... |
15-157 |
9.55e-24 |
|
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: 97.66 E-value: 9.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 15 SLLTWIQTFNVEAPCQ-TVEDLTSGVVMAQVLQKIDPAYFDEnwlnRIKTEVGDNWRLKVSNLKKILKGILDYNHEILGQ 93
Cdd:cd22223 5 PLVTWAKTFADDGSAElSYTDLVDGVFLNNVMLQIDPRPFSE----VSNRNVDDDVNARIQNLDLLLRNIKSFYQEVLQQ 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1865265942 94 QINdFTLPDVNLIGEHADA----AELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQEL 157
Cdd:cd22223 81 LIV-MKLPDILTIGREPESeqslEELEKLLLLLLGCAVQCERKEEFIERIKNLDLEVQHALVACIQEV 147
|
|
| HkD_Daple |
cd22228 |
Hook domain found in Daple (Dvl-associating protein with a high frequency of leucine residues) ... |
12-157 |
5.93e-17 |
|
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: 78.43 E-value: 5.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 12 LGESLLTWIQTFNV-----EAPCQTVEDLTSGVVMAQVLQKIDPAYFDEnwlnRIKTEVGDNWRLKVSNLKKILKGILDY 86
Cdd:cd22228 2 LQSPLVTWVKTFGPlgfgsEDKLSMYMDLVDGVFLNKIMLQIDPRPTNQ----RVNKHVNNDVNLRIQNLTILVRHIKTY 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1865265942 87 NHEILgQQINDFTLPDVNLIGEH----ADAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQEL 157
Cdd:cd22228 78 YQEVL-QQLIVMNLPNVLMIGKDplsgKSMEEIKKMLLLVLGCAVQCERKEEFIERIKQLDIETQAAIVSHIQEV 151
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
260-633 |
6.55e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.28 E-value: 6.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 260 RLEAAKDDY---RIRCEELEKEIAELRQQTEelttLAEEAQSLKDEIDVLrhssdkvaKLESQVESYKKKLEDLGDLRRQ 336
Cdd:COG1196 180 KLEATEENLerlEDILGELERQLEPLERQAE----KAERYRELKEELKEL--------EAELLLLKLRELEAELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 337 VKLLEEKNTMYMQNTVSLEEELRKANAARSQLEtykRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTE 416
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELE---LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 417 RDSLKETIEELrcvQAQEGQLTTTglmpLGTQEPSDSLAAEivtpEIKEKLIRLQHENKILKLNQEGSDNEKIALLQSLL 496
Cdd:COG1196 325 LAELEEELEEL---EEELEELEEE----LEEAEEELEEAEA----ELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 497 DDANLRKNELETENRLVN--QRLLEVQSQVEELQKSLQDQGSKAEDsilLKKKLEEHLEKLHEANNELQKKRAIIEDLEP 574
Cdd:COG1196 394 AAAELAAQLEELEEAEEAllERLERLEEELEELEEALAELEEEEEE---EEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1865265942 575 RCNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQAL 633
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL 529
|
|
| HkD_Girdin |
cd22229 |
Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation ... |
16-157 |
2.94e-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: 65.20 E-value: 2.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 16 LLTWIQTFNVEAPCQTVE-----DLTSGVVMAQVLQKIDPAYFDEnwlnRIKTEVGDNWRLKVSNLKKILKGILDYNHEI 90
Cdd:cd22229 9 LVTWVKTFGPLATGNGTPldeyvALVDGVFLNEVMLQINPKSSNQ----RVNKKVNNDASLRIQNLSILVKQIKLYYQET 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1865265942 91 LgQQINDFTLPDVNLIG-----EHAdAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQEL 157
Cdd:cd22229 85 L-QQLIMMSLPNVLVLGrnplsEQG-TEEMKKLLLLLLGCAVQCERKEEFIERIQTLDFDTKAAVAAHIQEV 154
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
130-664 |
1.20e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.17 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 130 EQKQEYIQTIMMMEESVQHVVMTAIQELMSKESPVSVGNDAYVDLDRQLKKTTEELNEALATKEEIAqrchELDMQVAAL 209
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIE----ELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 210 QEEKSSLLAENQILMERLNQSDS-IEDPNSPAGR---------RHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEI 279
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKeIEELEEKVKElkelkekaeEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 280 AELRQQTEELTTLAEEAQSLKDEIDVLRHSS---DKVAKLESQVESYKKKLEDL--GDLRRQVKLLEEKNTmymqntvSL 354
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEELEERHelyEEAKAKKEELERLKKRLTGLtpEKLEKELEELEKAKE-------EI 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 355 EEELRKANAARSQLETYKRQAVELQNRL--------------SEESKKADKLDY---------ECKRLKEKVDSLQKEKD 411
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKKAIEELkkakgkcpvcgrelTEEHRKELLEEYtaelkriekELKEIEEKERKLRKELR 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 412 RLRTERD------SLKETIEELRCVQAQegqltttglmpLGTQEPSDSLAAEIVTPEIKEKLIRLQHENKILKlnqegSD 485
Cdd:PRK03918 484 ELEKVLKkeseliKLKELAEQLKELEEK-----------LKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLK-----KE 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 486 NEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQ-SQVEELQKSLQDQGSKAEDSILLK---KKLEEHLEKLHEANNE 561
Cdd:PRK03918 548 LEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKdaeKELEREEKELKKLEEE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 562 LQKKRAIIEDLEPRCNNSSLKIEELQealrkKEEEMKQMEERYKKYLEKAKSVirtldpkqnQGAAPEIQALKNQLQERD 641
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELEELE-----KKYSEEEYEELREEYLELSREL---------AGLRAELEELEKRREEIK 693
|
570 580
....*....|....*....|...
gi 1865265942 642 RMFHSLEKEYEKTKSQREMEEKF 664
Cdd:PRK03918 694 KTLEKLKEELEEREKAKKELEKL 716
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
260-562 |
1.32e-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: 65.08 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 260 RLEAAKDDYRIRCEELEKEIAELRQQTEELTTLAEEAQSLKDEIDVLRHSSDK-VAKLESQVESYKKKLEDL----GDLR 334
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdLARLEAEVEQLEERIAQLskelTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 335 RQVKLLEEKNTMYMQNTVSLEEEL----RKANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEK 410
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIeeleAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 411 DRLRTERDSLKETIEELRCVQAQEGQLTTTglmplgTQEPSDSLAAEIVTPEIKEKLIRLQHENKILKLNQEGSDN---- 486
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEE------LESELEALLNERASLEEALALLRSELEELSEELRELESKRselr 914
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1865265942 487 EKIALLQSLLDDANLRKNELEtenrlvnQRLLEVQSQV-EELQKSLQDQGSKAEDSILLKKKLEEHLEKLHEANNEL 562
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLE-------VRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
169-663 |
5.28e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.77 E-value: 5.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 169 DAYVDLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQ--------SDSIEDPNSPA 240
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPElreeleklEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 241 GRRHLQLQTQLEQLQEETfRLEAAKDDYRIRCEELEKEIAELRQQTEELTTLAEEAQS-------LKDEIDVLRHSSDKV 313
Cdd:PRK03918 238 EEIEELEKELESLEGSKR-KLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiklsefYEEYLDELREIEKRL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 314 AKLESQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQAVELQNRLSEE-SKKADKL 392
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKlEKELEEL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 393 DYECKRLKEKVDSLQKEKDRLRTERDSLKETIEELRcvqAQEGQLTTTG----------LMPLGTQEPSDSLAAEIVTPE 462
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGELKKEIKELKKAIEELK---KAKGKCPVCGrelteehrkeLLEEYTAELKRIEKELKEIEE 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 463 IKEKL-IRLQHENKILKLNQEGSDNEKIA----LLQSLLDDANLRKNELETEN-RLVNQRLLEVQSQVEELQKSLqdqgS 536
Cdd:PRK03918 474 KERKLrKELRELEKVLKKESELIKLKELAeqlkELEEKLKKYNLEELEKKAEEyEKLKEKLIKLKGEIKSLKKEL----E 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 537 KAEDsilLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRCnnsslkIEELQEALRKKEEEmkqmeerYKKYLEkAKSVIR 616
Cdd:PRK03918 550 KLEE---LKKKLAELEKKLDELEEELAELLKELEELGFES------VEELEERLKELEPF-------YNEYLE-LKDAEK 612
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1865265942 617 TLDPKQNqgaapEIQALKNQLQERDRMFHSLEKEYEKTKSQREMEEK 663
Cdd:PRK03918 613 ELEREEK-----ELKKLEEELDKAFEELAETEKRLEELRKELEELEK 654
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
176-663 |
5.37e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.77 E-value: 5.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 176 RQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQ 255
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 256 EETFRLEAAKDDYRIRCEELEKEIAELRQQTEELTTLAEEAQS-------LKDEIDVLRHSSDKVAKLESQVESYKKKLE 328
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiklsefYEEYLDELREIEKRLSRLEEEINGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 329 DLGDLRRQVKLLEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQAVELQNRLSEE-SKKADKLDYECKRLKEKVDSLQ 407
Cdd:PRK03918 332 ELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKlEKELEELEKAKEEIEEEISKIT 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 408 KEKDRLRTERDSLKETIEELRcvqAQEGQLTTTG----------LMPLGTQEPSDSLAAEIVTPEIKEKL-IRLQHENKI 476
Cdd:PRK03918 412 ARIGELKKEIKELKKAIEELK---KAKGKCPVCGrelteehrkeLLEEYTAELKRIEKELKEIEEKERKLrKELRELEKV 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 477 LKLNQEGSDNEKIA----LLQSLLDDANLRKNELETEN-RLVNQRLLEVQSQVEELQKSLQDQGSKAEDSILLKKKLEEH 551
Cdd:PRK03918 489 LKKESELIKLKELAeqlkELEEKLKKYNLEELEKKAEEyEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDEL 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 552 LEKLHEANNELQKK--------RAIIEDLEP------RCNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRT 617
Cdd:PRK03918 569 EEELAELLKELEELgfesveelEERLKELEPfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKE 648
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1865265942 618 LDPKQNQGAAPEIQALKNQLQERDRMFHSLEKEYEKTKSQREMEEK 663
Cdd:PRK03918 649 LEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKK 694
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
173-532 |
2.75e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.85 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 173 DLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLaENQILMERLnqsdsIEDPNSPAGRRHLQLQTQLE 252
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEK-----REYEGYELLKEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 253 QLQEETFRLEAAKDDYRIRCEELEKEIAELRQQTEELTT-----LAEEAQSLKDEIDVLrhsSDKVAKLESQVESYKKKL 327
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKkikdlGEEEQLRVKEKIGEL---EAEIASLERSIAEKEREL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 328 EDLGDLRRQVKLLEEKNTMYMQNtvsLEEELRKANAARSQLET--YKRQAV--ELQNRLSEESKKADKLDYECKRLKEKV 403
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEE---LEREIEEERKRRDKLTEeyAELKEEleDLRAELEEVDKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 404 DSLQKEKDRLRTERDSLKETIEELRCVQAQegqltttglmplgtqepsdsLAAEIvtPEIKEKLIRLQHENKILKLNQEg 483
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELAD--------------------LNAAI--AGIEAKINELEEEKEDKALEIK- 451
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1865265942 484 SDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQ 532
Cdd:TIGR02169 452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAR 500
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
213-663 |
3.01e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 213 KSSLLA-ENQILMERLNQSdsIEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEIAELRQQTEELTT 291
Cdd:COG4717 36 KSTLLAfIRAMLLERLEKE--ADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 292 LAEEAQSLKDEIDVLRHSSD------KVAKLESQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEELRkaNAAR 365
Cdd:COG4717 114 LREELEKLEKLLQLLPLYQElealeaELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLS--LATE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 366 SQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKdrlrtERDSLKETIEELR----------CVQAQEG 435
Cdd:COG4717 192 EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL-----EAAALEERLKEARlllliaaallALLGLGG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 436 QLTTTGLMPLGTQEPSDSLAAEIVTPEIKEKLIRLQHENKILKLN-QEGSDNEKIALLQSLLDDANLRKNELETENRLVN 514
Cdd:COG4717 267 SLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPaLEELEEEELEELLAALGLPPDLSPEELLELLDRI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 515 QRLLEVQSQVEELQKSLQDQGSKAEDSILLKK---KLEEHLEKLHEANNELQKKRAIIEDLEPRCNNSSLKIEELQEALr 591
Cdd:COG4717 347 EELQELLREAEELEEELQLEELEQEIAALLAEagvEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL- 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1865265942 592 kkeeemkqMEERYKKYLEKAKSVIRTLDPKQNQgAAPEIQALKNQLQ--ERDRMFHSLEKEYEKTKSQREMEEK 663
Cdd:COG4717 426 --------DEEELEEELEELEEELEELEEELEE-LREELAELEAELEqlEEDGELAELLQELEELKAELRELAE 490
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
174-428 |
3.18e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 174 LDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDPNSpagRRHLQLQTQLEQ 253
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE---ERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 254 LQEETFRLEAAKDDYRIRCEELEKEIAELRQQTEELttLAEEAQSLKDEIDVLRHSSDKVAKLESQVESYKKKLEDLGDL 333
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEA--EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 334 RRQVKLLEEKNTMYMQNTVSLEEELRKANAARSQLEtykRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRL 413
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELE---EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
250
....*....|....*
gi 1865265942 414 RTERDSLKETIEELR 428
Cdd:COG1196 476 EAALAELLEELAEAA 490
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
355-659 |
3.60e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.46 E-value: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 355 EEELRKANAARSQLETYKRQAVEL---QNRLSEESKKADKLdyecKRLKEKVDSLQK-----EKDRLRTERDSLKETIEE 426
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELerqLKSLERQAEKAERY----KELKAELRELELallvlRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 427 LrcvqaqegqltttglmplgtQEPSDSLAAEIVTPEIKEKLIRLQHenkilklnqeGSDNEKIALLQSLLDDANLRKNEL 506
Cdd:TIGR02168 251 A--------------------EEELEELTAELQELEEKLEELRLEV----------SELEEEIEELQKELYALANEISRL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 507 ETENRLVNQRLLEVQSQVEELQKSLQDQGSK----AEDSILLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRCNNSSLK 582
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKldelAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1865265942 583 IEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQLQERDRMFHSLEKEYEKTKSQRE 659
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE 457
|
|
| HkD_Gipie |
cd22230 |
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar ... |
12-157 |
8.65e-09 |
|
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar proteins; Gipie, also called coiled-coil domain-containing protein 88B (CCDC88B), or brain leucine zipper domain-containing protein, or Hook-related protein 3 (HkRP3), is a novel actin cytoskeleton-binding protein and Akt substrate that regulates cell migratory responses in various biological contexts. It acts as a positive regulator of T-cell maturation and inflammatory function. As a microtubule-binding protein, Gipie regulates lytic granule clustering and NK cell killing.
