|
Name |
Accession |
Description |
Interval |
E-value |
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
144-671 |
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: 655.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 144 ELNEALSTKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQEETFRLEA 223
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 224 AKDDYRIRCEELEKEIAELRQQTEELTALAEEAQSLKDEIDVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQVKLLEEK 303
Cdd:pfam05622 81 ARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLGDLRRQVKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 304 NTMYMQNTVSLEEELRKANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERDSLKET 383
Cdd:pfam05622 161 NAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRET 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 384 IEELRCVQAQEGQLTTTGLMPLGRQEPSDSLAAEIVTPEIKEKLIRLQHENKILKLNQEGSDNEKIALLQSLLDDANLRK 463
Cdd:pfam05622 241 NEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLGQEGSYRERLTELQQLLEDANRRK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 464 NELETENRLVNQRLLEVQSQVEELQKSLQDQDSKAEDaiSVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRCN-NSS 542
Cdd:pfam05622 321 NELETQNRLANQRILELQQQVEELQKALQEQGSKAED--SSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDsNLA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 543 LKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQLQERDRMFHSLEKEYEKTKNQREM 622
Cdd:pfam05622 399 QKIDELQEALRKKDEDMKAMEERYKKYVEKAKSVIKTLDPKQNPASPPEIQALKNQLLEKDKKIEHLERDFEKSKLQREQ 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2024431993 623 EEKFIVSAWYNMGMTLHKKAAEDRLASTGS-GQSFLARQRQATSTRRSYP 671
Cdd:pfam05622 479 EEKLIVTAWYNMGMALHRKAIEERLAGLSSpGQSFLARQRQATNARRGLS 528
|
|
| HkD_Hook3 |
cd22226 |
Hook domain found in protein Hook 3 (Hook3) and similar proteins; Hook3 is an adaptor protein ... |
1-120 |
2.90e-79 |
|
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: 249.12 E-value: 2.90e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 1 MAQVLQKIDPVYFDENWLNRIKTEVGDNWRLKVSNLKKILKGILDYNHEILGQQINDFTLPDVNLIGEHADAAELGRMLQ 80
Cdd:cd22226 34 MAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEILGQQINDFTLPDVNLIGEHSDAAELGRMLQ 113
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2024431993 81 LILGCAVNCEQKQEYIQTIMMMEESVQHMVMAAIQELMSK 120
Cdd:cd22226 114 LILGCAVNCEQKQEYIQTIMMMEESVQHVVMTAIQELMSK 153
|
|
| HOOK_N |
pfam19047 |
HOOK domain; This domain is found at the N-terminus of HOOK proteins. |
1-121 |
9.63e-73 |
|
HOOK domain; This domain is found at the N-terminus of HOOK proteins.
Pssm-ID: 465958 Cd Length: 151 Bit Score: 231.91 E-value: 9.63e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 1 MAQVLQKIDPVYFDENWLNRIKTEVGDNWRLKVSNLKKILKGILDYNHEILGQQINDFTLPDVNLIGEHADAAELGRMLQ 80
Cdd:pfam19047 31 MAQVLHQIDPSWFTEAWLSRIKEDVGDNWRLKVSNLKKILQSVVDYYQDVLGQQISDFLLPDVNLIGEHSDPAELGRLLQ 110
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2024431993 81 LILGCAVNCEQKQEYIQTIMMMEESVQHMVMAAIQELMSKE 121
Cdd:pfam19047 111 LILGCAVNCEKKQEYIQQIMTLEESVQHVVMTAIQELMSKD 151
|
|
| HkD_Hook |
cd22222 |
Hook domain found in Hook family of microtubule-binding proteins; The Hook family includes ... |
1-119 |
5.66e-72 |
|
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: 229.83 E-value: 5.66e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 1 MAQVLQKIDPVYFDENWLNRIKTEVGDNWRLKVSNLKKILKGILDYNHEILGQQINDFTLPDVNLIGEHADAAELGRMLQ 80
Cdd:cd22222 29 IAQVLNQIDPEYFSDSWLSKIKPDVGDNWRLKVSNLKKILKGIVDYYSEVLGQQISGFTMPDVNAIAEKEDPKELGRLLQ 108
|
90 100 110
....*....|....*....|....*....|....*....
gi 2024431993 81 LILGCAVNCEQKQEYIQTIMMMEESVQHMVMAAIQELMS 119
Cdd:cd22222 109 LVLGCAVNCERKEEYIQAIMGLEESVQHVVMEAIQELMS 147
|
|
| HkD_Hook1 |
cd22225 |
Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a ... |
1-121 |
6.46e-62 |
|
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: 203.16 E-value: 6.46e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 1 MAQVLQKIDPVYFDENWLNRIKTEVGDNWRLKVSNLKKILKGILDYNHEILGQQINDFTLPDVNLIGEHADAAELGRMLQ 80
Cdd:cd22225 30 MAQVLHQIDSSWFDESWLSRIKEDVGDNWRIKMSNLKKILQGIVDYYHEFLDQQISEFLLPDLNRIAEHSDPVELGRLLQ 109
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2024431993 81 LILGCAVNCEQKQEYIQTIMMMEESVQHMVMAAIQELMSKE 121
Cdd:cd22225 110 LILGCAVNCEKKQEHIQNIMTLEESVQHVVMTAIQELMSKE 150
|
|
| HkD_Hook2 |
cd22227 |
Hook domain found in protein Hook 2 (Hook2) and similar proteins; Hook2 is a ... |
1-120 |
9.35e-55 |
|
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: 183.92 E-value: 9.35e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 1 MAQVLQKIDPVYFDENWLNRIKTEVGDNWRLKVSNLKKILKGILDYNHEILGQQINDFTLPDVNLIGEHADAAELGRMLQ 80
Cdd:cd22227 31 IAQVLNRIDPSWFNEAWLGRIKEDTGDNWRLKVSNLKKILQSLLEYYQDVLGHQVSEDHLPDVNLIGEFSDDTELGKLLQ 110
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2024431993 81 LILGCAVNCEQKQEYIQTIMMMEESVQHMVMAAIQELMSK 120
Cdd:cd22227 111 LVLGCAISCEKKQEHIQQIMTLEESVQHVVMEAIQELLTK 150
|
|
| HkD_SF |
cd22211 |
Hook domain-containing proteins superfamily; The Hook domain superfamily includes Hook adaptor ... |
1-119 |
3.05e-40 |
|
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: 144.34 E-value: 3.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 1 MAQVLQKIDPVYFDENWLNriKTEVGDNWRLKVSNLKKILKGILDYNHEILGQQINDFTLPDVNLIGEHADAAELGRMLQ 80
Cdd:cd22211 29 LAEILSQIDPSYFDSEWLE--SRDSSDNWVLKLNNLKKLYRSLSKYYREVLGQQLSDLPLPDLSAIARDGDEEEIVKLLE 106
|
90 100 110
....*....|....*....|....*....|....*....
gi 2024431993 81 LILGCAVNCEQKQEYIQTIMMMEESVQHMVMAAIQELMS 119
Cdd:cd22211 107 LVLGAAVQCENKEEYIARIQQLDESTQAELMLIIQEVLE 145
|
|
| HkD_HkRP |
cd22223 |
Hook domain found in the Hook-related protein (HkRP) family; The HkRP family includes Daple, ... |
1-117 |
4.81e-18 |
|
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: 81.48 E-value: 4.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 1 MAQVLQKIDPVYFDEnwlnRIKTEVGDNWRLKVSNLKKILKGILDYNHEILGQQINdFTLPDVNLIGEHADA----AELG 76
Cdd:cd22223 32 LNNVMLQIDPRPFSE----VSNRNVDDDVNARIQNLDLLLRNIKSFYQEVLQQLIV-MKLPDILTIGREPESeqslEELE 106
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2024431993 77 RMLQLILGCAVNCEQKQEYIQTIMMMEESVQHMVMAAIQEL 117
Cdd:cd22223 107 KLLLLLLGCAVQCERKEEFIERIKNLDLEVQHALVACIQEV 147
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
220-595 |
5.29e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 5.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 220 RLEAAKDDY---RIRCEELEKEIAELRQQTEeltaLAEEAQSLKDEIDVLrhssdkvaKLESQVESYKKKLEDLGDLRRQ 296
Cdd:COG1196 180 KLEATEENLerlEDILGELERQLEPLERQAE----KAERYRELKEELKEL--------EAELLLLKLRELEAELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 297 VKLLEEKNTMYMQNTVSLEEELRKANAARSQLEtykRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTE 376
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELE---LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 377 RDSLKETIEELrcvQAQEGQLTTTglmpLGRQEPSDSLAAEivtpEIKEKLIRLQHENKILKLNQEGSDNEKIALLQSLL 456
Cdd:COG1196 325 LAELEEELEEL---EEELEELEEE----LEEAEEELEEAEA----ELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 457 DDANLRKNELETENRLvnQRLLEVQSQVEELQKSLQDQDSKAEDAIsVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEP 536
Cdd:COG1196 394 AAAELAAQLEELEEAE--EALLERLERLEEELEELEEALAELEEEE-EEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024431993 537 RCNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQAL 595
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL 529
|
|
| HkD_Daple |
cd22228 |
Hook domain found in Daple (Dvl-associating protein with a high frequency of leucine residues) ... |
3-117 |
1.61e-12 |
|
Hook domain found in Daple (Dvl-associating protein with a high frequency of leucine residues) and similar proteins; Protein Daple, also called coiled-coil domain-containing protein 88C (CCDC88C), or Hook-related protein 2 (HkRP2), is a novel non-receptor nucleotide exchange factor (GEF) required for activation of guanine nucleotide-binding proteins (G-proteins) during non-canonical Wnt signaling.