Pssm-ID: 411801 Cd Length: 170 Bit Score: 55.22 E-value: 8.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 12 LGESLLTWIQTF-------------NVEAPCQTVED-------LTSGVVMAQVLQKIDPAYFDENWLNRikteVGDNWRL 71
Cdd:cd22230 4 MSGALVTWALGFeglvgeeedslgfPEEEEEEGTLDaekrflrLSNGDLLNRVMGIIDPSPRGGPRMRG----DDGPAAH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 72 KVSNLKKILKGILDYNHEILgQQINDFTLPDVNLIGEH----ADAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQ 147
Cdd:cd22230 80 RVQNLHILWGRLRDFYQEEL-QQLILSPPPDLQVMGRDpfteEAVQELEKLLRLLLGAAVQCERRELFIRHIQGLDLDVQ 158
|
170
....*....|
gi 1865265942 148 HVVMTAIQEL 157
Cdd:cd22230 159 AELAEAIQEV 168
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
176-655 |
1.12e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 176 RQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERL----NQSDSIEDPNSPAGRRHLQLQTQL 251
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKqilrERLANLERQLEELEAQLEELESKL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 252 EQLQEETFRLEAAKDDYRIRCEELEKEIAELRQQTEELTTLAEEAQ----SLKDEIDVLRHssdKVAKLESQVESYKKKL 327
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEeqleTLRSKVAQLEL---QIASLNNEIERLEARL 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 328 EDLGdlRRQVKLLEEkntmymQNTVSLEEELRKANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQ 407
Cdd:TIGR02168 410 ERLE--DRRERLQQE------IEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 408 KEKDRLRTERDSLKETIEELR-----CVQAQEGQLTTTGLMPLGTQ----EPSDSLAAEIVTPEIKEKLI---------- 468
Cdd:TIGR02168 482 RELAQLQARLDSLERLQENLEgfsegVKALLKNQSGLSGILGVLSElisvDEGYEAAIEAALGGRLQAVVvenlnaakka 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 469 -----------------------RLQHENKILKLNQEG----------SDNEKIALLQSLL---------DDANLRKNEL 506
Cdd:TIGR02168 562 iaflkqnelgrvtflpldsikgtEIQGNDREILKNIEGflgvakdlvkFDPKLRKALSYLLggvlvvddlDNALELAKKL 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 507 ETENRLV--------------------NQRLLEVQSQVEELQKSLQDQGSKAEDsilLKKKLEEHLEKLHEANNELQKKR 566
Cdd:TIGR02168 642 RPGYRIVtldgdlvrpggvitggsaktNSSILERRREIEELEEKIEELEEKIAE---LEKALAELRKELEELEEELEQLR 718
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 567 AIIEDLEPRCNNSSLKIEEL---QEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAA------PEIQALKNQL 637
Cdd:TIGR02168 719 KELEELSRQISALRKDLARLeaeVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAeieeleAQIEQLKEEL 798
|
570
....*....|....*...
gi 1865265942 638 QERDRMFHSLEKEYEKTK 655
Cdd:TIGR02168 799 KALREALDELRAELTLLN 816
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
153-590 |
2.77e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.36 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 153 AIQELMSKESPVSVGNDAYVDLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDS 232
Cdd:PRK02224 207 RLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 233 IEDpnspagrrhlqlqtqleqlqeetfRLEAAKDDYRIRCEELEKEIAELRQQTEELTTLAEEAQslkdeiDVLRHSSDK 312
Cdd:PRK02224 287 RLE------------------------ELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELR------DRLEECRVA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 313 VAKLESQVESYKKKLEDlgdlrrqvklLEEKNTMYMQNTVSLEEELRkanAARSQLETYKRQAVELQNRLSEESKKADKL 392
Cdd:PRK02224 337 AQAHNEEAESLREDADD----------LEERAEELREEAAELESELE---EAREAVEDRREEIEELEEEIEELRERFGDA 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 393 DYECKRLKEKVDSLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTTGLMPLGTQEPSDSLAAEIVTpEIKEKLIRLQH 472
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIE-EDRERVEELEA 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 473 ENKILKLNQEGSDN--EKIALLQSLLDDANLRKNELETENRLVNQR---LLEVQSQVEELQKSLQDQGSKAEDSILLKKK 547
Cdd:PRK02224 483 ELEDLEEEVEEVEErlERAEDLVEAEDRIERLEERREDLEELIAERretIEEKRERAEELRERAAELEAEAEEKREAAAE 562
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1865265942 548 LEEHLEKLHEANNELQKKRAIIEDLEPRCNnsslKIEELQEAL 590
Cdd:PRK02224 563 AEEEAEEAREEVAELNSKLAELKERIESLE----RIRTLLAAI 601
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
282-652 |
3.19e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 57.44 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 282 LRQQTEELTTLAEEAQSLKDEIDVLRHSSDKvaKLESQVESYKKKLEDL-GDLRRQVKLLEEKNTMYMQNTVSLEEELRK 360
Cdd:pfam15921 226 LRELDTEISYLKGRIFPVEDQLEALKSESQN--KIELLLQQHQDRIEQLiSEHEVEITGLTEKASSARSQANSIQSQLEI 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 361 -ANAARSQLETYKRQAVELQNRLSEESKKADkldyECKRLKE-KVDSLQK-------EKDRLRTERDSLKEtieelrcvq 431
Cdd:pfam15921 304 iQEQARNQNSMYMRQLSDLESTVSQLRSELR----EAKRMYEdKIEELEKqlvlansELTEARTERDQFSQ--------- 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 432 aQEGQLtttglmplgtqepSDSLAAEIVTPEIKEKLIRLQHENKILKLNQEGSDNEKIALLQSLLDDANLRKNELETenr 511
Cdd:pfam15921 371 -ESGNL-------------DDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEA--- 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 512 LVNQRLLEVQSQVEELQKSLQDQGSKAEDSILLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRCNNSSLKIEELQEALR 591
Cdd:pfam15921 434 LLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIE 513
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1865265942 592 KKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNqgAAPEIQALKNQLQERDRMFHSLEKEYE 652
Cdd:pfam15921 514 ATNAEITKLRSRVDLKLQELQHLKNEGDHLRN--VQTECEALKLQMAEKDKVIEILRQQIE 572
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
174-471 |
7.93e-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: 7.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 174 LDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDsiedpnspagRRHLQLQTQLEQ 253
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK----------ERLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 254 LQEETFRLEAAKDDYRIRCEELEKEIAELRQQTEELTtlAEEAQSLKDEI-DVLRHSSDKVAKLESQVESYKKKLEDlgd 332
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE--ARLSHSRIPEIqAELSKLEEEVSRIEARLREIEQKLNR--- 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 333 lRRQVKLLEEKNTMYMQNTVSLEEELRKANAAR-----SQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQ 407
Cdd:TIGR02169 824 -LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEienlnGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1865265942 408 KEKDRLRTERDSLKETIEELRC-VQAQEGQLTTTG-LMPLGTQEPSDSLAAEIVTPEIKEKLIRLQ 471
Cdd:TIGR02169 903 RKIEELEAQIEKKRKRLSELKAkLEALEEELSEIEdPKGEDEEIPEEELSLEDVQAELQRVEEEIR 968
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
260-706 |
1.09e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 260 RLEAAKDDYRIRCEELEKEIAELRQQTEELTTLAEEAQSLkdeidvLRHSSDKVAKLESQVESYKKKLEDLGDLRRQVKL 339
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAE------EYELLAELARLEQDIARLEERRRELEERLEELEE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 340 -LEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERD 418
Cdd:COG1196 324 eLAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 419 SLKETIEELRcvQAQEGQLtttglmplgtqepSDSLAAEIVTPEIKEKLIRLQHENKILKLNQEGSDNEKIALLQSLLDD 498
Cdd:COG1196 404 ELEEAEEALL--ERLERLE-------------EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 499 anLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDSILLKKKLEEHLEKLHEANNELQKKRAIIEDLEprcnn 578
Cdd:COG1196 469 --LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE----- 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 579 sslkiEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQN-QGAAPEIQALKNQLQERDRMFHSLEKEYEKTKSQ 657
Cdd:COG1196 542 -----AALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKiRARAALAAALARGAIGAAVDLVASDLREADARYY 616
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1865265942 658 REME---EKFIVSAWYNMGMTLHKKAAEDRLASTGSGQSFLARQRQATSTRR 706
Cdd:COG1196 617 VLGDtllGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR 668
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
365-659 |
1.96e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 365 RSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTtglmp 444
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA----- 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 445 lgtQEPSDSLAAEIVTPEIKEKLIRLQHENKILKLNQEgSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQV 524
Cdd:TIGR02168 751 ---QLSKELTELEAEIEELEERLEEAEEELAEAEAEIE-ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 525 EELQKSLQDQGSKAEDSILLKKKLEEHLEKLHEAnnelqkkraiIEDLEPRCNNSSLKIEELQEALRKKEEEMKQMEERY 604
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAE----------IEELEELIEELESELEALLNERASLEEALALLRSEL 896
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1865265942 605 kkylEKAKSVIRTLDPKqnqgaapeIQALKNQLQERDRMFHSLEKEYEKTKSQRE 659
Cdd:TIGR02168 897 ----EELSEELRELESK--------RSELRRELEELREKLAQLELRLEGLEVRID 939
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
271-665 |
4.30e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 271 RCEELEKEIAELRQQTEELTTLAEE---AQSLKDEIDVLRHSSD--KVAKLESQVESYKKKLEDLGDLRRQVKLLEEKNT 345
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKAAAAkkkADEAKKKAEEKKKADEakKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 346 MymQNTVSLEEELRKANAARSQLETYKRQAVELQNRlSEESKKADKLDY--------ECKRLKEKVDSLQKEKDRLRTER 417
Cdd:PTZ00121 1472 A--DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA-AEAKKKADEAKKaeeakkadEAKKAEEAKKADEAKKAEEKKKA 1548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 418 DSLKETiEELRcvQAQEGQLTTTGLMPLGTQEPSDSLAAEIVTPEIK--EKLIRLQHENKILKLNQEGSDNEKIALLQSL 495
Cdd:PTZ00121 1549 DELKKA-EELK--KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAriEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL 1625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 496 LDDANLRKNELEtenrlVNQRLLEVQSQVEELQKSLQDQGSKAEDsilLKKKLEEHLEKLHEANNELQKKRAIIEDLEpR 575
Cdd:PTZ00121 1626 KKAEEEKKKVEQ-----LKKKEAEEKKKAEELKKAEEENKIKAAE---EAKKAEEDKKKAEEAKKAEEDEKKAAEALK-K 1696
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 576 CNNSSLKIEELqealRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAApEIQALKNQLQERDRMFHSLEKEYEKTK 655
Cdd:PTZ00121 1697 EAEEAKKAEEL----KKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK-KAEEAKKDEEEKKKIAHLKKEEEKKAE 1771
|
410
....*....|
gi 1865265942 656 SQREMEEKFI 665
Cdd:PTZ00121 1772 EIRKEKEAVI 1781
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
273-426 |
6.43e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 6.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 273 EELEKEIAELRqqtEELTTLAEEAQSLKDEIDVLRhssdKVAKLESQVESYKKKLEDLGDLRRQVklleekntmymqntV 352
Cdd:COG4913 613 AALEAELAELE---EELAEAEERLEALEAELDALQ----ERREALQRLAEYSWDEIDVASAEREI--------------A 671
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1865265942 353 SLEEELRKANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERDSLKETIEE 426
Cdd:COG4913 672 ELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
260-428 |
6.60e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 6.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 260 RLEAAKDDYRIRCEELEKEIAELRQQTEELTTLAE-------------EAQSLKDEIDVLRHSSDKVAKLESQVESYKKK 326
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeidvasaerEIAELEAELERLDASSDDLAALEEQLEELEAE 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 327 LEDL----GDLRRQVKLLEEKNTmymqntvSLEEELRKANAARSQLETYKRQAV--ELQNRLSEESKKAdkldyeckRLK 400
Cdd:COG4913 701 LEELeeelDELKGEIGRLEKELE-------QAEEELDELQDRLEAAEDLARLELraLLEERFAAALGDA--------VER 765
|
170 180
....*....|....*....|....*...
gi 1865265942 401 EKVDSLQKEKDRLRTERDSLKETIEELR 428
Cdd:COG4913 766 ELRENLEERIDALRARLNRAEEELERAM 793
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
262-659 |
6.98e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 6.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 262 EAAKDDYRIRCEELEKEiAELRQQTEELTTLAEEAQSLKDEIDvlrhssdKVAKLESQVESYKKKLEDLGDLRRQVKLLE 341
Cdd:PTZ00121 1370 EKKKEEAKKKADAAKKK-AEEKKKADEAKKKAEEDKKKADELK-------KAAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 342 EKNTMymQNTVSLEEELRKANAARSQLETyKRQAVELQNRlSEESKKADKLDYECKRLKEKVDSLQKeKDRLRTERDSLK 421
Cdd:PTZ00121 1442 EAKKA--DEAKKKAEEAKKAEEAKKKAEE-AKKADEAKKK-AEEAKKADEAKKKAEEAKKKADEAKK-AAEAKKKADEAK 1516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 422 ETIEELRCVQAQEGQltttglmplgtqepSDSLAAEIVTPEIKEKLIRLQHENKILKLNQEGSDNEKiallQSLLDDANL 501
Cdd:PTZ00121 1517 KAEEAKKADEAKKAE--------------EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEA----KKAEEDKNM 1578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 502 RKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDSIL----------LKKKLEEHLEKLHEANNELQKKRAIIED 571
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIkaeelkkaeeEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 572 LEPRCNNSSLKIEELQ---EALRKKEEEMKQMEERYKKYLEKAKSVIRTldPKQNQGAAPEIQALKNQLQERDRMFHSLE 648
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKkkaEEAKKAEEDEKKAAEALKKEAEEAKKAEEL--KKKEAEEKKKAEELKKAEEENKIKAEEAK 1736
|
410
....*....|.
gi 1865265942 649 KEYEKTKSQRE 659
Cdd:PTZ00121 1737 KEAEEDKKKAE 1747
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
260-591 |
8.69e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.76 E-value: 8.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 260 RLEAAKDDY---RIRCEELEKEIAELRQQTEELTTLAEEA------QSLKDEIDVLRHSSDK-------------VAKLE 317
Cdd:TIGR02169 171 KKEKALEELeevEENIERLDLIIDEKRQQLERLRREREKAeryqalLKEKREYEGYELLKEKealerqkeaierqLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 318 SQVESYKKKLEDLGD-LRRQVKLLEEKNTMYMQNT----VSLEEELRKANA----ARSQLETYKRQAVELQNRLSEESKK 388
Cdd:TIGR02169 251 EELEKLTEEISELEKrLEEIEQLLEELNKKIKDLGeeeqLRVKEKIGELEAeiasLERSIAEKERELEDAEERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 389 ADKLDYECKRLKEKVDSLQKEKDRLRTERDSLKETIEELRC-VQAQEGQLTTTGLMPLGTQEPSDSLAAEIvtPEIKEKL 467
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAeLEEVDKEFAETRDELKDYREKLEKLKREI--NELKREL 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 468 IRLQHENKilKLNQEGSD-NEKIALLQSllddanlRKNELETEnrlVNQRLLEVQSQVEELqKSLQDQGSKAEDSIL-LK 545
Cdd:TIGR02169 409 DRLQEELQ--RLSEELADlNAAIAGIEA-------KINELEEE---KEDKALEIKKQEWKL-EQLAADLSKYEQELYdLK 475
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1865265942 546 KKLEEHLEKLHEANNELQKKRAIIEDLEPRCNNSSLKIEELQEALR 591
Cdd:TIGR02169 476 EEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
179-577 |
1.09e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 179 KKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDsiEDPNSPAGRRHLQLQTQLEQLQEET 258
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE--EKKKAEEAKKAEEDKNMALRKAEEA 1586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 259 FRLEAAKDDYRIRCEELEKEI-AELRQQTEELTTLAEEAQSLKDEIDVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQV 337
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEEKKMkAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 338 KLLEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTER 417
Cdd:PTZ00121 1667 AKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA 1746
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 418 DSLKETIEELRCVQ---------AQEGQLTTTGLMPLGTQEPSDSLAAEI--VTPEIKEKLIRLQHENKILKLNQEGSDN 486
Cdd:PTZ00121 1747 EEAKKDEEEKKKIAhlkkeeekkAEEIRKEKEAVIEEELDEEDEKRRMEVdkKIKDIFDNFANIIEGGKEGNLVINDSKE 1826
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 487 EKIALLQSLLDDANLRKNELEtenrlvnqrllEVQSQVEELQKSLQDQGSKAEDSILLKKKLEEHLEKLHEANNELQKKR 566
Cdd:PTZ00121 1827 MEDSAIKEVADSKNMQLEEAD-----------AFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDK 1895
|
410
....*....|.