Pssm-ID: 411799 Cd Length: 153 Bit Score: 65.72 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 3 QVLQKIDPVYFDEnwlnRIKTEVGDNWRLKVSNLKKILKGILDYNHEILgQQINDFTLPDVNLIGEH----ADAAELGRM 78
Cdd:cd22228 38 KIMLQIDPRPTNQ----RVNKHVNNDVNLRIQNLTILVRHIKTYYQEVL-QQLIVMNLPNVLMIGKDplsgKSMEEIKKM 112
|
90 100 110
....*....|....*....|....*....|....*....
gi 2024431993 79 LQLILGCAVNCEQKQEYIQTIMMMEESVQHMVMAAIQEL 117
Cdd:cd22228 113 LLLVLGCAVQCERKEEFIERIKQLDIETQAAIVSHIQEV 151
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
90-626 |
3.90e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.63 E-value: 3.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 90 EQKQEYIQTIMMMEESVQHMVMAAIQELMSKESPVSVGNDAYVDLDRQLKKTTEELNEALSTKEEIAqrchELDMQVAAL 169
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIE----ELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 170 QEEKSSLLAENQILMERLNQSDS-IEDPNSPAGR---------RHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEI 239
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKeIEELEEKVKElkelkekaeEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 240 AELRQQTEELTALAEEAQSLKDEIDVLRHSS---DKVAKLESQVESYKKKLEDL--GDLRRQVKLLEEKNTmymqntvSL 314
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEELEERHelyEEAKAKKEELERLKKRLTGLtpEKLEKELEELEKAKE-------EI 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 315 EEELRKANAARSQLETYKRQAVELQNRL--------------SEESKKADKLDY---------ECKRLKEKVDSLQKEKD 371
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKKAIEELkkakgkcpvcgrelTEEHRKELLEEYtaelkriekELKEIEEKERKLRKELR 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 372 RLRTERD------SLKETIEELRCVqaqEGQLTTTGLMPLGRQEPSdslaaeivTPEIKEKLIRLQHENKILKlnqegSD 445
Cdd:PRK03918 484 ELEKVLKkeseliKLKELAEQLKEL---EEKLKKYNLEELEKKAEE--------YEKLKEKLIKLKGEIKSLK-----KE 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 446 NEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQ-SQVEELQKSLQDQDSKAEDAISVL-LKKKLEEHLEKLHEANNE 523
Cdd:PRK03918 548 LEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKdAEKELEREEKELKKLEEE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 524 LQKKRAIIEDLEPRCNNSSLKIEELQealrkKEEEMKQMEERYKKYLEKAKSVirtldpkqnQGAAPEIQALKNQLQERD 603
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELEELE-----KKYSEEEYEELREEYLELSREL---------AGLRAELEELEKRREEIK 693
|
570 580
....*....|....*....|...
gi 2024431993 604 RMFHSLEKEYEKTKNQREMEEKF 626
Cdd:PRK03918 694 KTLEKLKEELEEREKAKKELEKL 716
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
220-537 |
5.41e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.77 E-value: 5.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 220 RLEAAKDDYRIRCEELEKEIAELRQQTEELTALAEEAQSLKDEID-VLRHSSDKVAKLESQVESYKKKLEdlgDLRRQVK 298
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQkELYALANEISRLEQQKQILRERLA---NLERQLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 299 LLEEkntmymqntvSLEEELRKANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERD 378
Cdd:TIGR02168 320 ELEA----------QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 379 SLKETIEelrcvqaqegqltttglmplgrqepsdSLAAEIVtpEIKEKLIRLQHENKILKLNQEGSDNE----KIALLQS 454
Cdd:TIGR02168 390 QLELQIA---------------------------SLNNEIE--RLEARLERLEDRRERLQQEIEELLKKleeaELKELQA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 455 LLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQDSKAEDAISVL-LKKKLEEHLEKLHEANNELQKKRAIIED 533
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLdSLERLQENLEGFSEGVKALLKNQSGLSG 520
|
....
gi 2024431993 534 LEPR 537
Cdd:TIGR02168 521 ILGV 524
|
|
| HkD_Girdin |
cd22229 |
Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation ... |
20-117 |
1.10e-09 |
|
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: 57.49 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 20 RIKTEVGDNWRLKVSNLKKILKGILDYNHEILgQQINDFTLPDVNLIG-----EHAdAAELGRMLQLILGCAVNCEQKQE 94
Cdd:cd22229 54 RVNKKVNNDASLRIQNLSILVKQIKLYYQETL-QQLIMMSLPNVLVLGrnplsEQG-TEEMKKLLLLLLGCAVQCERKEE 131
|
90 100
....*....|....*....|...
gi 2024431993 95 YIQTIMMMEESVQHMVMAAIQEL 117
Cdd:cd22229 132 FIERIQTLDFDTKAAVAAHIQEV 154
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
220-535 |
1.74e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.23 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 220 RLEAAKDDYRIRCEELEKEIAELRQQTEELTALAEEAQSLKDEIDVLRHSSDK-VAKLESQVESYKKKLEDL----GDLR 294
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdLARLEAEVEQLEERIAQLskelTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 295 RQVKLLEEKNTMYMQNTVSLEEEL----RKANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEK 370
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIeeleAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 371 DRLRTERDSLKETIEELRCVQAQEGQLTTtglmplgrqepsdslaaeivtpEIKEKLIRLqhenkilkLNQEGSDNEKIA 450
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIE----------------------ELESELEAL--------LNERASLEEALA 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 451 LLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQDSKAE---DAISVLLKKKLEEHLEKLHEANNELQKK 527
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDnlqERLSEEYSLTLEEAEALENKIEDDEEEA 970
|
....*...
gi 2024431993 528 RAIIEDLE 535
Cdd:TIGR02168 971 RRRLKRLE 978
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
129-625 |
2.29e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 129 DAYVDLDRQLKKTTEELNEALSTKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQ--------SDSIEDPNSPA 200
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPElreeleklEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 201 GRRHLQLQTQLEQLQEETfRLEAAKDDYRIRCEELEKEIAELRQQTEELTALAEEAQS-------LKDEIDVLRHSSDKV 273
Cdd:PRK03918 238 EEIEELEKELESLEGSKR-KLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiklsefYEEYLDELREIEKRL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 274 AKLESQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQAVELQNRLSEE-SKKADKL 352
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKlEKELEEL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 353 DYECKRLKEKVDSLQKEKDRLRTERDSLKETIEELRcvqAQEGQLTTTG----------LMPLGRQEPSDSLAAEIVTPE 422
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGELKKEIKELKKAIEELK---KAKGKCPVCGrelteehrkeLLEEYTAELKRIEKELKEIEE 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 423 IKEKL-IRLQHENKILKLNQEGSDNEKIA----LLQSLLDDANLRKNELETEN-RLVNQRLLEVQSQVEELQKSLqdqdS 496
Cdd:PRK03918 474 KERKLrKELRELEKVLKKESELIKLKELAeqlkELEEKLKKYNLEELEKKAEEyEKLKEKLIKLKGEIKSLKKEL----E 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 497 KAEDaisvlLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRCnnsslkIEELQEALRKKEEEmkqmeerYKKYLEkAKSV 576
Cdd:PRK03918 550 KLEE-----LKKKLAELEKKLDELEEELAELLKELEELGFES------VEELEERLKELEPF-------YNEYLE-LKDA 610
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2024431993 577 IRTLDPKQNqgaapEIQALKNQLQERDRMFHSLEKEYEKTKNQREMEEK 625
Cdd:PRK03918 611 EKELEREEK-----ELKKLEEELDKAFEELAETEKRLEELRKELEELEK 654
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
220-601 |
2.47e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.82 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 220 RLEAAKDDYRIRCEELEKEIAEL----RQQTEELTALAEEAQSLKDEIDVLRHSSDKVAKLESQVESYKKKLED-LGDLR 294
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREELaeevRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDrLEECR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 295 RQVKLLEEKNTMYMQNTVSLEE---ELR--------KANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKV 363
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDLEEraeELReeaaelesELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 364 DSLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTTGLMPLGRQEPSDSLAAEIVTpEIKEKLIRLQHENKILKLNQEG 443
Cdd:PRK02224 415 EELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIE-EDRERVEELEAELEDLEEEVEE 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 444 SDN--EKIALLQSLLDDANLRKNELETENRLVNQR---LLEVQSQVEELQKSLQDQDSKAEDAISVLLKKKL--EEHLEK 516
Cdd:PRK02224 494 VEErlERAEDLVEAEDRIERLEERREDLEELIAERretIEEKRERAEELRERAAELEAEAEEKREAAAEAEEeaEEAREE 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 517 LHEANNELQKKRAIIEDLEpRCNNSSLKIEELQ---EALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQ 593
Cdd:PRK02224 574 VAELNSKLAELKERIESLE-RIRTLLAAIADAEdeiERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAR 652
|
....*...
gi 2024431993 594 ALKNQLQE 601
Cdd:PRK02224 653 EDKERAEE 660
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
133-492 |
5.19e-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: 59.70 E-value: 5.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 133 DLDRQLKKTTEELNEALSTKEEIAQRCHELDMQVAALQEEKSSLLaENQILMERLnqsdsIEDPNSPAGRRHLQLQTQLE 212
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEK-----REYEGYELLKEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 213 QLQEETFRLEAAKDDYRIRCEELEKEIAELRQQTEELTA-----LAEEAQSLKDEIDVLrhsSDKVAKLESQVESYKKKL 287
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKkikdlGEEEQLRVKEKIGEL---EAEIASLERSIAEKEREL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 288 EDLGDLRRQVKLLEEKNTMYMQNtvsLEEELRKANAARSQLET--YKRQAV--ELQNRLSEESKKADKLDYECKRLKEKV 363
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEE---LEREIEEERKRRDKLTEeyAELKEEleDLRAELEEVDKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 364 DSLQKEKDRLRTERDSLKETIEELRCVQAQegqltttglmplgrqepsdsLAAEIvtPEIKEKLIRLQHENKILKLNQEg 443
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELAD--------------------LNAAI--AGIEAKINELEEEKEDKALEIK- 451
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2024431993 444 SDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQ 492
Cdd:TIGR02169 452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAR 500
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
233-540 |
6.61e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.30 E-value: 6.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 233 EELEKEIAELRQQTEELTA---LAEEAQSLKDEIDVLRHSSdKVAKLESQVESYKKKLEDLGDLRRQVKLLEEKNTMYmq 309
Cdd:TIGR02168 189 DRLEDILNELERQLKSLERqaeKAERYKELKAELRELELAL-LVLRLEELREELEELQEELKEAEEELEELTAELQEL-- 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 310 ntvslEEELRKANAARSQLEtykRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERD----SLKETIE 385
Cdd:TIGR02168 266 -----EEKLEELRLEVSELE---EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEelesKLDELAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 386 ELRCVQAQEGQLTTTGLMPLGRQEPSDSLAAEIVT-PEIKEKLIRLQHENKILKLNQEGSDNEKIALLQSLLDDANLRKN 464
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLEAELEELEAELEELESrLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 465 ELETEN-----RLVNQRLLEVQSQVEELQKSLQDQDSKAEDAISVL--LKKKLEEHLEKLHEANNELQKKRAIIEDLEPR 537
Cdd:TIGR02168 418 RLQQEIeellkKLEEAELKELQAELEELEEELEELQEELERLEEALeeLREELEEAEQALDAAERELAQLQARLDSLERL 497
|
...