gi 1865265942 567 AIIEDLEPRCN 577
Cdd:PTZ00121 1896 DDIEREIPNNN 1906
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
304-591 |
1.24e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 304 DVLRHSSDKVAKLESQVESYKkkleDLGDLRRQVK--LLEEKNTM--------YMQNTVSLEEELRKANAARSQLEtykr 373
Cdd:COG4913 184 RRLGIGSEKALRLLHKTQSFK----PIGDLDDFVReyMLEEPDTFeaadalveHFDDLERAHEALEDAREQIELLE---- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 374 QAVELQNRLSEESKKADKLDYECKRLK-----EKVDSLQKEKDRLRTERDSLKETIEELrcvQAQEGQLtttglmplgtq 448
Cdd:COG4913 256 PIRELAERYAAARERLAELEYLRAALRlwfaqRRLELLEAELEELRAELARLEAELERL---EARLDAL----------- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 449 epsdslaaeivtpeiKEKLIRLQHEnkilklnQEGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQ 528
Cdd:COG4913 322 ---------------REELDELEAQ-------IRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASA 379
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1865265942 529 KSLQDQGSKAEDSI--------LLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRCNNSSLKIEELQEALR 591
Cdd:COG4913 380 EEFAALRAEAAALLealeeeleALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
462-663 |
1.53e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 462 EIKEKLIRLQHENKILKLN----QEGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSK 537
Cdd:COG1196 217 ELKEELKELEAELLLLKLReleaELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 538 AE----DSILLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRCNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKS 613
Cdd:COG1196 297 LArleqDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1865265942 614 VIRTLDPKQNQGAAP--EIQALKNQLQERDRMFHSLEKEYEKTKSQREMEEK 663
Cdd:COG1196 377 AEEELEELAEELLEAlrAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
260-662 |
1.58e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 260 RLEAAKDDYRIRCEELEKEIAELRQQTEELTTLAEeaqslkdEIDVLRhssDKVAKLESQVESYKkklEDLGDLRRQVKL 339
Cdd:PRK02224 224 RYEEQREQARETRDEADEVLEEHEERREELETLEA-------EIEDLR---ETIAETEREREELA---EEVRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 340 LEEKNTmYMQNTVSLEEELRKANAARsqLETYKRQAVELQNRLSEES--------------KKADKLDYECKRLKEKVDS 405
Cdd:PRK02224 291 LEEERD-DLLAEAGLDDADAEAVEAR--REELEDRDEELRDRLEECRvaaqahneeaeslrEDADDLEERAEELREEAAE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 406 LQKEKDRLRTERDSLKETIEELRC-VQAQEGQLTTTGLMPLGTQEPSDSLAAEI--VTPEIKEKLIRLQHENKILKLNQE 482
Cdd:PRK02224 368 LESELEEAREAVEDRREEIEELEEeIEELRERFGDAPVDLGNAEDFLEELREERdeLREREAELEATLRTARERVEEAEA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 483 ----------GSDNEKIALLQSlLDDANLRKNELETEnrlvnqrLLEVQSQVEELQKSLQdqgsKAEDSILLKKKLEEHL 552
Cdd:PRK02224 448 lleagkcpecGQPVEGSPHVET-IEEDRERVEELEAE-------LEDLEEEVEEVEERLE----RAEDLVEAEDRIERLE 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 553 EKLHEANNELQKKRAIIEDLEPRCNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDpkQNQGAAPEIQA 632
Cdd:PRK02224 516 ERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLA--ELKERIESLER 593
|
410 420 430
....*....|....*....|....*....|
gi 1865265942 633 LKNQLQERDRMFHSLEKEYEKTKSQREMEE 662
Cdd:PRK02224 594 IRTLLAAIADAEDEIERLREKREALAELND 623
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
336-558 |
2.03e-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: 50.53 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 336 QVKLLEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRT 415
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 416 ERDSLKETIEELRCVQAQEGQLTTTGLMpLGTQEPSDSLAA----EIVTPEIKEKLIRLQHENKILKLNQEGSDNEKiAL 491
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALL-LSPEDFLDAVRRlqylKYLAPARREQAEELRADLAELAALRAELEAER-AE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1865265942 492 LQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDSILLKKKLEEHLEKLHEA 558
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
304-578 |
2.44e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 304 DVLRHSSDKVAKLESQVES------YKKKLEDL------GDLRRQVKLLEEKNTMYMQNTVSLEEELRKANAARSQLETY 371
Cdd:TIGR02168 193 DILNELERQLKSLERQAEKaerykeLKAELRELelallvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 372 KRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERDSLKETIEELRC--------VQAQEGQLTTTGLM 443
Cdd:TIGR02168 273 RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESkldelaeeLAELEEKLEELKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 444 PLGTQEPSDSLAAEIVTPEIKEKLIRLQHENK----ILKLNQEGSDNEKIALLQSLLDDANLRKNELETEN-----RLVN 514
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLETLrskvAQLELQIASLNNEIERLEARLERLEDRRERLQQEIeellkKLEE 432
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1865265942 515 QRLLEVQSQVEELQKSLQDQGSKAEDSILLKKKLEEHLEK----LHEANNELQKKRAIIEDLEPRCNN 578
Cdd:TIGR02168 433 AELKELQAELEELEEELEELQEELERLEEALEELREELEEaeqaLDAAERELAQLQARLDSLERLQEN 500
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
350-590 |
2.70e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.84 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 350 NTVSLEEELRKANAarsQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERDSLKETIEELRC 429
Cdd:TIGR02169 668 FSRSEPAELQRLRE---RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 430 ------------------VQAQEGQLTTT-GLMPLGTQEPSDSLAAEIVtPEIKEKL-----------IRLQHENKIL-- 477
Cdd:TIGR02169 745 dlssleqeienvkselkeLEARIEELEEDlHKLEEALNDLEARLSHSRI-PEIQAELskleeevsrieARLREIEQKLnr 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 478 KLNQEGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDsilLKKKLEEHLEKLHE 557
Cdd:TIGR02169 824 LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD---LKKERDELEAQLRE 900
|
250 260 270
....*....|....*....|....*....|...
gi 1865265942 558 ANNELQKKRAIIEDLEPRCNNSSLKIEELQEAL 590
Cdd:TIGR02169 901 LERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
260-426 |
3.00e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.15 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 260 RLEAAKDDYRIRCEELEKEIAELRQQTEELTTLAEEAQSLKDEIDV-LRHSSDKVAKLESQVESYKKKLEDLGDLRRQVK 338
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKeIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 339 LLEEKNTMYMQNTVsLEEELRKANAarsQLETYKRQAVELQNRLSEeskKADKLDYECKRLKEKVDSLQKEKDRLRTERD 418
Cdd:COG1579 94 LQKEIESLKRRISD-LEDEILELME---RIEELEEELAELEAELAE---LEAELEEKKAELDEELAELEAELEELEAERE 166
|
....*...
gi 1865265942 419 SLKETIEE 426
Cdd:COG1579 167 ELAAKIPP 174
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
325-663 |
3.20e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.84 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 325 KKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEElrkanaaRSQLETYKRQAVELQN-RLSEESKKADKLDYECKRLKEKV 403
Cdd:TIGR02169 174 KALEELEEVEENIERLDLIIDEKRQQLERLRRE-------REKAERYQALLKEKREyEGYELLKEKEALERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 404 DSLQKEKDRLRTERDSLKETIEELRCVQAQEgqltTTGLMPLGTQEpsdSLAAEIVTPEIKEKLIRLQHENKILKLNQEG 483
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEEL----NKKIKDLGEEE---QLRVKEKIGELEAEIASLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 484 SDnEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDqgskaedsilLKKKLEEHLEKLHEANNELQ 563
Cdd:TIGR02169 320 AE-ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELED----------LRAELEEVDKEFAETRDELK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 564 KKRAIIEDLEPRCNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNqgaapEIQALKNQLQERDRM 643
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL-----EIKKQEWKLEQLAAD 463
|
330 340
....*....|....*....|.
gi 1865265942 644 FHSLEKEYEKTKS-QREMEEK 663
Cdd:TIGR02169 464 LSKYEQELYDLKEeYDRVEKE 484
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
191-440 |
3.35e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 191 TKEEIAQRCHELDMQVAALQEEKSSL---LAENQILMERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDD 267
Cdd:PRK02224 469 TIEEDRERVEELEAELEDLEEEVEEVeerLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAE 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 268 YRIRCEELEKEIAELRQQTEE----LTTLAEEAQSLKDEIDVL---RHSSDKVAKLESQVESYKKKLEDLGDLRRQVK-L 339
Cdd:PRK02224 549 LEAEAEEKREAAAEAEEEAEEareeVAELNSKLAELKERIESLeriRTLLAAIADAEDEIERLREKREALAELNDERReR 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 340 LEEKNTMYMQNTVSLEEE-LRKANAARSQLETYKRQAVElqnRLSEESKKADKLDYECKRLKEKVDSLqkekDRLRTERD 418
Cdd:PRK02224 629 LAEKRERKRELEAEFDEArIEEAREDKERAEEYLEQVEE---KLDELREERDDLQAEIGAVENELEEL----EELRERRE 701
|
250 260
....*....|....*....|..
gi 1865265942 419 SLKETIEELRCVQAQEGQLTTT 440
Cdd:PRK02224 702 ALENRVEALEALYDEAEELESM 723
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
173-639 |
3.97e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 173 DLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDpnsPAGRRHLQLQTQLE 252
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA---EAEEELEELAEELL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 253 QLQEETFRLEAAKDDYRIRCEELEKEIAELRQQTEEL-TTLAEEAQSLKDEIDVLRHSSDKVAKLESQVESYKKKLEDLG 331
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELeEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 332 DLRRQVKLLEEKNTMYMQNTVSLEEELRKANAARSQ-LETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEK 410
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGfLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 411 DRLRTERDSLKETIEELRcvQAQEGQLTttgLMPLGTQEPSDSLAAEIVTPEIKEKLIRLQHENKIL--KLNQEGSDNEK 488
Cdd:COG1196 550 NIVVEDDEVAAAAIEYLK--AAKAGRAT---FLPLDKIRARAALAAALARGAIGAAVDLVASDLREAdaRYYVLGDTLLG 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 489 IALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGS----KAEDSILLKKKLEEHLEKLHEANNELQK 564
Cdd:COG1196 625 RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAalleAEAELEELAERLAEEELELEEALLAEEE 704
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1865265942 565 KRAIIEDLEPRCNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQgAAPEIQALKNQLQE 639
Cdd:COG1196 705 EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEE-LERELERLEREIEA 778
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
263-428 |
4.83e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.01 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 263 AAKDDYRIRCEELEKEIAELRQQTEELTT-LAEEAQSLKDEIDVLRHSSDKVAKLESQVESYKK--KLEDLGDL----RR 335
Cdd:PHA02562 213 ENIARKQNKYDELVEEAKTIKAEIEELTDeLLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKviKMYEKGGVcptcTQ 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 336 QVKLLEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRT 415
Cdd:PHA02562 293 QISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQA 372
|
170
....*....|...
gi 1865265942 416 ERDSLKETIEELR 428
Cdd:PHA02562 373 EFVDNAEELAKLQ 385
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
327-663 |
6.08e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 6.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 327 LEDL-GDLRRQVKlleekntmymqntvSLEEELRKANAARsqleTYKRQAVELQNRLSeeSKKADKLDYECKRLKEKVDS 405
Cdd:COG1196 191 LEDIlGELERQLE--------------PLERQAEKAERYR----ELKEELKELEAELL--LLKLRELEAELEELEAELEE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 406 LQKEKDRLRTERDSLKETIEELRCVQAQEGQLtttglmplgtqepSDSLAAEIVtpEIKEKLIRLQHENKILKlnqegsd 485
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELE-------------LEEAQAEEY--ELLAELARLEQDIARLE------- 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 486 nEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDsilLKKKLEEHLEKLHEANNELQKK 565
Cdd:COG1196 309 -ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE---AEEALLEAEAELAEAEEELEEL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 566 RAIIEDLEPRCNNSSLKIEELQEALRkkeeEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQLQERDRMFH 645
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEE----ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
330
....*....|....*...
gi 1865265942 646 SLEKEYEKTKSQREMEEK 663
Cdd:COG1196 461 LLELLAELLEEAALLEAA 478
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
173-470 |
8.32e-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: 49.28 E-value: 8.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 173 DLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAE----NQILMERLNQSDSIEDPNSPAGRRHLQLQ 248
Cdd:TIGR02168 723 ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERleeaEEELAEAEAEIEELEAQIEQLKEELKALR 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 249 TQLEQLQEETFRLEAAKDDYRIRCEELEKEIAELRQqteELTTLAEEAQSLKDEIDVLRHSsdkVAKLESQVESYKKKLE 328
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAATER---RLEDLEEQIEELSEDIESLAAE---IEELEELIEELESELE 876
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 329 DLGDLRRqvklleekntmymqntvSLEEELRKANAARSQLETykrqavelqnRLSEESKKADKLDYECKRLKEKVDSLQK 408
Cdd:TIGR02168 877 ALLNERA-----------------SLEEALALLRSELEELSE----------ELRELESKRSELRRELEELREKLAQLEL 929
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1865265942 409 EKDRLRTERDSLKETIEElrcvqaqEGQLTTTGLMPLGTQEPSDSLAAEIVTPEIKEKLIRL 470
Cdd:TIGR02168 930 RLEGLEVRIDNLQERLSE-------EYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
260-663 |
8.61e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 8.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 260 RLEAAKDDYRIRCEELEKEIAELRQQTEELTTLAEEAQSLKDEIDVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQVKL 339
Cdd:PTZ00121 1225 KAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKA 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 340 LEEKNTmymqntvslEEELRKANAARSQLETYKRQAVELQNRlSEESKKAD--------KLDYECKRLKEKVDSLQKEKD 411
Cdd:PTZ00121 1305 DEAKKK---------AEEAKKADEAKKKAEEAKKKADAAKKK-AEEAKKAAeaakaeaeAAADEAEAAEEKAEAAEKKKE 1374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 412 RLRTERDSLKETIEELRcvQAQEGQLTTTGLMPlGTQEPSDSLAAEIVTPEIKEKLIRLQHENKILKLNQEGSDNEKIAL 491
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEKK--KADEAKKKAEEDKK-KADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKK 1451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 492 LQSLLDDA-NLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDSillkKKLEEHLEKLHEANNELQKKRAIie 570
Cdd:PTZ00121 1452 KAEEAKKAeEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEA----KKAAEAKKKADEAKKAEEAKKAD-- 1525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 571 dlEPRCNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQLQERDRMFHSLEKE 650
Cdd:PTZ00121 1526 --EAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE 1603
|
410
....*....|...
gi 1865265942 651 YEKTKSQREMEEK 663
Cdd:PTZ00121 1604 EKKMKAEEAKKAE 1616
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
273-591 |
9.71e-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: 49.20 E-value: 9.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 273 EELEKEIAELRQQTEELTTLAEEAQSLKDEIDVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTV 352
Cdd:pfam02463 206 AKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 353 SLEEEL-RKANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERDSLKETIEELRCVQ 431
Cdd:pfam02463 286 EELKLLaKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQ 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 432 AQEGQLTTTGLMPLGTQEpsdslaaeivtpEIKEKLIRLQHENKILKLNQEGSDNEKIALLQSLLDDANLRKNELETENR 511
Cdd:pfam02463 366 EKLEQLEEELLAKKKLES------------ERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILE 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 512 LVNQRLLEVQSQVEELQKSLQDQGSKAEDSILLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRCNNSSLKIEELQEALR 591
Cdd:pfam02463 434 EEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLL 513
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
264-427 |
1.38e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 48.32 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 264 AKDDYRIRCEELEKEIAElRQQTEEL-------TTLAEEAQSLKDEIDVLRHSSDKVAKLESQVESYKKKlEDLGDLRRQ 336
Cdd:COG2433 344 AYDAYKNKFERVEKKVPP-DVDRDEVkarvirgLSIEEALEELIEKELPEEEPEAEREKEHEERELTEEE-EEIRRLEEQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 337 VKLLEEKNtmymqntVSLEEELRKANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTE 416
Cdd:COG2433 422 VERLEAEV-------EELEAELEEKDERIERLERELSEARSEERREIRKDREISRLDREIERLERELEEERERIEELKRK 494
|
170
....*....|.
gi 1865265942 417 RDSLKETIEEL 427
Cdd:COG2433 495 LERLKELWKLE 505
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
360-567 |
1.95e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 360 KANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTT 439
Cdd:COG3883 24 ELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 440 TGLMPLGTQEPSDSLAaeivtpeikekliRLQHENKILKlnqegSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLE 519
Cdd:COG3883 104 YLDVLLGSESFSDFLD-------------RLSALSKIAD-----ADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1865265942 520 VQSQVEELQKSLQDQGSKAEDSILLKKKLEEHLEKLHEANNELQKKRA 567
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
260-665 |
2.05e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 260 RLEAAKDDYRIRCEELEKEIAELRQQTEELTTLAEEAQSLKDEIDVLrhsSDKVAKLESQVESYKKKLEDLGDLRRQVKL 339
Cdd:PRK03918 166 NLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEI---SSELPELREELEKLEKEVKELEELKEEIEE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 340 LEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQAVELQNRLSEESKKAD---KLDYECKRLKEKVDSLQKEKDRLRTE 416
Cdd:PRK03918 243 LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEeyiKLSEFYEEYLDELREIEKRLSRLEEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 417 RDSLKETIEELRCVQAQEGQLTTTglmplgTQEPSDSLAAEIVTPEIKEKLIRLQHENKILKLNQEGSDNEKIAllqSLL 496
Cdd:PRK03918 323 INGIEERIKELEEKEERLEELKKK------LKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLE---KEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 497 DDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDSILLKKKLEEHLEKlheanNELQKKRAIIEDLEPRC 576
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRK-----ELLEEYTAELKRIEKEL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 577 NNSSLKIEELQEALRkkeeemkqmeeRYKKYLEKAKSVIRTLDpkqnqgAAPEIQALKNQLQErdrmfHSLEKEYEKTKS 656
Cdd:PRK03918 469 KEIEEKERKLRKELR-----------ELEKVLKKESELIKLKE------LAEQLKELEEKLKK-----YNLEELEKKAEE 526
|
....*....
gi 1865265942 657 QREMEEKFI 665
Cdd:PRK03918 527 YEKLKEKLI 535
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
259-668 |
2.69e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 259 FRLEAAKDDYRIRCEELEKEIAELRQQTEELTTLAEEAQSLKDEI--DVLRHSSDKVAKLESQVEsykkkledlgDLRRQ 336
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELeaQIRGNGGDRLEQLEREIE----------RLERE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 337 VKLLEEKNTMYMQNTVSLEEElrkANAARSQLETYKRQAVELQNRLSEESKKA----DKLDYECKRLKEKVDSLQKEKDR 412
Cdd:COG4913 354 LEERERRRARLEALLAALGLP---LPASAEEFAALRAEAAALLEALEEELEALeealAEAEAALRDLRRELRELEAEIAS 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 413 LRTERDSLKETIEELRCVQAQEGQLTTTGLMPLG---------------------------------------------- 446
Cdd:COG4913 431 LERRKSNIPARLLALRDALAEALGLDEAELPFVGelievrpeeerwrgaiervlggfaltllvppehyaaalrwvnrlhl 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 447 ------------------TQEPSDSLAAEI------------------------------------VTPE--IKEKLIRL 470
Cdd:COG4913 511 rgrlvyervrtglpdperPRLDPDSLAGKLdfkphpfrawleaelgrrfdyvcvdspeelrrhpraITRAgqVKGNGTRH 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 471 QH--ENKILKLNQEGSDN-EKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKsLQDQGSKAEDSILLKKK 547
Cdd:COG4913 591 EKddRRRIRSRYVLGFDNrAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQR-LAEYSWDEIDVASAERE 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 548 ---LEEHLEKLHEANNELQKKRAIIEDLEprcnnssLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQ 624
Cdd:COG4913 670 iaeLEAELERLDASSDDLAALEEQLEELE-------AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1865265942 625 GAAPEIQALKNQLQE------RDRMFHSLEKEYEKTKSQREMEEKFIVSA 668
Cdd:COG4913 743 ARLELRALLEERFAAalgdavERELRENLEERIDALRARLNRAEEELERA 792
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
260-575 |
3.60e-05 |
|
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: 47.27 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 260 RLEAAKDDYRIRCEELEKEIAELRQQTEELTTLAEEAQSLKDEIDVLR---HSSDKVAKLESQVESYKKKLEDLGDLR-- 334
Cdd:pfam02463 146 IIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEelkLQELKLKEQAKKALEYYQLKEKLELEEey 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 335 ----RQVKLLEEKNTMYMQNTVSLEEELRKANaARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEK 410
Cdd:pfam02463 226 llylDYLKLNEERIDLLQELLRDEQEEIESSK-QEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 411 DRLRTERDSLKETIEELRCVQAQEGQltttglmplgTQEPSDSLAAEIVTPEIKEKLIRLQHENKILKLNQEGSDNEKIA 490
Cdd:pfam02463 305 LERRKVDDEEKLKESEKEKKKAEKEL----------KKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEE 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 491 LLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDSILLKKKLEEHLEKLHEANNELQKKRAIIE 570
Cdd:pfam02463 375 LLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELE 454
|
....*
gi 1865265942 571 DLEPR 575
Cdd:pfam02463 455 KQELK 459
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
280-632 |
4.08e-05 |
|
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: 46.98 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 280 AELRQQTEELTTLAEEAQSLKDEIDVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTV-----SL 354
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIerqlaSL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 355 EEELRKANAARSQLEtykRQAVELQNRLSEESKKADKL-DYECKRLKEKVDSLQKEKDRLrteRDSLKETIEELRCVQAQ 433
Cdd:TIGR02169 250 EEELEKLTEEISELE---KRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASL---ERSIAEKERELEDAEER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 434 EGQLtttglmplgtQEPSDSLAAEIvtPEIKEKLIRLQHENKILKlnqegsdnEKIALLQSLLDDANLRKNELETENRLV 513
Cdd:TIGR02169 324 LAKL----------EAEIDKLLAEI--EELEREIEEERKRRDKLT--------EEYAELKEELEDLRAELEEVDKEFAET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 514 NQRLLEVQSQVEELQKSLQDqgSKAEDSILLKKKLEEHlEKLHEANNELQKKRAIIEDLEPRCNNSSLKIEELQEALRKK 593
Cdd:TIGR02169 384 RDELKDYREKLEKLKREINE--LKRELDRLQEELQRLS-EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460
|
330 340 350
....*....|....*....|....*....|....*....
gi 1865265942 594 EEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQA 632
Cdd:TIGR02169 461 AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQA 499
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
156-573 |
5.51e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 5.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 156 ELMSKESPVSVGNDAYVDLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALqEEKSSLLAENQILMERLNQSDSIED 235
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEL-EERHELYEEAKAKKEELERLKKRLT 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 236 PNSPagrrhlqlqtqlEQLQEETFRLEAAKDDYRIRCEELEKEIAELRQQTEELTTLAEEAQSLK-------------DE 302
Cdd:PRK03918 383 GLTP------------EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgrelteeHR 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 303 IDVLRHSSDKVAKLESQVESYKKKLEDL-GDLRRQVKLLEEKNTMYMQNTV-----SLEEELRKANAarSQLETYKRQAV 376
Cdd:PRK03918 451 KELLEEYTAELKRIEKELKEIEEKERKLrKELRELEKVLKKESELIKLKELaeqlkELEEKLKKYNL--EELEKKAEEYE 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 377 ELQNRLSEESKKADKLDYECKRLKE---KVDSLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTTGLMPLgTQEPSDS 453
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPF-YNEYLEL 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 454 LAAEIVTPEIKEKLIRLQHENKILKLNQEGSDNEkIALLQSLLDDANLRKNELETENrlVNQRLLEVQSQVEELQKSLQD 533
Cdd:PRK03918 608 KDAEKELEREEKELKKLEEELDKAFEELAETEKR-LEELRKELEELEKKYSEEEYEE--LREEYLELSRELAGLRAELEE 684
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1865265942 534 QGSKAEDSILLKKKLEEHLEKLHEANNELQKKRAIIEDLE 573
Cdd:PRK03918 685 LEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVE 724
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
273-613 |
6.72e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.26 E-value: 6.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 273 EELEKEIAELRQQTEELTTLAEEAQSLKDE-------IDVLRHSSD----KVAKLESQVESYKKKLEdlGDLRRQVKLLE 341
Cdd:pfam15921 377 DQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDdrnmEVQRLEALLKAMKSECQ--GQMERQMAAIQ 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 342 EKN------TMYMQNTVSLEEELRKA----NAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKD 411
Cdd:pfam15921 455 GKNeslekvSSLTAQLESTKEMLRKVveelTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQ 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 412 RLRTERDSLKETieelrcvqaqegqltttglmplgtQEPSDSLAAEIVTPEIKEKLIRLQHENKILKLNQEGSDNEKI-- 489
Cdd:pfam15921 535 HLKNEGDHLRNV------------------------QTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMqv 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 490 --ALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQ---KSLQDQGSKAEDSIL-LKKKLEEHLEKLHEANNELq 563
Cdd:pfam15921 591 ekAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLElekVKLVNAGSERLRAVKdIKQERDQLLNEVKTSRNEL- 669
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1865265942 564 kkraiiedleprcNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKS 613
Cdd:pfam15921 670 -------------NSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQS 706
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
283-614 |
7.16e-05 |
|
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: 46.21 E-value: 7.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 283 RQQTEELTTLAEEAQSLKDEIDVLRhssDKVAKLESQVESYKKKLED----LGDLRRQVKLLEEKNTMYMQNTVSLEEEL 358
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQ---SELRRIENRLDELSQELSDasrkIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 359 ----RKANAARSQLETYKRQAVELQNRLSEESKKADKLdyECKRLKEKVDSLQKEKDRLRTERDSLKETIEELrcvqaqE 434
Cdd:TIGR02169 747 ssleQEIENVKSELKELEARIEELEEDLHKLEEALNDL--EARLSHSRIPEIQAELSKLEEEVSRIEARLREI------E 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 435 GQLTTTGLMPLGTQEPSDSLAAEIVTPEIKEKLIRLQHENkilklnqegsDNEKIALLQSLLDDANLRKNELETENRLVN 514
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN----------LNGKKEELEEELEELEAALRDLESRLGDLK 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 515 QRLLEVQSQVEELQKSLQDQGSKAEDSILLKKKLEEHLEKLHEANNEL------------------------QKKRAIIE 570
Cdd:TIGR02169 889 KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIedpkgedeeipeeelsledvqaelQRVEEEIR 968
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1865265942 571 DLEPRCN-------NSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSV 614
Cdd:TIGR02169 969 ALEPVNMlaiqeyeEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
260-410 |
7.55e-05 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 45.39 E-value: 7.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 260 RLEAAKDDYRIRC-------EELEKEIAELRQQ----TEELTTLAEEAQSLKDEIDVLRHSSDKVAKLESQVESYKKklE 328
Cdd:smart00787 127 RLEAKKMWYEWRMklleglkEGLDENLEGLKEDykllMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDP--T 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 329 DLGDLRRQVKLLEEKNTMYMQNTVSLEEELRKANAArsqLETYKRQAVELQNRLSEESKKADKLD----YECKRLKEKVD 404
Cdd:smart00787 205 ELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESK---IEDLTNKKSELNTEIAEAEKKLEQCRgftfKEIEKLKEQLK 281
|
....*.