gi 2024431993 538 CNN 540
Cdd:TIGR02168 498 QEN 500
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
134-388 |
8.24e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 8.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 134 LDRQLKKTTEELNEALSTKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDPNSpagRRHLQLQTQLEQ 213
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE---ERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 214 LQEETFRLEAAKDDYRIRCEELEKEIAELRQQTEEltALAEEAQSLKDEIDVLRHSSDKVAKLESQVESYKKKLEDLGDL 293
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEE--AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 294 RRQVKLLEEKNTMYMQNTVSLEEELRKANAARSQLEtykRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRL 373
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELE---EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
250
....*....|....*
gi 2024431993 374 RTERDSLKETIEELR 388
Cdd:COG1196 476 EAALAELLEELAEAA 490
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
133-624 |
2.61e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 133 DLDRQLKKTTEELNEALSTKEEIAQRCHELDMQVAALQEEKSSLLA-----ENQILMERLNQSDSIEDpnspAGRRHLQL 207
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAelarlEQDIARLEERRRELEER----LEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 208 QTQLEQLQEETFRLEAAKDDYRIRCEELEKEIAELRQQTEELTALAEEAQSLKDEIDVLRhsSDKVAKLESQVESYKKKL 287
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA--EELLEALRAAAELAAQLE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 288 EDLGDLRRQVKLLEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQ 367
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 368 KEKDRLRTERDSLKETIEE----LRCVQAQEGQLTTTGLMPLGRQEPSDSLAAEIVTPE---------IKEKLIRLQHEN 434
Cdd:COG1196 484 EELAEAAARLLLLLEAEADyegfLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAalaaalqniVVEDDEVAAAAI 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 435 KILKLNQEGsdneKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQDSKAEDAISVLLKKKLEEHL 514
Cdd:COG1196 564 EYLKAAKAG----RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRA 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 515 EKLHEANNELQKKRAIIEDLEPRCNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQA 594
Cdd:COG1196 640 VTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEE 719
|
490 500 510
....*....|....*....|....*....|
gi 2024431993 595 LKNQLQERDRMFHSLEKEYEKTKNQREMEE 624
Cdd:COG1196 720 ELEEEALEEQLEAEREELLEELLEEEELLE 749
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
173-625 |
3.03e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 173 KSSLLA-ENQILMERLNQSdsIEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEIAELRQQTEELTA 251
Cdd:COG4717 36 KSTLLAfIRAMLLERLEKE--ADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 252 LAEEAQSLKDEIDVLRHSSD------KVAKLESQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEELRkaNAAR 325
Cdd:COG4717 114 LREELEKLEKLLQLLPLYQElealeaELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLS--LATE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 326 SQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKdrlrtERDSLKETIEELR----------CVQAQEG 395
Cdd:COG4717 192 EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL-----EAAALEERLKEARlllliaaallALLGLGG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 396 QLTTTGLMPLGRQEPSDSLAAEIVTPEIKEKLIRLQHENKILKLN-QEGSDNEKIALLQSLLDDANLRKNELETENRLVN 474
Cdd:COG4717 267 SLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPaLEELEEEELEELLAALGLPPDLSPEELLELLDRI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 475 QRLLEVQSQVEELQKSLQDQDskAEDAISVLLKK---KLEEHLEKLHEANNELQKKRAIIEDLEPRCNNSSLKIEELQEA 551
Cdd:COG4717 347 EELQELLREAEELEEELQLEE--LEQEIAALLAEagvEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEA 424
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024431993 552 LrkkeeemkqMEERYKKYLEKAKSVIRTLDPKQNQgAAPEIQALKNQLQ--ERDRMFHSLEKEYEKTKNQREMEEK 625
Cdd:COG4717 425 L---------DEEELEEELEELEEELEELEEELEE-LREELAELEAELEqlEEDGELAELLQELEELKAELRELAE 490
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
133-388 |
9.08e-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: 55.83 E-value: 9.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 133 DLDRQLKKTTEELNEALSTKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSiedpnspagrrhlqlqtQLE 212
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER-----------------QLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 213 QLQEETFRLEAAKDDYRIRCEELEKEIAELRQQTEELTALAEEAQSLKDEI--------DVLRHSSDKVAKLESQVESYK 284
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELesrleeleEQLETLRSKVAQLELQIASLN 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 285 KKLEdlgDLRRQVKLLEEKNTMYMQNTVSLEEELRKAN--AARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEK 362
Cdd:TIGR02168 400 NEIE---RLEARLERLEDRRERLQQEIEELLKKLEEAElkELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
250 260
....*....|....*....|....*.
gi 2024431993 363 VDSLQKEKDRLRTERDSLKETIEELR 388
Cdd:TIGR02168 477 LDAAERELAQLQARLDSLERLQENLE 502
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
134-431 |
1.09e-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: 55.46 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 134 LDRQLKKTTEELNEALSTKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDsiedpnspagRRHLQLQTQLEQ 213
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK----------ERLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 214 LQEETFRLEAAKDDYRIRCEELEKEIAELRQQTEELTalAEEAQSLKDEI-DVLRHSSDKVAKLESQVESYKKKLEDlgd 292
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE--ARLSHSRIPEIqAELSKLEEEVSRIEARLREIEQKLNR--- 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 293 lRRQVKLLEEKNTMYMQNTVSLEEELRKANAAR-----SQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQ 367
Cdd:TIGR02169 824 -LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEienlnGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024431993 368 KEKDRLRTERDSLKETIEELRC-VQAQEGQLTTTG-LMPLGRQEPSDSLAAEIVTPEIKEKLIRLQ 431
Cdd:TIGR02169 903 RKIEELEAQIEKKRKRLSELKAkLEALEEELSEIEdPKGEDEEIPEEELSLEDVQAELQRVEEEIR 968
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
90-614 |
1.39e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 55.12 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 90 EQKQEYIQTIMMMEESVQHMVMA--AIQELMSKEspvsvgNDAYVDLDRQLKKTTEELNEALSTKEEIaqrcheLDMQVA 167
Cdd:pfam15921 103 KQKFYLRQSVIDLQTKLQEMQMErdAMADIRRRE------SQSQEDLRNQLQNTVHELEAAKCLKEDM------LEDSNT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 168 ALQEEKSSLLAENQILMERLNQSDSIEDPNSPAGRRHlqlqtqlEQLQEETFRLEAAKDDYRIRceELEKEIAELRQQT- 246
Cdd:pfam15921 171 QIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEH-------DSMSTMHFRSLGSAISKILR--ELDTEISYLKGRIf 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 247 ---EELTALAEEAQSlKDEIdVLRHSSDKVAKLESQVEsykkkLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEelrkana 323
Cdd:pfam15921 242 pveDQLEALKSESQN-KIEL-LLQQHQDRIEQLISEHE-----VEITGLTEKASSARSQANSIQSQLEIIQEQ------- 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 324 ARSQLETYKRQAVELQNRLSEESKKADkldyECKRLKE-KVDSLQK-------EKDRLRTERDSLKEtieelrcvqaQEG 395
Cdd:pfam15921 308 ARNQNSMYMRQLSDLESTVSQLRSELR----EAKRMYEdKIEELEKqlvlansELTEARTERDQFSQ----------ESG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 396 QLtttglmplgrqepSDSLAAEIVTPEIKEKLIRLQHENKILKLNQEGSDNEKIALLQSLLDDANLRKNELETenrLVNQ 475
Cdd:pfam15921 374 NL-------------DDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEA---LLKA 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 476 RLLEVQSQVEELQKSLQDQDSKAEDAISvlLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRCNNSSLKIEELQEALRKK 555
Cdd:pfam15921 438 MKSECQGQMERQMAAIQGKNESLEKVSS--LTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEAT 515
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024431993 556 EEEMKQMEERYKKYLEKAKSVIRTLDPKQNqgAAPEIQALKNQLQERDRMFHSLEKEYE 614
Cdd:pfam15921 516 NAEITKLRSRVDLKLQELQHLKNEGDHLRN--VQTECEALKLQMAEKDKVIEILRQQIE 572
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
220-668 |
3.01e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 220 RLEAAKDDYRIRCEELEKEIAELRQQTEELTALAEEAQSLkdeidvLRHSSDKVAKLESQVESYKKKLEDLgdLRRQVKL 299
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAE------EYELLAELARLEQDIARLEERRREL--EERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 300 LEEKNtmymQNTVSLEEELRKANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERDS 379
Cdd:COG1196 322 EEELA----ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 380 LKETIEELRCVQAQEgqltttglmpLGRQEPSDSLAAEIVTPEIKEKLIRLQHENKILKLNQEgsDNEKIALLQSLLDDA 459
Cdd:COG1196 398 LAAQLEELEEAEEAL----------LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE--EAELEEEEEALLELL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 460 NLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQDSKAEDAISVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEprcn 539
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE---- 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 540 nsslkiEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQN-QGAAPEIQALKNQLQERDRMFHSLEKEYEKTKN 618
Cdd:COG1196 542 ------AALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKiRARAALAAALARGAIGAAVDLVASDLREADARY 615
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2024431993 619 QREME---EKFIVSAWYNMGMTLHKKAAEDRLASTGSGQSFLARQRQATSTRR 668
Cdd:COG1196 616 YVLGDtllGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR 668
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
288-553 |
4.49e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 4.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 288 EDLGDLRRQVKLLEEKNTMYmQNTVSLEEELRKANAARSQLETYKRQavelqnrlseesKKADKLDYECKRLKEKVDSLQ 367
Cdd:COG4913 242 EALEDAREQIELLEPIRELA-ERYAAARERLAELEYLRAALRLWFAQ------------RRLELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 368 KEKDRLRTERDSLKETIEELRCVQAQEGqltttglmplGRQEpsDSLAAEIVTPEIKEKLIRLQHENkilklnqegsdne 447
Cdd:COG4913 309 AELERLEARLDALREELDELEAQIRGNG----------GDRL--EQLEREIERLERELEERERRRAR------------- 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 448 kialLQSLLDDANLRKNELETEnrlvnqrLLEVQSQVEELQKSLQDQDSKAEDAISvllkkkleEHLEKLHEANNELQKK 527
Cdd:COG4913 364 ----LEALLAALGLPLPASAEE-------FAALRAEAAALLEALEEELEALEEALA--------EAEAALRDLRRELREL 424
|
250 260
....*....|....*....|....*.
gi 2024431993 528 RAIIEDLEPRCNNSSLKIEELQEALR 553
Cdd:COG4913 425 EAEIASLERRKSNIPARLLALRDALA 450
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
231-627 |
5.13e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 5.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 231 RCEELEKEIAELRQQTEELTALAEE---AQSLKDEIDVLRHSSD--KVAKLESQVESYKKKLEDLGDLRRQVKLLEEKNT 305
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKAAAAkkkADEAKKKAEEKKKADEakKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 306 MymQNTVSLEEELRKANAARSQLETYKRQAVELQNRlSEESKKADKLDY--------ECKRLKEKVDSLQKEKDRLRTER 377
Cdd:PTZ00121 1472 A--DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA-AEAKKKADEAKKaeeakkadEAKKAEEAKKADEAKKAEEKKKA 1548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 378 DSLKETiEELRcvQAQEGQLTTTGLMPLGRQEPSDSLAAEIVTPEIK--EKLIRLQHENKILKLNQEGSDNEKIALLQSL 455
Cdd:PTZ00121 1549 DELKKA-EELK--KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAriEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL 1625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 456 LDDANLRKNELEtenrlVNQRLLEVQSQVEELQKSLQDQDSKAEDaisvlLKKKLEEHLEKLHEANNELQKKRAIIEDLE 535
Cdd:PTZ00121 1626 KKAEEEKKKVEQ-----LKKKEAEEKKKAEELKKAEEENKIKAAE-----EAKKAEEDKKKAEEAKKAEEDEKKAAEALK 1695
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 536 pRCNNSSLKIEELqealRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAApEIQALKNQLQERDRMFHSLEKEYEK 615
Cdd:PTZ00121 1696 -KEAEEAKKAEEL----KKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK-KAEEAKKDEEEKKKIAHLKKEEEKK 1769
|
410
....*....|..