gi 1865265942 405 SLQKEK 410
Cdd:smart00787 282 LLQSLT 287
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
260-531 |
1.22e-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: 45.60 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 260 RLEAAKDDYRIRCEELEKEIAELRQQTE-ELTTLAEEAQSLKDEIDVLrhSSDKVAKLESQVESYKKKLEDLGDLRRQVK 338
Cdd:pfam12128 280 ERQETSAELNQLLRTLDDQWKEKRDELNgELSAADAAVAKDRSELEAL--EDQHGAFLDADIETAAADQEQLPSWQSELE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 339 LLEEKNTMYMQNTVSLEEELRKanaarsqletyKRQAVELQNrlseeskkADKLDyeckRLKEKVDSLQKEKDRLRT-ER 417
Cdd:pfam12128 358 NLEERLKALTGKHQDVTAKYNR-----------RRSKIKEQN--------NRDIA----GIKDKLAKIREARDRQLAvAE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 418 DSLKETIEELRcvQAQEGQLTTTGLMPLGTQEPSDSLAAEIVTPEIKEKLIrLQHENKILKLN----QEGSDNEKIALLQ 493
Cdd:pfam12128 415 DDLQALESELR--EQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELL-LQLENFDERIErareEQEAANAEVERLQ 491
|
250 260 270
....*....|....*....|....*....|....*...
gi 1865265942 494 SLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSL 531
Cdd:pfam12128 492 SELRQARKRRDQASEALRQASRRLEERQSALDELELQL 529
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
182-441 |
1.22e-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: 45.14 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 182 TEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQsdsiedpnspagrrhlqlqtqleqlqeetfrL 261
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA-------------------------------L 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 262 EAAKDDYRIRCEELEKEIAELRQQTEELTT-LAEEAQSLKDEIDVL-RHSSDKVAKLESQVESYKKKLEDLGDLRRQVKL 339
Cdd:COG4942 68 ARRIRALEQELAALEAELAELEKEIAELRAeLEAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 340 LEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQAVELQNRLSEESKKADKLDyecKRLKEKVDSLQKEKDRLRTERDS 419
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLL---ARLEKELAELAAELAELQQEAEE 224
|
250 260
....*....|....*....|..
gi 1865265942 420 LKETIEELRCVQAQEGQLTTTG 441
Cdd:COG4942 225 LEALIARLEAEAAAAAERTPAA 246
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
154-425 |
2.68e-04 |
|
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: 44.35 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 154 IQELMSKESPVSVGNDAYVDLDRQLKKTTEELNEALATKE-----------EIAQRCHELDMQVAALQEEKSSLLAENQI 222
Cdd:pfam05557 57 IRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKEsqladarevisCLKNELSELRRQIQRAELELQSTNSELEE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 223 LMERLNQSDS----IEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRI---------RCEELEKEIAELRQQTEEL 289
Cdd:pfam05557 137 LQERLDLLKAkaseAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIvknskselaRIPELEKELERLREHNKHL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 290 TT-------LAEEAQSLKDEIDVLRHSSDKVA-------KLESQVESYKKKLEDLG-------DLRRQVKLLEEKNTMYM 348
Cdd:pfam05557 217 NEnienkllLKEEVEDLKRKLEREEKYREEAAtlelekeKLEQELQSWVKLAQDTGlnlrspeDLSRRIEQLQQREIVLK 296
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1865265942 349 QNTVSLEEELRKANAARSQLETYKRQAVelqnrlseesKKADKLDYECKRLKEKVDSLQKEKDRLRTERDSLKETIE 425
Cdd:pfam05557 297 EENSSLTSSARQLEKARRELEQELAQYL----------KKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILE 363
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
174-427 |
5.20e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 5.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 174 LDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQS----DSIEDPNSPAGRRHLQLQT 249
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLrerlESLERRIAATERRLEDLEE 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 250 QLEQLQEETFRLEAAKDDYRIRCEELEKEIAELrqqTEELTTLAEEAQSLKDEIDVLrhsSDKVAKLESQVESYKKKLED 329
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEAL---LNERASLEEALALLRSELEEL---SEELRELESKRSELRRELEE 919
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 330 LGDLRRQVKLLEEKNTMYMQNT---------VSLEEELRKANAARSQLETYKRQAVELQNRLSE---------Eskkadk 391
Cdd:TIGR02168 920 LREKLAQLELRLEGLEVRIDNLqerlseeysLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaaiE------ 993
|
250 260 270
....*....|....*....|....*....|....*.
gi 1865265942 392 ldyECKRLKEKVDSLQKEKDRLRTERDSLKETIEEL 427
Cdd:TIGR02168 994 ---EYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
274-615 |
5.63e-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: 43.42 E-value: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 274 ELEKEIAELRQQTEELTTLAEEAQSLKDEIDVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQVKLLEEKNtmymqNTVS 353
Cdd:pfam02463 663 EVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDK-----INEE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 354 LEEELRKANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERDSLKETIEELRCVQAQ 433
Cdd:pfam02463 738 LKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELL 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 434 EGQLTTTGLMPLGTQEPSDSLAAEIVTPEIKEKLIRLQHENKILKLNQEGSDNEKIALLQSLLDDANLRKNEL--ETENR 511
Cdd:pfam02463 818 EEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESkeEKEKE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 512 LVNQRLLEVQSQVEELQKSLQDQGSKAEDSILLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRCNNSSLKIEELQEALR 591
Cdd:pfam02463 898 EKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNL 977
|
330 340
....*....|....*....|....
gi 1865265942 592 KKEEEMKQMEERYKKYLEKAKSVI 615
Cdd:pfam02463 978 MAIEEFEEKEERYNKDELEKERLE 1001
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
273-572 |
6.58e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.09 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 273 EELEKEIAELRQQTEELTTLAEEAQSLKDEIDVLRH--SSDKVAKLESQVESYKKKLEDL-----------GDLRRQVKL 339
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNqkEQDWNKELKSELKNQEKKLEEIqnqisqnnkiiSQLNEQISQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 340 LEEKNTMYMQNTVSLEEELRKANAA-----------RSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQK 408
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEieklkkenqsyKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 409 EKDRLRTERDSLKETIEELRcVQAQEGQLTTTGLMPLGTQEPSDSLAAEIVTPEIKEKLIRLQHE-----NKILKLNQEG 483
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLT-NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKElkskeKELKKLNEEK 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 484 SD-NEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEdsillKKKLEEHLEKLHEANNEL 562
Cdd:TIGR04523 506 KElEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKE-----IDEKNKEIEELKQTQKSL 580
|
330
....*....|
gi 1865265942 563 QKKRAIIEDL 572
Cdd:TIGR04523 581 KKKQEEKQEL 590
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
263-553 |
7.74e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 7.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 263 AAKDDYRIRCEELEKEIA----ELRQQTEELTTLAEEAQSLKDEidvlRHSSDKVAKLESQVEsykKKLEDLGDLRrqvk 338
Cdd:PRK11281 73 DKIDRQKEETEQLKQQLAqapaKLRQAQAELEALKDDNDEETRE----TLSTLSLRQLESRLA---QTLDQLQNAQ---- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 339 lleekntmymqntvsleEELRKANaarSQLETYKRQAVELQNRLSEESKKADKLDYECKRLK-EKVDSLQKEKDRLRTER 417
Cdd:PRK11281 142 -----------------NDLAEYN---SQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKvGGKALRPSQRVLLQAEQ 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 418 DSLKETIEELRCVQAQEGQLTTTGlmplgtQEPSDSLAAEIVtpeikekliRLQHEnkilklnqegsdnekIALLQSLLD 497
Cdd:PRK11281 202 ALLNAQNDLQRKSLEGNTQLQDLL------QKQRDYLTARIQ---------RLEHQ---------------LQLLQEAIN 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1865265942 498 DanlrkneletenrlvnQRLLEVQSQVEELQKslQDQGSKAEDSILLKKKLEEHLE 553
Cdd:PRK11281 252 S----------------KRLTLSEKTVQEAQS--QDEAARIQANPLVAQELEINLQ 289
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
364-641 |
8.74e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 8.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 364 ARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERDsLKETIEELRCVQAQEGQLTttglm 443
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID-VASAEREIAELEAELERLD----- 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 444 plgtqEPSDSLAaeivtpEIKEKLIRLQHEnkilklnqegsdnekiallqslLDDANLRKNELETENRLVNQRLLEVQSQ 523
Cdd:COG4913 682 -----ASSDDLA------ALEEQLEELEAE----------------------LEELEEELDELKGEIGRLEKELEQAEEE 728
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 524 VEELQKSLQDQGSKAEDsiLLKKKLEEHLEKLHEANNELQKKRAIIEDLEprcnNSSLKIEELQEALRKKEeemkqmeer 603
Cdd:COG4913 729 LDELQDRLEAAEDLARL--ELRALLEERFAAALGDAVERELRENLEERID----ALRARLNRAEEELERAM--------- 793
|
250 260 270
....*....|....*....|....*....|....*...
gi 1865265942 604 yKKYLEKAKSVIRTLDPkqNQGAAPEIQALKNQLQERD 641
Cdd:COG4913 794 -RAFNREWPAETADLDA--DLESLPEYLALLDRLEEDG 828
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
360-586 |
8.88e-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: 8.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 360 KANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERDSLKETIEELRCVQA------- 432
Cdd:TIGR04523 69 KINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDkflteik 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 433 ---QEGQLTTTGLMPLGTQEPS-----DSLAAEIVTPEIKEKLIRLQHENKILKLNQEGSDNEKIALLQSLLDDANLRKN 504
Cdd:TIGR04523 149 kkeKELEKLNNKYNDLKKQKEElenelNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNN 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 505 ELETENRLVNQRLLEVQSQVEELQKSLQDqgskaedsilLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRCNNSSLKIE 584
Cdd:TIGR04523 229 QLKDNIEKKQQEINEKTTEISNTQTQLNQ----------LKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEIS 298
|
..
gi 1865265942 585 EL 586
Cdd:TIGR04523 299 DL 300
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
351-591 |
9.56e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 9.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 351 TVSLEEELRKANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTE----RDSLKETIEE 426
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKvkelKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 427 LRCVQAQEGQLTTTGLMPLGTQEPSDSLAAEIvtpeikEKLIRlQHENKILKLNQEGSDNEKIALLQSLLDDAnLRKNEL 506
Cdd:COG1340 87 LNELREELDELRKELAELNKAGGSIDKLRKEI------ERLEW-RQQTEVLSPEEEKELVEKIKELEKELEKA-KKALEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 507 ETENRLVNQRLLEVQSQVEELQKSLQ---DQGSKAEDSIL-LKKKLEEHLEKLHEANNELQKKRAIIEDLEPRCNNSSLK 582
Cdd:COG1340 159 NEKLKELRAELKELRKEAEEIHKKIKelaEEAQELHEEMIeLYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKE 238
|
....*....
gi 1865265942 583 IEELQEALR 591
Cdd:COG1340 239 LRELRKELK 247
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
301-666 |
1.09e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 301 DEIDVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQAVELQN 380
Cdd:PRK03918 138 DAILESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELP 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 381 RLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERDSLKETIEELRcVQAQEGQLTTTGLMPLGTQEPSDSLAAEIVT 460
Cdd:PRK03918 218 ELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE-ERIEELKKEIEELEEKVKELKELKEKAEEYI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 461 PEIKEKLIRLQHENKILKLnqEGSDNEKIALLQSLLDDA---NLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGS- 536
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKR--LSRLEEEINGIEERIKELeekEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEl 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 537 ---KAEDSILLKKKLEEHLEKLHEANNELQKKraiIEDLEPRCNNSSLKIEELQEALRKkeeemkqmeerykkyLEKAKS 613
Cdd:PRK03918 375 erlKKRLTGLTPEKLEKELEELEKAKEEIEEE---ISKITARIGELKKEIKELKKAIEE---------------LKKAKG 436
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1865265942 614 VI----RTLDPKQNQGA----APEIQALKNQLQERDRMFHSLEKEYEKTKSQREMEEKFIV 666
Cdd:PRK03918 437 KCpvcgRELTEEHRKELleeyTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIK 497
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
261-428 |
1.33e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 261 LEAAKDDYRIRCEELEKEIAELRQQTeELTTLAEEAQSLKDEIDVLRhssDKVAKLESQVESYKKKLEdlgDLRRQVKLL 340
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKN-GLVDLSEEAKLLLQQLSELE---SQLAEARAELAEAEARLA---ALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 341 EEKNTMYMQNTV--SLEEELRKANAARSQLET-----------YKRQAVELQNRLSEESKKA-DKLDYECKRLKEKVDSL 406
Cdd:COG3206 253 PDALPELLQSPViqQLRAQLAELEAELAELSArytpnhpdviaLRAQIAALRAQLQQEAQRIlASLEAELEALQAREASL 332
|
170 180
....*....|....*....|..
gi 1865265942 407 QKEKDRLRTERDSLKETIEELR 428
Cdd:COG3206 333 QAQLAQLEARLAELPELEAELR 354
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
260-575 |
1.39e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 260 RLEAAKDDYRIRCEELEKEIAELRQQTEELTTLAEEAQSLKDEIDVLRHSSDK-VAKLESQVESYKKKLED-----LGDL 333
Cdd:pfam01576 409 KLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKdVSSLESQLQDTQELLQEetrqkLNLS 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 334 RRQVKLLEEKNTMYMQntvsLEEELRKANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQK----- 408
Cdd:pfam01576 489 TRLRQLEDERNSLQEQ----LEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQqleek 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 409 --EKDRLRTERDSLKETIEELRCVQAQEGQLTTTglmPLGTQEPSDSLAAEivtpeikEKLIRLQHENKILKLNQEGSDN 486
Cdd:pfam01576 565 aaAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSN---LEKKQKKFDQMLAE-------EKAISARYAEERDRAEAEAREK 634
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 487 EKIAL-LQSLLDDANLRKNELETENRLvnqrlleVQSQVEELQKSLQDQGSKAEDSILLKKKLEEHLEKLHEANNELQKK 565
Cdd:pfam01576 635 ETRALsLARALEEALEAKEELERTNKQ-------LRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDE 707
|
330
....*....|
gi 1865265942 566 RAIIEDLEPR 575
Cdd:pfam01576 708 LQATEDAKLR 717
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
266-376 |
1.69e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 266 DDYRIRCEELEKEIAELRQQTEELTtlAEEAQSLKDEIDVLRhssDKVAKLESQVESYKKKLEDLGDLRRQvklLEEKNt 345
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEQDEAS--FERLAELRDELAELE---EELEALKARWEAEKELIEEIQELKEE---LEQRY- 484
|
90 100 110
....*....|....*....|....*....|.
gi 1865265942 346 mymQNTVSLEEELRKANAARSQLETYKRQAV 376
Cdd:COG0542 485 ---GKIPELEKELAELEEELAELAPLLREEV 512
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
169-428 |
2.10e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 169 DAYVDLDRQLKKTTEELnEALATKEEIAQRCHELDMQVAALQEEKSSLLAENqilmerlnqsdsiedpnspAGRRHLQLQ 248
Cdd:COG4913 235 DDLERAHEALEDAREQI-ELLEPIRELAERYAAARERLAELEYLRAALRLWF-------------------AQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 249 TQLEQLQEETFRLEAAKDDYRIRCEELEKEIAELRQQTEELTTlaEEAQSLKDEIDVLRhssDKVAKLESQVESYKKKLE 328
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGG--DRLEQLEREIERLE---RELEERERRRARLEALLA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 329 DLGdlrrqvklleekntmyMQNTVSLEEELRKANAARSQLETYKRQAVELQNRLseeskkaDKLDYECKRLKEKVDSLQK 408
Cdd:COG4913 370 ALG----------------LPLPASAEEFAALRAEAAALLEALEEELEALEEAL-------AEAEAALRDLRRELRELEA 426
|
250 260
....*....|....*....|
gi 1865265942 409 EKDRLRTERDSLKETIEELR 428
Cdd:COG4913 427 EIASLERRKSNIPARLLALR 446
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
164-426 |
2.27e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 164 VSVGNDAYVDLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQsdsiedpnspagrr 243
Cdd:COG1340 17 IEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDE-------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 244 HLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEIAEL--RQQTEELTTlaEEAQSLKDEIDVLRHSSDKVAKLESQVE 321
Cdd:COG1340 83 LNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLewRQQTEVLSP--EEEKELVEKIKELEKELEKAKKALEKNE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 322 SYKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEELrkaNAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKE 401
Cdd:COG1340 161 KLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEM---IELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQK 237
|
250 260
....*....|....*....|....*
gi 1865265942 402 KVDSLQKEKDRLRTERDSLKETIEE 426
Cdd:COG1340 238 ELRELRKELKKLRKKQRALKREKEK 262
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
168-427 |
2.41e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 168 NDAYVDLDRQLKKTTEELNEALATKEEIAQrchELDMQVAALQEEKSSLLAENQILM-ERLNQSDSIEDPNSPAGRRHLQ 246
Cdd:TIGR04523 379 NQSYKQEIKNLESQINDLESKIQNQEKLNQ---QKDEQIKKLQQEKELLEKEIERLKeTIIKNNSEIKDLTNQDSVKELI 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 247 LQTQLEQLQEETFRLEAAKDDYRIRCEELEKEIAELRQQTEELTTLAEEAQSLKDEIDVLRHSSDKVAKLESQVESYKKK 326
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 327 LED-LGDLRRQVKLLEEKNTMYMQNTVSLE-----EELRKANAA----------------------RSQLETYKRQAVEL 378
Cdd:TIGR04523 536 KESkISDLEDELNKDDFELKKENLEKEIDEknkeiEELKQTQKSlkkkqeekqelidqkekekkdlIKEIEEKEKKISSL 615
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1865265942 379 QNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERDSLKETIEEL 427
Cdd:TIGR04523 616 EKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEI 664
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
192-428 |
2.49e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.07 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 192 KEEIAQRCHELD-MQVAALQEEKSS-----LLAENQILMERLNQSDSIEDPNSpagrrhlqlQTQLEQLQEETFRLEAAK 265
Cdd:PRK05771 18 KDEVLEALHELGvVHIEDLKEELSNerlrkLRSLLTKLSEALDKLRSYLPKLN---------PLREEKKKVSVKSLEELI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 266 DDYRIRCEELEKEIAELrqqTEELTTLAEEAQSLKDEIDVLrhssdkvaklesqvesykKKLEDLG-DLRRqvkLLEEKN 344
Cdd:PRK05771 89 KDVEEELEKIEKEIKEL---EEEISELENEIKELEQEIERL------------------EPWGNFDlDLSL---LLGFKY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 345 TMYMQNTVSLE-EELRKANAARSQLETYKR----------QAVELQNRLSEESKKAD--KLDY-ECKRLKEKVDSLQKEK 410
Cdd:PRK05771 145 VSVFVGTVPEDkLEELKLESDVENVEYISTdkgyvyvvvvVLKELSDEVEEELKKLGfeRLELeEEGTPSELIREIKEEL 224
|
250
....*....|....*...
gi 1865265942 411 DRLRTERDSLKETIEELR 428
Cdd:PRK05771 225 EEIEKERESLLEELKELA 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
274-427 |
2.62e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 274 ELEKEIAELRQQTEELTTLAEEAQSLKDEIDVLRHssdkvakLESQVESYKKKLEDLGDLRrqvklleekntmYMQNTVS 353
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIELLEP-------IRELAERYAAARERLAELE------------YLRAALR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 354 LEEELRKANAARSQLETYKRQAVELQNRLSEESKKADKLDYEC---------------KRLKEKVDSLQKEKDRLRTERD 418
Cdd:COG4913 283 LWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELdeleaqirgnggdrlEQLEREIERLERELEERERRRA 362
|
....*....
gi 1865265942 419 SLKETIEEL 427
Cdd:COG4913 363 RLEALLAAL 371
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
261-575 |
2.90e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.96 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 261 LEAAKDDYRIRCEE----LEKEIAELRQQTEELTTLAEEAQSLKDEIDVlrhSSDKVAKLESQVESYKKKLED----LGD 332
Cdd:pfam10174 343 LQTEVDALRLRLEEkesfLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDV---KERKINVLQKKIENLQEQLRDkdkqLAG 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 333 LRRQVKLLEEKNTMYMQNTVSLEEEL----RKANAARSQLETYKRQAVELqnrlSEESKKadkldyECKRLKEKVDSLQK 408
Cdd:pfam10174 420 LKERVKSLQTDSSNTDTALTTLEEALsekeRIIERLKEQREREDRERLEE----LESLKK------ENKDLKEKVSALQP 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 409 EKdrlrTERDSLKETIEELRCVQAQEGQLTTTGLMPLgtqepsdslaaEIVTPEIKEKLIRLQHEnkiLKLNQEGSDNEK 488
Cdd:pfam10174 490 EL----TEKESSLIDLKEHASSLASSGLKKDSKLKSL-----------EIAVEQKKEECSKLENQ---LKKAHNAEEAVR 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 489 IAllqsllDDANLRKNELETEnrlvnqrlleVQSQVEELQKSLQDqgskaedsillkkkLEEHLEKLHEANNELQKKRAI 568
Cdd:pfam10174 552 TN------PEINDRIRLLEQE----------VARYKEESGKAQAE--------------VERLLGILREVENEKNDKDKK 601
|
....*..