gi 2024431993 616 TKNQREMEEKFI 627
Cdd:PTZ00121 1770 AEEIRKEKEAVI 1781
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
233-386 |
6.70e-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: 6.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 233 EELEKEIAELRqqtEELTALAEEAQSLKDEIDVLRhssdKVAKLESQVESYKKKLEDLGDLRRQVklleekntmymqntV 312
Cdd:COG4913 613 AALEAELAELE---EELAEAEERLEALEAELDALQ----ERREALQRLAEYSWDEIDVASAEREI--------------A 671
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024431993 313 SLEEELRKANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERDSLKETIEE 386
Cdd:COG4913 672 ELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
220-388 |
8.02e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 8.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 220 RLEAAKDDYRIRCEELEKEIAELRQQTEELTALAE-------------EAQSLKDEIDVLRHSSDKVAKLESQVESYKKK 286
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeidvasaerEIAELEAELERLDASSDDLAALEEQLEELEAE 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 287 LEDL----GDLRRQVKLLEEKNTmymqntvSLEEELRKANAARSQLETYKRQAV--ELQNRLSEESKKAdkldyeckRLK 360
Cdd:COG4913 701 LEELeeelDELKGEIGRLEKELE-------QAEEELDELQDRLEAAEDLARLELraLLEERFAAALGDA--------VER 765
|
170 180
....*....|....*....|....*...
gi 2024431993 361 EKVDSLQKEKDRLRTERDSLKETIEELR 388
Cdd:COG4913 766 ELRENLEERIDALRARLNRAEEELERAM 793
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
222-621 |
8.99e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 8.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 222 EAAKDDYRIRCEELEKEiAELRQQTEELTALAEEAQSLKDEIDvlrhssdKVAKLESQVESYKKKLEDLGDLRRQVKLLE 301
Cdd:PTZ00121 1370 EKKKEEAKKKADAAKKK-AEEKKKADEAKKKAEEDKKKADELK-------KAAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 302 EKNTMymQNTVSLEEELRKANAARSQLETyKRQAVELQNRlSEESKKADKLDYECKRLKEKVDSLQKEKDRlrterdslK 381
Cdd:PTZ00121 1442 EAKKA--DEAKKKAEEAKKAEEAKKKAEE-AKKADEAKKK-AEEAKKADEAKKKAEEAKKKADEAKKAAEA--------K 1509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 382 ETIEELRcvQAQEGQLTTTGlmplgRQEPSDSLAAEIVTPEIKEKLIRLQHENKILKLNQEGSDNEKiallQSLLDDANL 461
Cdd:PTZ00121 1510 KKADEAK--KAEEAKKADEA-----KKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEA----KKAEEDKNM 1578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 462 RKNELETENRLVNQRLLEVQSQVEELQKSLQDQDSKAEDA-ISVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRCNN 540
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAkIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 541 SSLKIEELQ----------EALRKKEEEMKQMEERYKKYLEKAKSVIRTldPKQNQGAAPEIQALKNQLQERDRMFHSLE 610
Cdd:PTZ00121 1659 NKIKAAEEAkkaeedkkkaEEAKKAEEDEKKAAEALKKEAEEAKKAEEL--KKKEAEEKKKAEELKKAEEENKIKAEEAK 1736
|
410
....*....|.
gi 2024431993 611 KEYEKTKNQRE 621
Cdd:PTZ00121 1737 KEAEEDKKKAE 1747
|
|
| HkD_Gipie |
cd22230 |
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar ... |
4-117 |
1.10e-06 |
|
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: 49.06 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 4 VLQKIDPVYFDENWLNRikteVGDNWRLKVSNLKKILKGILDYNHEILgQQINDFTLPDVNLIGEH----ADAAELGRML 79
Cdd:cd22230 56 VMGIIDPSPRGGPRMRG----DDGPAAHRVQNLHILWGRLRDFYQEEL-QQLILSPPPDLQVMGRDpfteEAVQELEKLL 130
|
90 100 110
....*....|....*....|....*....|....*...
gi 2024431993 80 QLILGCAVNCEQKQEYIQTIMMMEESVQHMVMAAIQEL 117
Cdd:cd22230 131 RLLLGAAVQCERRELFIRHIQGLDLDVQAELAEAIQEV 168
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
133-601 |
1.26e-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: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 133 DLDRQLKKTTEELNEALSTKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDpnsPAGRRHLQLQTQLE 212
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA---EAEEELEELAEELL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 213 QLQEETFRLEAAKDDYRIRCEELEKEIAELRQQTEEL-TALAEEAQSLKDEIDVLRHSSDKVAKLESQVESYKKKLEDLG 291
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELeEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 292 DLRRQVKLLEEKNTMYMQNTVSLEEELRKANAARSQ-LETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEK 370
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGfLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 371 DRLRTERDSLKETIEELRcvQAQEGQLTttgLMPLGRQEPSDSLAAEIVTPEIKEKLIRLQHENKIL--KLNQEGSDNEK 448
Cdd:COG1196 550 NIVVEDDEVAAAAIEYLK--AAKAGRAT---FLPLDKIRARAALAAALARGAIGAAVDLVASDLREAdaRYYVLGDTLLG 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 449 IALLQSLLDDANLRKNELETENRLVNQ--RLLEVQSQVEELQKSLQDQDSKAEDAISVLLKKKLEEHLEKLHEANNELQK 526
Cdd:COG1196 625 RTLVAARLEAALRRAVTLAGRLREVTLegEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEE 704
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024431993 527 KRAIIEDLEPRCNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQgAAPEIQALKNQLQE 601
Cdd:COG1196 705 EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEE-LERELERLEREIEA 778
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
139-391 |
3.30e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 139 KKTTEELNEALSTKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDsiEDPNSPAGRRHLQLQTQLEQLQEET 218
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE--EKKKAEEAKKAEEDKNMALRKAEEA 1586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 219 FRLEAAKDDYRIRCEELEKEI-AELRQQTEELTALAEEAQSLKDEIDVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQV 297
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEEKKMkAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 298 KLLEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTER 377
Cdd:PTZ00121 1667 AKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA 1746
|
250
....*....|....
gi 2024431993 378 DSLKETIEELRCVQ 391
Cdd:PTZ00121 1747 EEAKKDEEEKKKIA 1760
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
150-400 |
3.62e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 150 STKEEIAQRCHELDMQVAALQEEKSSL---LAENQILMERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKD 226
Cdd:PRK02224 468 ETIEEDRERVEELEAELEDLEEEVEEVeerLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAA 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 227 DYRIRCEELEKEIAELRQQTEE----LTALAEEAQSLKDEIDVL---RHSSDKVAKLESQVESYKKKLEDLGDLRRQVK- 298
Cdd:PRK02224 548 ELEAEAEEKREAAAEAEEEAEEareeVAELNSKLAELKERIESLeriRTLLAAIADAEDEIERLREKREALAELNDERRe 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 299 LLEEKNTMYMQNTVSLEEE-LRKANAARSQLETYKRQAVElqnRLSEESKKADKLDYECKRLKEKVDSLqkekDRLRTER 377
Cdd:PRK02224 628 RLAEKRERKRELEAEFDEArIEEAREDKERAEEYLEQVEE---KLDELREERDDLQAEIGAVENELEEL----EELRERR 700
|
250 260
....*....|....*....|...
gi 2024431993 378 DSLKETIEELRCVQAQEGQLTTT 400
Cdd:PRK02224 701 EALENRVEALEALYDEAEELESM 723
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
133-430 |
5.17e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 5.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 133 DLDRQLKKTTEELNEALSTKEEIAQRCHELDMQVAALQEEKSSLLAE----NQILMERLNQSDSIEDPNSPAGRRHLQLQ 208
Cdd:TIGR02168 723 ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERleeaEEELAEAEAEIEELEAQIEQLKEELKALR 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 209 TQLEQLQEETFRLEAAKDDYRIRCEELEKEIAELRQQTEELTALAEEAqslkdeidvlrhsSDKVAKLESQVESYKKKLE 288
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL-------------SEDIESLAAEIEELEELIE 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 289 DLgdLRRQVKLLEEKNtmymqntvSLEEELRKANAARSQLETykrqavelqnRLSEESKKADKLDYECKRLKEKVDSLQK 368
Cdd:TIGR02168 870 EL--ESELEALLNERA--------SLEEALALLRSELEELSE----------ELRELESKRSELRRELEELREKLAQLEL 929
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024431993 369 EKDRLRTERDSLKETIEElrcvqaqEGQLTTTGLMPLGRQEPSDSLAAEIVTPEIKEKLIRL 430
Cdd:TIGR02168 930 RLEGLEVRIDNLQERLSE-------EYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
422-625 |
5.63e-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: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 422 EIKEKLIRLQHENKILKLN----QEGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQDSK 497
Cdd:COG1196 217 ELKEELKELEAELLLLKLReleaELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 498 AEDAISVL--LKKKLEEHLEKLHEANNELQKKRAIIEDLEPRCNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKS 575
Cdd:COG1196 297 LARLEQDIarLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2024431993 576 VIRTLDPKQNQGAAP--EIQALKNQLQERDRMFHSLEKEYEKTKNQREMEEK 625
Cdd:COG1196 377 AEEELEELAEELLEAlrAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
220-386 |
7.97e-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: 47.61 E-value: 7.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 220 RLEAAKDDYRIRCEELEKEIAELRQQTEELTALAEEAQSLKDEIDV-LRHSSDKVAKLESQVESYKKKLEDLGDLRRQVK 298
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKeIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 299 LLEEKNTMYMQNTVsLEEELRKANAarsQLETYKRQAVELQNRLSEeskKADKLDYECKRLKEKVDSLQKEKDRLRTERD 378
Cdd:COG1579 94 LQKEIESLKRRISD-LEDEILELME---RIEELEEELAELEAELAE---LEAELEEKKAELDEELAELEAELEELEAERE 166
|
....*...
gi 2024431993 379 SLKETIEE 386
Cdd:COG1579 167 ELAAKIPP 174
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
233-547 |
9.81e-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: 9.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 233 EELEKEIAELRQQTEELTALAEEAQS-LKDEIDVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNT 311
Cdd:pfam02463 205 QAKKALEYYQLKEKLELEEEYLLYLDyLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQ 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 312 VSLEEEL-RKANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERDSLKETIEELRCV 390
Cdd:pfam02463 285 EEELKLLaKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 391 QAQEGQLtttglmplgRQEPSDSLAAEIVTPEIKEKLIRLQHEnkiLKLNQEGSDNEKIALLQSLLDDANLRKNELETEN 470
Cdd:pfam02463 365 QEKLEQL---------EEELLAKKKLESERLSSAAKLKEEELE---LKSEEEKEAQLLLELARQLEDLLKEEKKEELEIL 432
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024431993 471 RLVNQRLLEVQSQVEELQKSLQDQDSKAEDAISVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRCNNSSLKIEE 547
Cdd:pfam02463 433 EEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGL 509
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
223-388 |
1.01e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.86 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 223 AAKDDYRIRCEELEKEIAELRQQTEELT-ALAEEAQSLKDEIDVLRHSSDKVAKLESQVESYKK--KLEDLGDL----RR 295
Cdd:PHA02562 213 ENIARKQNKYDELVEEAKTIKAEIEELTdELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKviKMYEKGGVcptcTQ 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 296 QVKLLEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRT 375
Cdd:PHA02562 293 QISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQA 372
|
170
....*....|...