gi 1865265942 569 IEDLEPR 575
Cdd:pfam10174 602 IAELESL 608
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
298-575 |
3.28e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.68 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 298 SLKDEID-VLR--HSSDKVaklesQVESYKKKLEDLgdlrrQVKLLEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQ 374
Cdd:PRK05771 13 TLKSYKDeVLEalHELGVV-----HIEDLKEELSNE-----RLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 375 avELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERDSLK--ETIE-ELRCVQAQEGQLTTTGLMPLGTQEPS 451
Cdd:PRK05771 83 --SLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwGNFDlDLSLLLGFKYVSVFVGTVPEDKLEEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 452 DSLAAEIVTPEIKEKlirlqHENKILKLNQEGSDNEKIAllqSLLDDANLRKNELETENRL------VNQRLLEVQSQVE 525
Cdd:PRK05771 161 KLESDVENVEYISTD-----KGYVYVVVVVLKELSDEVE---EELKKLGFERLELEEEGTPselireIKEELEEIEKERE 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1865265942 526 ELQKSLQDQGSKAEDSIL--------LKKKLE--------------------EHLEKLHEANNELQKKRAIIEDLEPR 575
Cdd:PRK05771 233 SLLEELKELAKKYLEELLalyeyleiELERAEalskflktdktfaiegwvpeDRVKKLKELIDKATGGSAYVEFVEPD 310
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
273-663 |
5.04e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.09 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 273 EELEKEIAELRQQTEEL-TTLAEEAQSLKDEIDVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNT 351
Cdd:pfam05483 229 EEYKKEINDKEKQVSLLlIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRS 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 352 VS----LEEELRKANAARSQLETYKRQAVElqnrlsEESKKADKLDYECKRLKEKVDSLQkekDRLRTERDSLKETIEEL 427
Cdd:pfam05483 309 MStqkaLEEDLQIATKTICQLTEEKEAQME------ELNKAKAAHSFVVTEFEATTCSLE---ELLRTEQQRLEKNEDQL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 428 RCVqAQEGQLTTTGLMPLGTQEPSDSLAAEIVTPEIKEKLIRLQHENKILKLNQE--GSDNEKIALLQSL---LDDANLR 502
Cdd:pfam05483 380 KII-TMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEElkGKEQELIFLLQARekeIHDLEIQ 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 503 KNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDSILLKKKLEE-------HLEKLHE--ANNELQKKRAI--IED 571
Cdd:pfam05483 459 LTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQeasdmtlELKKHQEdiINCKKQEERMLkqIEN 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 572 LEPRCNNSSLKIEELQEALRkkeEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQA--LKNQLQERDRMFHSLEK 649
Cdd:pfam05483 539 LEEKEMNLRDELESVREEFI---QKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCnnLKKQIENKNKNIEELHQ 615
|
410
....*....|....
gi 1865265942 650 EYEKTKSQREMEEK 663
Cdd:pfam05483 616 ENKALKKKGSAENK 629
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
261-554 |
5.07e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.21 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 261 LEAAKDDYRIRCEELEKEIAELRQQTEELTTLAEEA-QSLKDEIDVLR-----HSSDKVAKLESQVESYKKKLEDLGDLR 334
Cdd:pfam12128 609 AEEALQSAREKQAAAEEQLVQANGELEKASREETFArTALKNARLDLRrlfdeKQSEKDKKNKALAERKDSANERLNSLE 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 335 RQVKLLEEKNTMYMQNTvslEEELRKANAARSQletyKRQAVELQNRLSEESKKADKLDYECKRlKEKVDSLQKEKDR-- 412
Cdd:pfam12128 689 AQLKQLDKKHQAWLEEQ---KEQKREARTEKQA----YWQVVEGALDAQLALLKAAIAARRSGA-KAELKALETWYKRdl 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 413 ------------LRTERDSLKETIEELrcvqAQEGQLTTTGLMPLGTQEPSDSLAAEIVTPEIKEKLIRLQHENKILKLN 480
Cdd:pfam12128 761 aslgvdpdviakLKREIRTLERKIERI----AVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIAD 836
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1865265942 481 QEgSDNEKIALLQSLLDDANLRKNELETENRLVNQRL--LEVQSQVEELQKSLQDQGSKAEDSILLKKKLEEHLEK 554
Cdd:pfam12128 837 TK-LRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLatLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKK 911
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
175-411 |
5.85e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 175 DRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSiedpnspagrrhlqlqtqleql 254
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA---------------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 255 qeetfRLEAAKDDYRIRCEELEKEIAELRQQTEELTTLAE--EAQSLKDEIDvlrhssdKVAKLESQVESYKKKLEDLGD 332
Cdd:COG3883 73 -----EIAEAEAEIEERREELGERARALYRSGGSVSYLDVllGSESFSDFLD-------RLSALSKIADADADLLEELKA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1865265942 333 LRRQVKLLEEKntmymqntvsLEEELRKANAARSQLETYKRqavELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKD 411
Cdd:COG3883 141 DKAELEAKKAE----------LEAKLAELEALKAELEAAKA---ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
262-411 |
5.94e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.11 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 262 EAAKDDYRIRCEELEK--EIAELRQQTEELTTLAEEAQSLKDEIDVLRHSSDKVakLESQVESYKKKLEdlgDLRRQVKL 339
Cdd:pfam17380 443 ERAREMERVRLEEQERqqQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKI--LEKELEERKQAMI---EEERKRKL 517
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1865265942 340 LeEKNTMYMQNTVSLEEELRKANAA-RSQLETYKRQAVELQNRL-SEESKKADKLDYECKRLKEKVDSLQKEKD 411
Cdd:pfam17380 518 L-EKEMEERQKAIYEEERRREAEEErRKQQEMEERRRIQEQMRKaTEERSRLEAMEREREMMRQIVESEKARAE 590
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
264-433 |
7.21e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 7.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 264 AKDDYRIRCEELEKEIAELRQQTEELTTLAEEAQSLKDEIDVLRhssDKVAKLESQVESYKKKLEDL-GDLRRQVKLLEE 342
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQ---AELEALQAEIDKLQAEIAEAeAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 343 K-NTMYMQ-NTVSLEEELRKAN---------AARSQLETYKRQAVELQNRLSEESKKADkldyecKRLKEKVDSLQKEKD 411
Cdd:COG3883 91 RaRALYRSgGSVSYLDVLLGSEsfsdfldrlSALSKIADADADLLEELKADKAELEAKK------AELEAKLAELEALKA 164
|
170 180
....*....|....*....|..
gi 1865265942 412 RLRTERDSLKETIEELRCVQAQ 433
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQ 186
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
173-597 |
8.89e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 8.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 173 DLDRQLKKTTEELNEALATKEEIAQRCHELDMQVAALQEEKSSLLAENQilMERLNQsDSIEDPNSPAGRRHLQLQTQLE 252
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG--LDDADA-EAVEARREELEDRDEELRDRLE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 253 QLQEETFRLEAAKDDYRIRCEELEKEIAELRQQTEELTTLAEEAQSlkdeidVLRHSSDKVAKLESQVESYKKKLED--- 329
Cdd:PRK02224 332 ECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEARE------AVEDRREEIEELEEEIEELRERFGDapv 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 330 -LGDLRRQVKLLEEKNTMYMQNTVSLEEELRKANAARSQ-------------------------LETYKRQAVELQNRLS 383
Cdd:PRK02224 406 dLGNAEDFLEELREERDELREREAELEATLRTARERVEEaealleagkcpecgqpvegsphvetIEEDRERVEELEAELE 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 384 EESKKADKLDYECKRLKEKVdSLQKEKDRLRTERDSLKETIEELRcVQAQEGQLTTTGLmplgtQEPSDSLAAEivtPEI 463
Cdd:PRK02224 486 DLEEEVEEVEERLERAEDLV-EAEDRIERLEERREDLEELIAERR-ETIEEKRERAEEL-----RERAAELEAE---AEE 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 464 KEKLIRLQHEN------KILKLNQEGSDN-------EKIALLQSLLDDA-------NLRKNELETENRLVNQRLLEVQSQ 523
Cdd:PRK02224 556 KREAAAEAEEEaeeareEVAELNSKLAELkerieslERIRTLLAAIADAedeierlREKREALAELNDERRERLAEKRER 635
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1865265942 524 VEELQKSLQDqgSKAEDSILLKKKLEEHLEKLHEANNELQKKRaiiedleprcnnsslkiEELQEALRKKEEEM 597
Cdd:PRK02224 636 KRELEAEFDE--ARIEEAREDKERAEEYLEQVEEKLDELREER-----------------DDLQAEIGAVENEL 690
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
360-637 |
9.41e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 38.98 E-value: 9.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 360 KANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERDSLKETIEELrcvQAQEGQLtt 439
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL---EKEIAEL-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 440 tglmplgtqepsdslaaeivtpeiKEKLIRLQHE-NKILKLNQEGSDNEKIALLQSLlDDANLRKNELETENRLVNQRll 518
Cdd:COG4942 96 ------------------------RAELEAQKEElAELLRALYRLGRQPPLALLLSP-EDFLDAVRRLQYLKYLAPAR-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 519 evQSQVEELQKSLQDQGSKAEDSILLKKKLEEHLEKLHEANNELQKKRAIIEDLeprcnnsslkIEELQEALRKKEEEMK 598
Cdd:COG4942 149 --REQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL----------LARLEKELAELAAELA 216
|
250 260 270
....*....|....*....|....*....|....*....
gi 1865265942 599 QMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQL 637
Cdd:COG4942 217 ELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
174-409 |
9.69e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 39.50 E-value: 9.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 174 LDRQLKKTTEELNEALATKEEIAqrcHELDMQVAALQEEKSSLLAENQILMERLnqsDSIEDPNSPAGRRHLQLQTQLEQ 253
Cdd:PLN02939 199 LEEQLEKLRNELLIRGATEGLCV---HSLSKELDVLKEENMLLKDDIQFLKAEL---IEVAETEERVFKLEKERSLLDAS 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 254 LQEETFRLEAAKDDYR----IRCEELEKEIAELRQQTEELTTLAEEAQSLKDEIDVLRhssDKVAKLESQVES---YKKK 326
Cdd:PLN02939 273 LRELESKFIVAQEDVSklspLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLR---DKVDKLEASLKEanvSKFS 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865265942 327 LEDLGDLRRQVKLLEEKntmymqntvsleeeLRKANAA-RSQLETYKRQAVELQ---NRLSEESKKadkldyecKRLKEK 402
Cdd:PLN02939 350 SYKVELLQQKLKLLEER--------------LQASDHEiHSYIQLYQESIKEFQdtlSKLKEESKK--------RSLEHP 407
|
....*..
gi 1865265942 403 VDSLQKE 409
Cdd:PLN02939 408 ADDMPSE 414
|
|
| |