gi 2024431993 376 ERDSLKETIEELR 388
Cdd:PHA02562 373 EFVDNAEELAKLQ 385
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
310-552 |
1.02e-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: 48.91 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 310 NTVSLEEELRKANAarsQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERDSLKETIEELRC 389
Cdd:TIGR02169 668 FSRSEPAELQRLRE---RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 390 ------------------VQAQEGQLTTT-GLMPLGRQEPSDSLAAEIVtPEIKEKL-----------IRLQHENKIL-- 437
Cdd:TIGR02169 745 dlssleqeienvkselkeLEARIEELEEDlHKLEEALNDLEARLSHSRI-PEIQAELskleeevsrieARLREIEQKLnr 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 438 KLNQEGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQDSKAEDaisvlLKKKLEEHLEKL 517
Cdd:TIGR02169 824 LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD-----LKKERDELEAQL 898
|
250 260 270
....*....|....*....|....*....|....*
gi 2024431993 518 HEANNELQKKRAIIEDLEPRCNNSSLKIEELQEAL 552
Cdd:TIGR02169 899 RELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
285-625 |
1.10e-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: 48.91 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 285 KKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEElrkanaaRSQLETYKRQAVELQN-RLSEESKKADKLDYECKRLKEKV 363
Cdd:TIGR02169 174 KALEELEEVEENIERLDLIIDEKRQQLERLRRE-------REKAERYQALLKEKREyEGYELLKEKEALERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 364 DSLQKEKDRLRTERDSLKETIEELRCVQAQEgqltTTGLMPLGRQEpsdSLAAEIVTPEIKEKLIRLQHENKILKLNQEG 443
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEEL----NKKIKDLGEEE---QLRVKEKIGELEAEIASLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 444 SDnEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDqdskaedaisvlLKKKLEEHLEKLHEANNE 523
Cdd:TIGR02169 320 AE-ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELED------------LRAELEEVDKEFAETRDE 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 524 LQKKRAIIEDLEPRCNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNqgaapEIQALKNQLQERD 603
Cdd:TIGR02169 387 LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL-----EIKKQEWKLEQLA 461
|
330 340
....*....|....*....|..
gi 2024431993 604 RMFHSLEKEYEKTKNQREMEEK 625
Cdd:TIGR02169 462 ADLSKYEQELYDLKEEYDRVEK 483
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
224-388 |
1.28e-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: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 224 AKDDYRIRCEELEKEIAElRQQTEELTALAEEAQSLKDEIDVLRHssDKVAKLESQVESYKKKLE-DLGDLRRQVKLLEE 302
Cdd:COG2433 344 AYDAYKNKFERVEKKVPP-DVDRDEVKARVIRGLSIEEALEELIE--KELPEEEPEAEREKEHEErELTEEEEEIRRLEE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 303 KntmymqntvslEEELRKANAA-RSQLETYKRQAVELQNRLSEESKKAdkldYECKRLKEKVDSLQKEKDRLRTERDSLK 381
Cdd:COG2433 421 Q-----------VERLEAEVEElEAELEEKDERIERLERELSEARSEE----RREIRKDREISRLDREIERLERELEEER 485
|
....*..
gi 2024431993 382 ETIEELR 388
Cdd:COG2433 486 ERIEELK 492
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
296-500 |
1.37e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 296 QVKLLEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRT 375
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 376 ERDSLKETIEELRCVQAQEGQLTTTGLMpLGRQEPSDSLAA----EIVTPEIKEKLIRLQHENKILKLNQEGSDNEKiAL 451
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALL-LSPEDFLDAVRRlqylKYLAPARREQAEELRADLAELAALRAELEAER-AE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2024431993 452 LQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQDSKAED 500
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
220-648 |
2.23e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 220 RLEAAKDDYRIRCEELEKEIAELRQQTEELTALAEEAQSLKDEIDVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQVKL 299
Cdd:PTZ00121 1225 KAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKA 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 300 LEEKNTmymqntvslEEELRKANAARSQLETYKRQAVELQNRlSEESKKAD--------KLDYECKRLKEKVDSLQKEKD 371
Cdd:PTZ00121 1305 DEAKKK---------AEEAKKADEAKKKAEEAKKKADAAKKK-AEEAKKAAeaakaeaeAAADEAEAAEEKAEAAEKKKE 1374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 372 RLRTERDSLKETIEELRcvQAQEGQLTTTGLMPLGrQEPSDSLAAEIVTPEIKEKLIRLQHENKILKLNQEGSDNEKIAL 451
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEKK--KADEAKKKAEEDKKKA-DELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKK 1451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 452 LQSLLDDA-NLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQDSKAEDAISVLLKKKLEEHLEKLHEAN--NELQKKR 528
Cdd:PTZ00121 1452 KAEEAKKAeEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKkaDEAKKAE 1531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 529 AIIEDLEPRCNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQLQERDRMFHS 608
Cdd:PTZ00121 1532 EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEE 1611
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2024431993 609 LEKEYEKTKN----QREMEEKFIVSAWYNMGMTLHKKAAEDRLA 648
Cdd:PTZ00121 1612 AKKAEEAKIKaeelKKAEEEKKKVEQLKKKEAEEKKKAEELKKA 1655
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
315-630 |
2.70e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.74 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 315 EEELRKANAARSQLETYKRQAVEL---QNRLSEESKKADKLdyecKRLKEKVDSLQK-----EKDRLRTERDSLKETIEE 386
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELerqLKSLERQAEKAERY----KELKAELRELELallvlRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 387 LrcvqaqegqltttglmplgrQEPSDSLAAEIVTPEIKEKLIRLQHenkilklnqeGSDNEKIALLQSLLDDANLRKNEL 466
Cdd:TIGR02168 251 A--------------------EEELEELTAELQELEEKLEELRLEV----------SELEEEIEELQKELYALANEISRL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 467 ETENRLVNQRLLEVQSQVEELQKSLQDqdskaedaisvlLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRCNNSSLKIE 546
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEE------------LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 547 ELQEALRKKEEEMKQMEERYKKYLEkaksvirtldpkqnqgaapEIQALKNQLQERDRMFHSLEKEYEKTKNQREMEEKF 626
Cdd:TIGR02168 369 ELESRLEELEEQLETLRSKVAQLEL-------------------QIASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429
|
....
gi 2024431993 627 IVSA 630
Cdd:TIGR02168 430 LEEA 433
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
324-603 |
2.81e-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: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 324 ARSQLETYKRQAVELQNRLSEeskkadkldyeckrLKEKVDSLQKEKDRLRTERDSLkETIEELRcvqaqegqltttglm 403
Cdd:COG4913 608 NRAKLAALEAELAELEEELAE--------------AEERLEALEAELDALQERREAL-QRLAEYS--------------- 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 404 plgrqepsdslAAEIVTPEIKEKLIRLQHEnkilkLNQEGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQ 483
Cdd:COG4913 658 -----------WDEIDVASAEREIAELEAE-----LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE 721
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 484 V---EELQKSLQDQDSKAEDAISVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEprcnNSSLKIEELQEALRKKEeemk 560
Cdd:COG4913 722 LeqaEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERID----ALRARLNRAEEELERAM---- 793
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2024431993 561 qmeeryKKYLEKAKSVIRTLDPkqNQGAAPEIQALKNQLQERD 603
Cdd:COG4913 794 ------RAFNREWPAETADLDA--DLESLPEYLALLDRLEEDG 828
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
104-628 |
3.26e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 104 ESVQHMVMAAIQELMSKESPVSVGNDAYVDLDRQLKKTTEELNEALSTKEEIAQRCHELDMQVAALQEEKSSLLAENQil 183
Cdd:TIGR02168 284 EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE-- 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 184 merlnqsdsiedpnspagRRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEIAELRQQTEELTALAEEAQSLKDEI 263
Cdd:TIGR02168 362 ------------------ELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 264 DVLRHSSDKVAKLESQVESYKKK------LEDLGDLRRQVKLLEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQAVE 337
Cdd:TIGR02168 424 EELLKKLEEAELKELQAELEELEeeleelQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 338 LQNRLSEESKKADKLDYECKRLKEK-----------------------VDSLQKEKDRLRTERDSLKETIEELRCVQAQE 394
Cdd:TIGR02168 504 FSEGVKALLKNQSGLSGILGVLSELisvdegyeaaieaalggrlqavvVENLNAAKKAIAFLKQNELGRVTFLPLDSIKG 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 395 GQLTTTGLMPLGRQEPSDSLAAEIVTPEIK----------------------EKLIRLQHENKILKLNQE---------G 443
Cdd:TIGR02168 584 TEIQGNDREILKNIEGFLGVAKDLVKFDPKlrkalsyllggvlvvddldnalELAKKLRPGYRIVTLDGDlvrpggvitG 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 444 SDNEKIALLQSllddanlRKNELETenrlVNQRLLEVQSQVEELQKSLQDQDSKAEDAISVL--LKKKLEEHLEKLHEAN 521
Cdd:TIGR02168 664 GSAKTNSSILE-------RRREIEE----LEEKIEELEEKIAELEKALAELRKELEELEEELeqLRKELEELSRQISALR 732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 522 NELQKKRAIIEDLEPRCNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPE--IQALKNQL 599
Cdd:TIGR02168 733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALReaLDELRAEL 812
|
570 580
....*....|....*....|....*....
gi 2024431993 600 QERDRMFHSLEKEYEKTKNQREMEEKFIV 628
Cdd:TIGR02168 813 TLLNEEAANLRERLESLERRIAATERRLE 841
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
222-625 |
3.65e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 222 EAAKDDYRIRCEELEKEiAELRQQTEELTALAEEAQSLKDEIDVLRHSSDKVAKL-ESQVESYKKKLEDLGDLRRQVKLL 300
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKK-AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAaKAEAEAAADEAEAAEEKAEAAEKK 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 301 EEKNTMYMQNTVSLEEELRKANAARSQLETYKRQAVELQNRlSEESKKADKLDYECKRlKEKVDSLQKEKDRLRtERDSL 380
Cdd:PTZ00121 1373 KEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKA-AAAKKKADEAKKKAEE-KKKADEAKKKAEEAK-KADEA 1449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 381 KETIEELRCVQAQEGQLTTTGLMPLGRQEPSDSLAAEIV---TPEIKEKLIRLQHENKILKLNQEGSDNEKIALLQSLLD 457
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAkkkAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK 1529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 458 DANLRKNEletenrlvNQRLLEVQSQVEELQKSlqDQDSKAEDAISVLLKKKLEEHLEKLHEANNELQK--KRAIIEDLE 535
Cdd:PTZ00121 1530 AEEAKKAD--------EAKKAEEKKKADELKKA--EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaeEARIEEVMK 1599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 536 PRCNNSSLKIEELQEALRK--------KEEEMKQMEERYKKYLEKAKSVIRTLDpKQNQGAAPEIQALKNQLQERDRMFH 607
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAkikaeelkKAEEEKKKVEQLKKKEAEEKKKAEELK-KAEEENKIKAAEEAKKAEEDKKKAE 1678
|
410
....*....|....*...
gi 2024431993 608 SLEKEYEKTKNQREMEEK 625
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKK 1696
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
233-525 |
3.71e-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: 47.04 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 233 EELEKEIAELRQQTEELTALAEEAQSLKDE-------IDVLRHSSD----KVAKLESQVESYKKKLEdlGDLRRQVKLLE 301
Cdd:pfam15921 377 DQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDdrnmEVQRLEALLKAMKSECQ--GQMERQMAAIQ 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 302 EKN------TMYMQNTVSLEEELRKA----NAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKD 371
Cdd:pfam15921 455 GKNeslekvSSLTAQLESTKEMLRKVveelTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQ 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 372 RLRTERDSLKETIEELRCVQAQEGQLTTT---------GLMPL----GRQEPSDSLAAEIVTPEIKEKLIRLQhENKILK 438
Cdd:pfam15921 535 HLKNEGDHLRNVQTECEALKLQMAEKDKVieilrqqieNMTQLvgqhGRTAGAMQVEKAQLEKEINDRRLELQ-EFKILK 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 439 LNQEGsdneKIALLQSLLDDANLRKNELETEN----RLVNQRLLEVQSQVEELQKSLQDQDSKAEDaiSVLLKKKLEEHL 514
Cdd:pfam15921 614 DKKDA----KIRELEARVSDLELEKVKLVNAGserlRAVKDIKQERDQLLNEVKTSRNELNSLSED--YEVLKRNFRNKS 687
|
330
....*....|.
gi 2024431993 515 EKLHEANNELQ 525
Cdd:pfam15921 688 EEMETTTNKLK 698
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
220-627 |
9.07e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 9.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 220 RLEAAKDDYRIRCEELEKEIAELRQQTEELTALAEEAQSLKDEIDVLrhsSDKVAKLESQVESYKKKLEDLGDLRRQVKL 299
Cdd:PRK03918 166 NLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEI---SSELPELREELEKLEKEVKELEELKEEIEE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 300 LEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQAVELQNRLSEESKKAD---KLDYECKRLKEKVDSLQKEKDRLRTE 376
Cdd:PRK03918 243 LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEeyiKLSEFYEEYLDELREIEKRLSRLEEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 377 RDSLKETIEELRCVQAQEGQLTTTglmplgRQEPSDSLAAEIVTPEIKEKLIRLQHENKILKLNQEGSDNEKIAllqSLL 456
Cdd:PRK03918 323 INGIEERIKELEEKEERLEELKKK------LKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLE---KEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 457 DDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQDsKAEDAISVLLKKKLEEHLEKLheanneLQKKRAIIEDLEP 536
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK-KAKGKCPVCGRELTEEHRKEL------LEEYTAELKRIEK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 537 RCNNSSLKIEELQEALRkkeeemkqmeeRYKKYLEKAKSVIRTLDpkqnqgAAPEIQALKNQLQErdrmfHSLEKEYEKT 616
Cdd:PRK03918 467 ELKEIEEKERKLRKELR-----------ELEKVLKKESELIKLKE------LAEQLKELEEKLKK-----YNLEELEKKA 524
|
410
....*....|.
gi 2024431993 617 KNQREMEEKFI 627
Cdd:PRK03918 525 EEYEKLKEKLI 535
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
220-624 |
9.38e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 9.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 220 RLEAAKDDYRIRCEELEKEIAELRQQTEELtalaeeaQSLKDEIDVLRhssDKVAKLESQVESYKkklEDLGDLRRQVKL 299
Cdd:PRK02224 224 RYEEQREQARETRDEADEVLEEHEERREEL-------ETLEAEIEDLR---ETIAETEREREELA---EEVRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 300 LEEKNTmYMQNTVSLEEELRKANAARsqLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERDS 379
Cdd:PRK02224 291 LEEERD-DLLAEAGLDDADAEAVEAR--REELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 380 L--------------KETIEELRC-VQAQEGQLTTTGLMPLGRQEPSDSLAAEI--VTPEIKEKLIRLQHENKILKLNQE 442
Cdd:PRK02224 368 LeseleeareavedrREEIEELEEeIEELRERFGDAPVDLGNAEDFLEELREERdeLREREAELEATLRTARERVEEAEA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 443 ----------GSDNEKIALLQSlLDDANLRKNELETEnrlvnqrLLEVQSQVEELQKSLQdqdsKAEDAisVLLKKKLEE 512
Cdd:PRK02224 448 lleagkcpecGQPVEGSPHVET-IEEDRERVEELEAE-------LEDLEEEVEEVEERLE----RAEDL--VEAEDRIER 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 513 HLEKLHEANNELQKKRAIIEDLEPRCNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDpkQNQGAAPEI 592
Cdd:PRK02224 514 LEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLA--ELKERIESL 591
|
410 420 430
....*....|....*....|....*....|..
gi 2024431993 593 QALKNQLQERDRMFHSLEKEYEKTKNQREMEE 624
Cdd:PRK02224 592 ERIRTLLAAIADAEDEIERLREKREALAELND 623
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
143-617 |
1.20e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.28 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 143 EELNEALSTKEEIaqrcHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQEETFRLE 222
Cdd:PRK01156 239 SALNELSSLEDMK----NRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQIL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 223 AAKDDYRIRCEELEKEIAELRQQTEELTALAEEAQSLKDEIDVLRHSSDKVAKLESQVESYKKKLEDlgdlrrqvkllEE 302
Cdd:PRK01156 315 SNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEE-----------YS 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 303 KNTMYMQNTVSLEEELRKANAArsqletykrqavELQNRLSEESKKADKLDyeckrlkEKVDSLQKEKDRLRTERDSLKE 382
Cdd:PRK01156 384 KNIERMSAFISEILKIQEIDPD------------AIKKELNEINVKLQDIS-------SKVSSLNQRIRALRENLDELSR 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 383 TIEELrcvqaqEGQltttGLMPLGRQEPSDSLAAEIVTpEIKEKLIRLqhENKILKLNQEGSD-NEKIALLQSLLDDANL 461
Cdd:PRK01156 445 NMEML------NGQ----SVCPVCGTTLGEEKSNHIIN-HYNEKKSRL--EEKIREIEIEVKDiDEKIVDLKKRKEYLES 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 462 RK-NELETENRLVNQRLLEVQsQVEELQKSLQDQDSKAEDAISVLLKKKLEEHLEKLHEANNELQKKRAI-IEDLEPRCN 539
Cdd:PRK01156 512 EEiNKSINEYNKIESARADLE-DIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVISLIdIETNRSRSN 590
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024431993 540 NSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNqgaapEIQALKNQLQERDRMFHSLEKEYEKTK 617
Cdd:PRK01156 591 EIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYN-----EIQENKILIEKLRGKIDNYKKQIAEID 663
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
220-565 |
1.95e-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: 44.96 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 220 RLEAAKDDYRIRCEELEKEIAELRQQTEELTALAEEAQSLKDEIDVLR---HSSDKVAKLESQVESYKKKLEDLGDLR-- 294
Cdd:pfam02463 146 IIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEelkLQELKLKEQAKKALEYYQLKEKLELEEey 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 295 ----RQVKLLEEKNTMYMQNTVSLEEELRKANaARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEK 370
Cdd:pfam02463 226 llylDYLKLNEERIDLLQELLRDEQEEIESSK-QEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 371 DRLRTERDSLKETIEELRCVQAQEGQLtttglmplgrQEPSDSLAAEIVTPEIKEKLIRLQHENKILKLNQEGSDNEKIA 450
Cdd:pfam02463 305 LERRKVDDEEKLKESEKEKKKAEKELK----------KEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEE 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 451 LLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQDSKAEDAISVLLKKKLEEHLEKLHEANNELQKKRAI 530
Cdd:pfam02463 375 LLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELE 454
|
330 340 350
....*....|....*....|....*....|....*
gi 2024431993 531 IEDLEPRCNNSSLKIEELQEALRKKEEEMKQMEER 565
Cdd:pfam02463 455 KQELKLLKDELELKKSEDLLKETQLVKLQEQLELL 489
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
243-576 |
2.64e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 243 RQQTEELTALAEEAQSLKDEIDVLRhssDKVAKLESQVESYKKKLED----LGDLRRQVKLLEEKNTMYMQNTVSLEEEL 318
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQ---SELRRIENRLDELSQELSDasrkIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 319 ----RKANAARSQLETYKRQAVELQNRLSEESKKADKLdyECKRLKEKVDSLQKEKDRLRTERDSLKETIEELrcvqaqE 394
Cdd:TIGR02169 747 ssleQEIENVKSELKELEARIEELEEDLHKLEEALNDL--EARLSHSRIPEIQAELSKLEEEVSRIEARLREI------E 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 395 GQLTTTGLMPLGRQEPSDSLAAEIVTPEIKEKLIRLQHENkilklnqegsDNEKIALLQSLLDDANLRKNELETENRLVN 474
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN----------LNGKKEELEEELEELEAALRDLESRLGDLK 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 475 QRLLEVQSQVEELQKSLQDQDSKAEDAISVL--LKKKLEEHLEKLHEANN--------------------ELQKKRAIIE 532
Cdd:TIGR02169 889 KERDELEAQLRELERKIEELEAQIEKKRKRLseLKAKLEALEEELSEIEDpkgedeeipeeelsledvqaELQRVEEEIR 968
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2024431993 533 DLEPRCN-------NSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSV 576
Cdd:TIGR02169 969 ALEPVNMlaiqeyeEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
220-491 |
3.87e-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: 44.06 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 220 RLEAAKDDYRIRCEELEKEIAELRQQTE-ELTALAEEAQSLKDEIDVLrhSSDKVAKLESQVESYKKKLEDLGDLRRQVK 298
Cdd:pfam12128 280 ERQETSAELNQLLRTLDDQWKEKRDELNgELSAADAAVAKDRSELEAL--EDQHGAFLDADIETAAADQEQLPSWQSELE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 299 LLEEKNTMYMQNTVSLEEELRKanaarsqletyKRQAVELQNrlseeskkADKLDyeckRLKEKVDSLQKEKDRLRT-ER 377
Cdd:pfam12128 358 NLEERLKALTGKHQDVTAKYNR-----------RRSKIKEQN--------NRDIA----GIKDKLAKIREARDRQLAvAE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 378 DSLKETIEELRcvQAQEGQLTTTGLMPLGRQEPSDSLAAEIVTPEIKEKLIrLQHENKILKLN----QEGSDNEKIALLQ 453
Cdd:pfam12128 415 DDLQALESELR--EQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELL-LQLENFDERIErareEQEAANAEVERLQ 491
|
250 260 270
....*....|....*....|....*....|....*...
gi 2024431993 454 SLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSL 491
Cdd:pfam12128 492 SELRQARKRRDQASEALRQASRRLEERQSALDELELQL 529
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
240-594 |
4.40e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 240 AELRQQTEELTALAEEAQSLKDEIDVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTV-----SL 314
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIerqlaSL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 315 EEELRKANAARSQLEtykRQAVELQNRLSEESKKADKL-DYECKRLKEKVDSLQKEKDRLrteRDSLKETIEELRCVQAQ 393
Cdd:TIGR02169 250 EEELEKLTEEISELE---KRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASL---ERSIAEKERELEDAEER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 394 EGQLtttglmplgrQEPSDSLAAEIvtPEIKEKLIRLQHENKILKlnqegsdnEKIALLQSLLDDANLRKNELETENRLV 473
Cdd:TIGR02169 324 LAKL----------EAEIDKLLAEI--EELEREIEEERKRRDKLT--------EEYAELKEELEDLRAELEEVDKEFAET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 474 NQRLLEVQSQVEELQKSLqdQDSKAEDAISVLLKKKLEEHLEklhEANNELQKKRAIIEDLEPRCNNSSLKIEELQEALR 553
Cdd:TIGR02169 384 RDELKDYREKLEKLKREI--NELKRELDRLQEELQRLSEELA---DLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2024431993 554 KKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQA 594
Cdd:TIGR02169 459 QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQA 499
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
129-671 |
4.62e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.57 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 129 DAYVDLDRQLKKTTEELNEALSTKEEIAQRCHELDMQVAAL-----QEEKSSLLAENQilMERLNQSDSIEDPNSPAGRR 203
Cdd:pfam15921 342 DKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLladlhKREKELSLEKEQ--NKRLWDRDTGNSITIDHLRR 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 204 HLQLQTQLEQlqeetfRLEAAKDDYRIRCE-ELEKEIAELRQQTEELTALAEEAQSLKDEIDVLRHSSDKVAKLESQVES 282
Cdd:pfam15921 420 ELDDRNMEVQ------RLEALLKAMKSECQgQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLES 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 283 YKKKLEDL-GDLRRQVKLLEEKNTM-----------------------YMQNTVSLEEELRKANAARSQLETYKRQAVEL 338
Cdd:pfam15921 494 SERTVSDLtASLQEKERAIEATNAEitklrsrvdlklqelqhlknegdHLRNVQTECEALKLQMAEKDKVIEILRQQIEN 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 339 QNRL-SEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERDSLKETIEELRcVQAQEGQLTTTGLMPLGrqepSDSLAAe 417
Cdd:pfam15921 574 MTQLvGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELE-ARVSDLELEKVKLVNAG----SERLRA- 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 418 ivTPEIKEKLIRLQHENKILKlNQEGSDNEKIALLQSLLDDanlRKNELETENRLVNQRLLEVQSQVEELQKSLQDQDSK 497
Cdd:pfam15921 648 --VKDIKQERDQLLNEVKTSR-NELNSLSEDYEVLKRNFRN---KSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGS 721
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 498 AEDAISVLLkkKLEEHLEKLHEANNELQKKRAIIEDLEPRCNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVI 577
Cdd:pfam15921 722 DGHAMKVAM--GMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQE 799
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 578 RTLDPK-QNQGAAPEIQALknQLQERDRMFHSLEKEYEKTKNQREMEEKFIVSAWY----NMGMTLHKKAAEDR----LA 648
Cdd:pfam15921 800 RRLKEKvANMEVALDKASL--QFAECQDIIQRQEQESVRLKLQHTLDVKELQGPGYtsnsSMKPRLLQPASFTRthsnVP 877
|
570 580
....*....|....*....|...
gi 2024431993 649 STGSGQSFLARQRQATSTRRSYP 671
Cdd:pfam15921 878 SSQSTASFLSHHSRKTNALKEDP 900
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
258-537 |
5.14e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.38 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 258 SLKDEID-VLR--HSSDKVaklesQVESYKKKLEDLgdlrrQVKLLEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQ 334
Cdd:PRK05771 13 TLKSYKDeVLEalHELGVV-----HIEDLKEELSNE-----RLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 335 avELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERDSLK--ETIE-ELRCVQAQEGQLTTTGLMPLGRQEPS 411
Cdd:PRK05771 83 --SLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwGNFDlDLSLLLGFKYVSVFVGTVPEDKLEEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 412 DSLAAEIVTPEIKEKlirlqHENKILKLNQEGSDNEKIAllqSLLDDANLRKNELETENRL------VNQRLLEVQSQVE 485
Cdd:PRK05771 161 KLESDVENVEYISTD-----KGYVYVVVVVLKELSDEVE---EELKKLGFERLELEEEGTPselireIKEELEEIEKERE 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024431993 486 ELQKSLQDQDSKAEDAISVL------LKKKLE--------------------EHLEKLHEANNELQKKRAIIEDLEPR 537
Cdd:PRK05771 233 SLLEELKELAKKYLEELLALyeyleiELERAEalskflktdktfaiegwvpeDRVKKLKELIDKATGGSAYVEFVEPD 310
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
234-577 |
5.15e-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: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 234 ELEKEIAELRQQTEELTALAEEAQSLKDEIDVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQVKLLEEKNtmymqNTVS 313
Cdd:pfam02463 663 EVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDK-----INEE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 314 LEEELRKANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERDSLKETIEELRCVQAQ 393
Cdd:pfam02463 738 LKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELL 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 394 EGQLTTTGLMPLGRQEPSDSLAAEIVTPEIKEKLIRLQHENKILKLNQEGSDNEKIALLQSLLDDANLRKNELETENRLV 473
Cdd:pfam02463 818 EEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 474 NQRLLEVQSQVEELQKSLQDQDSKAEDAISVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRCNNSSLKIEELQEALR 553
Cdd:pfam02463 898 EKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNL 977
|
330 340
....*....|....*....|....
gi 2024431993 554 KKEEEMKQMEERYKKYLEKAKSVI 577
Cdd:pfam02463 978 MAIEEFEEKEERYNKDELEKERLE 1001
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
128-385 |
5.97e-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: 5.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 128 NDAYVDLDRQLKKTTEELNEALSTKEEIAQrchELDMQVAALQEEKSSLLAENQILM-ERLNQSDSIEDPNSPAGRRHLQ 206
Cdd:TIGR04523 379 NQSYKQEIKNLESQINDLESKIQNQEKLNQ---QKDEQIKKLQQEKELLEKEIERLKeTIIKNNSEIKDLTNQDSVKELI 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 207 LQTQLEQLQEETFRLEAAKDDYRIRCEELEKEIAELRQQTEELTALAEEAQSLKDEIDVLRHSSDKVAKLESQVESYKKK 286
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 287 LED-LGDLRRQVK---------LLEEKNTMYMQNTVSLEEELRKANAARSQLET----YKRQAVELQNRLSEESKKADKL 352
Cdd:TIGR04523 536 KESkISDLEDELNkddfelkkeNLEKEIDEKNKEIEELKQTQKSLKKKQEEKQElidqKEKEKKDLIKEIEEKEKKISSL 615
|
250 260 270
....*....|....*....|....*....|...
gi 2024431993 353 DYECKRLKEKVDSLQKEKDRLRTERDSLKETIE 385
Cdd:TIGR04523 616 EKELEKAKKENEKLSSIIKNIKSKKNKLKQEVK 648
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
114-385 |
6.19e-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: 43.19 E-value: 6.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 114 IQELMSKESPVSVGNDAYVDLDRQLKKTTEELNEALSTKE-----------EIAQRCHELDMQVAALQEEKSSLLAENQI 182
Cdd:pfam05557 57 IRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKEsqladarevisCLKNELSELRRQIQRAELELQSTNSELEE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 183 LMERLNQSDS----IEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRI---------RCEELEKEIAELRQQTEEL 249
Cdd:pfam05557 137 LQERLDLLKAkaseAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIvknskselaRIPELEKELERLREHNKHL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 250 TA-------LAEEAQSLKDEIDVLRHSSDKVA-------KLESQVESYKKKLEDLG-------DLRRQVKLLEEKNTMYM 308
Cdd:pfam05557 217 NEnienkllLKEEVEDLKRKLEREEKYREEAAtlelekeKLEQELQSWVKLAQDTGlnlrspeDLSRRIEQLQQREIVLK 296
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024431993 309 QNTVSLEEELRKANAARSQLETYKRQAVelqnrlseesKKADKLDYECKRLKEKVDSLQKEKDRLRTERDSLKETIE 385
Cdd:pfam05557 297 EENSSLTSSARQLEKARRELEQELAQYL----------KKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILE 363
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
261-628 |
6.41e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 261 DEIDVLRHSSDKVAKLESQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQAVELQN 340
Cdd:PRK03918 138 DAILESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELP 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 341 RLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERDSLKETIEELRcVQAQEGQLTTTGLMPLGRQEPSDSLAAEIVT 420
Cdd:PRK03918 218 ELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE-ERIEELKKEIEELEEKVKELKELKEKAEEYI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 421 PEIKEKLIRLQHENKILKLnqEGSDNEKIALLQSLLDDA---NLRKNELETENRLVNQRLLEVQSQVEELQ--KSLQDQD 495
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKR--LSRLEEEINGIEERIKELeekEERLEELKKKLKELEKRLEELEERHELYEeaKAKKEEL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 496 SKAEDAISVLLKKKLEEHLEKLHEANNELQKKraiIEDLEPRCNNSSLKIEELQEALRKkeeemkqmeerykkyLEKAKS 575
Cdd:PRK03918 375 ERLKKRLTGLTPEKLEKELEELEKAKEEIEEE---ISKITARIGELKKEIKELKKAIEE---------------LKKAKG 436
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024431993 576 VI----RTLDPKQNQGA----APEIQALKNQLQERDRMFHSLEKEYEKTKNQREMEEKFIV 628
Cdd:PRK03918 437 KCpvcgRELTEEHRKELleeyTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIK 497
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
133-387 |
7.23e-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: 43.12 E-value: 7.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 133 DLDRQLKKTTEELNEALSTKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQ-----------SDSIEDPNSPAG 201
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaanlrerLESLERRIAATE 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 202 RRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEIAELrqqTEELTALAEEAQSLKDEIDVLrhsSDKVAKLESQVE 281
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL---LNERASLEEALALLRSELEEL---SEELRELESKRS 911
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 282 SYKKKLEDLGDLRRQVKLLEEKNTMYMQNT---------VSLEEELRKANAARSQLETYKRQAVELQNRLSE-------- 344
Cdd:TIGR02168 912 ELRRELEELREKLAQLELRLEGLEVRIDNLqerlseeysLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaa 991
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2024431993 345 -EskkadkldyECKRLKEKVDSLQKEKDRLRTERDSLKETIEEL 387
Cdd:TIGR02168 992 iE---------EYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
320-619 |
9.98e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 9.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 320 KANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERDSLKETIEELRCVQA------- 392
Cdd:TIGR04523 69 KINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDkflteik 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 393 ---QEGQLTTTGLMPLGRQEPS-----DSLAAEIVTPEIKEKLIRLQHENKILKLNQEGSDNEKIALLQSLLDDANLRKN 464
Cdd:TIGR04523 149 kkeKELEKLNNKYNDLKKQKEElenelNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNN 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 465 ELETENRLVNQRLLEVQSQVEELQKSLQDQDSKAEDAISVLLKK--KLEEHLEKLHEANNELQKKRAIIEDLEPRCNNSS 542
Cdd:TIGR04523 229 QLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKqkELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDW 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 543 LK-----IEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNqgaapEIQALKNQLQERDRMFHSLEKEYEKTK 617
Cdd:TIGR04523 309 NKelkseLKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES-----ENSEKQRELEEKQNEIEKLKKENQSYK 383
|
..
gi 2024431993 618 NQ 619
Cdd:TIGR04523 384 QE 385
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
226-336 |
1.13e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 226 DDYRIRCEELEKEIAELRQQTEEltALAEEAQSLKDEIDVLRhssDKVAKLESQVESYKKKLEDLGDLRRQvklLEEKNt 305
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEQDE--ASFERLAELRDELAELE---EELEALKARWEAEKELIEEIQELKEE---LEQRY- 484
|
90 100 110
....*....|....*....|....*....|.
gi 2024431993 306 mymQNTVSLEEELRKANAARSQLETYKRQAV 336
Cdd:COG0542 485 ---GKIPELEKELAELEEELAELAPLLREEV 512
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
129-630 |
1.18e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 129 DAYVDLDRQLKKTTEELnEALSTKEEIAQRCHELDMQVAALQEEKSSLLAENqilmerlnqsdsiedpnspAGRRHLQLQ 208
Cdd:COG4913 235 DDLERAHEALEDAREQI-ELLEPIRELAERYAAARERLAELEYLRAALRLWF-------------------AQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 209 TQLEQLQEETFRLEAAKDDYRIRCEELEKEIAELRQQ-----TEELTALAEEAQSLKDEIDVLRHSSDKVAKLESQVE-S 282
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQirgngGDRLEQLEREIERLERELEERERRRARLEALLAALGlP 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 283 YKKKLEDLGDLRRQVK-LLEEKNTMYMQntvsLEEELRKANAARSQLetyKRQAVELQNRLSEESKKADKLDYE------ 355
Cdd:COG4913 375 LPASAEEFAALRAEAAaLLEALEEELEA----LEEALAEAEAALRDL---RRELRELEAEIASLERRKSNIPARllalrd 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 356 --CKRLKEKVDSLQ--------KEKDR---------LRTERDSL----------KETIEELRcvqaQEGQLTTTGLMPLG 406
Cdd:COG4913 448 alAEALGLDEAELPfvgelievRPEEErwrgaiervLGGFALTLlvppehyaaaLRWVNRLH----LRGRLVYERVRTGL 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 407 RQE-----PSDSLAAEI------------------------------------VTPE--IKEKLIRLQH--ENKILKLNQ 441
Cdd:COG4913 524 PDPerprlDPDSLAGKLdfkphpfrawleaelgrrfdyvcvdspeelrrhpraITRAgqVKGNGTRHEKddRRRIRSRYV 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 442 EGSDN-EKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQDSK-----AEDAISvllkkKLEEHLE 515
Cdd:COG4913 604 LGFDNrAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEidvasAEREIA-----ELEAELE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 516 KLHEANNELQKKRAIIEDLEprcnnssLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQAL 595
Cdd:COG4913 679 RLDASSDDLAALEEQLEELE-------AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL 751
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 2024431993 596 KNQLQE------RDRMFHSLEKEYEKTKNQREMEEKFIVSA 630
Cdd:COG4913 752 EERFAAalgdavERELRENLEERIDALRARLNRAEEELERA 792
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
320-536 |
1.26e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 320 KANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERDSLKETIEELRCV-------QA 392
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElgeraraLY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 393 QEGQLTTTGLMPLGRQEPSDSLAaeivtpeikekliRLQHENKILKlnqegSDNEKIALLQSLLDDANLRKNELETENRL 472
Cdd:COG3883 97 RSGGSVSYLDVLLGSESFSDFLD-------------RLSALSKIAD-----ADADLLEELKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024431993 473 VNQRLLEVQSQVEELQKSLQDQDSKAEDaisvlLKKKLEEHLEKLHEANNELQKKRAIIEDLEP 536
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQ-----LSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
221-388 |
1.81e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 221 LEAAKDDYRIRCEELEKEIAELRQQTeELTALAEEAQSLKDEIDVLRhssDKVAKLESQVESYKKKLEdlgDLRRQVKLL 300
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKN-GLVDLSEEAKLLLQQLSELE---SQLAEARAELAEAEARLA---ALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 301 EEKNTMYMQNTV--SLEEELRKANAARSQLET-----------YKRQAVELQNRLSEESKKA-DKLDYECKRLKEKVDSL 366
Cdd:COG3206 253 PDALPELLQSPViqQLRAQLAELEAELAELSArytpnhpdviaLRAQIAALRAQLQQEAQRIlASLEAELEALQAREASL 332
|
170 180
....*....|....*....|..
gi 2024431993 367 QKEKDRLRTERDSLKETIEELR 388
Cdd:COG3206 333 QAQLAQLEARLAELPELEAELR 354
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
152-388 |
1.81e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.45 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 152 KEEIAQRCHELD-MQVAALQEEKSS-----LLAENQILMERLNQSDSIEDPNSpagrrhlqlQTQLEQLQEETFRLEAAK 225
Cdd:PRK05771 18 KDEVLEALHELGvVHIEDLKEELSNerlrkLRSLLTKLSEALDKLRSYLPKLN---------PLREEKKKVSVKSLEELI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 226 DDYRIRCEELEKEIAELrqqTEELTALAEEAQSLKDEIDVLrhssdkvaklesqvesykKKLEDLG-DLRRqvkLLEEKN 304
Cdd:PRK05771 89 KDVEEELEKIEKEIKEL---EEEISELENEIKELEQEIERL------------------EPWGNFDlDLSL---LLGFKY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 305 TMYMQNTVSLE-EELRKANAARSQLETYKR----------QAVELQNRLSEESKKAD--KLDY-ECKRLKEKVDSLQKEK 370
Cdd:PRK05771 145 VSVFVGTVPEDkLEELKLESDVENVEYISTdkgyvyvvvvVLKELSDEVEEELKKLGfeRLELeEEGTPSELIREIKEEL 224
|
250
....*....|....*...
gi 2024431993 371 DRLRTERDSLKETIEELR 388
Cdd:PRK05771 225 EEIEKERESLLEELKELA 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
213-388 |
1.95e-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: 40.90 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 213 QLQEETFRLEAAKDDYRIRCEELEKEIAELRQQ----TEELTALAEEAQSLKDEIDVLRHssdKVAKLESQVESYKKKLE 288
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRiaalARRIRALEQELAALEAELAELEK---EIAELRAELEAQKEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 289 DLgdLRRQVKLLEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQK 368
Cdd:COG4942 108 EL--LRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180
....*....|....*....|
gi 2024431993 369 EKDRLRTERDSLKETIEELR 388
Cdd:COG4942 186 ERAALEALKAERQKLLARLE 205
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
344-625 |
2.32e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.20 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 344 EESKKADKLDYECKRLKEKVDSLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTTGLMPLGRQEPSDSLAAEIVTpei 423
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA--- 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 424 kekliRLQHENKILklnqegsdNEKIALLQSLLDDANLRKNELETEnrlvnqrLLEVQSQVEELQKSLQDQDSKAEDais 503
Cdd:TIGR02168 751 -----QLSKELTEL--------EAEIEELEERLEEAEEELAEAEAE-------IEELEAQIEQLKEELKALREALDE--- 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 504 vlLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRcnnsslkIEELQEALRKKEEEmkqmeerykkyLEKAKSVIRTLDPK 583
Cdd:TIGR02168 808 --LRAELTLLNEEAANLRERLESLERRIAATERR-------LEDLEEQIEELSED-----------IESLAAEIEELEEL 867
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2024431993 584 QNQgAAPEIQALKNQLQERDRMFHSLEKEYEK-TKNQREMEEK 625
Cdd:TIGR02168 868 IEE-LESELEALLNERASLEEALALLRSELEElSEELRELESK 909
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
222-430 |
3.74e-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: 40.49 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 222 EAAKDDYRIRCEELEKEiaelrQQTEELTALAEEAQSLKDEIDvlRHSSDKVAKLESQVESYKKKLEDlgdlrRQVKLLE 301
Cdd:pfam17380 443 ERAREMERVRLEEQERQ-----QQVERLRQQEEERKRKKLELE--KEKRDRKRAEEQRRKILEKELEE-----RKQAMIE 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 302 EKNTMYMqntvsLEEELRKANAARSQletykrqavELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRT---ERD 378
Cdd:pfam17380 511 EERKRKL-----LEKEMEERQKAIYE---------EERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAmerERE 576
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2024431993 379 SLKETIEELRCVQAQEGQLTTTGLMPLGRQEPSdslaaEIVTPEIKEKLIRL 430
Cdd:pfam17380 577 MMRQIVESEKARAEYEATTPITTIKPIYRPRIS-----EYQPPDVESHMIRF 623
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
461-625 |
3.90e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.43 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 461 LRKNELETENRLVN-----QRLLEVQSQVEELQKSLQDQDSKAEDAISV----------LLKKKLEEHLEKLHEANNELQ 525
Cdd:TIGR02168 170 YKERRKETERKLERtrenlDRLEDILNELERQLKSLERQAEKAERYKELkaelrelelaLLVLRLEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 526 KKRAIIEDLEPRCNNSSLKIEELQEALRKKEEEMKQMEERY----------KKYLEKAKSVIRTLDPKQNQGAApEIQAL 595
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELyalaneisrlEQQKQILRERLANLERQLEELEA-QLEEL 328
|
170 180 190
....*....|....*....|....*....|
gi 2024431993 596 KNQLQERDRMFHSLEKEYEKTKNQREMEEK 625
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEA 358
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
135-371 |
4.80e-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: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 135 DRQLKKTTEELNEALSTKEEIAQRCHELDMQVAALQEEKSSLLAENQilmerlnqsdsiedpnspagrrhlqlqtqleql 214
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE--------------------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 215 qeetfRLEAAKDDYRIRCEELEKEIAELRQQTEELTALAEEAQSLKDEIDVLRHSS------DKVAKLESQVESYKKKLE 288
Cdd:COG3883 62 -----ALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVLLGSEsfsdflDRLSALSKIADADADLLE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 289 DLGDLRRQVKLLEEKntmymqntvsLEEELRKANAARSQLETYKRqavELQNRLSEESKKADKLDYECKRLKEKVDSLQK 368
Cdd:COG3883 137 ELKADKAELEAKKAE----------LEAKLAELEALKAELEAAKA---ELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
...
gi 2024431993 369 EKD 371
Cdd:COG3883 204 ELA 206
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
223-519 |
4.94e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.28 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 223 AAKDDYRIRCEELEKEIA----ELRQQTEELTALAEEAQSLKDEidvlRHSSDKVAKLESQVEsykKKLEDLGDLRrqvk 298
Cdd:PRK11281 73 DKIDRQKEETEQLKQQLAqapaKLRQAQAELEALKDDNDEETRE----TLSTLSLRQLESRLA---QTLDQLQNAQ---- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 299 lleekntmymqntvsleEELRKANaarSQLETYKRQAVELQNRLSEESKKADKLDYECKRLK-EKVDSLQKEKDRLRTER 377
Cdd:PRK11281 142 -----------------NDLAEYN---SQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKvGGKALRPSQRVLLQAEQ 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 378 DSLKETIEELRCVQAQEGQLTTTGlmplgrQEPSDSLAAEIVtpeikekliRLQHEnkilklnqegsdnekIALLQSLLD 457
Cdd:PRK11281 202 ALLNAQNDLQRKSLEGNTQLQDLL------QKQRDYLTARIQ---------RLEHQ---------------LQLLQEAIN 251
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024431993 458 DANLRKNEletenrlvnQRLLEVQSQvEELQKSLQDQDSKAEDAISVLLKKKLEEHLEKLHE 519
Cdd:PRK11281 252 SKRLTLSE---------KTVQEAQSQ-DEAARIQANPLVAQELEINLQLSQRLLKATEKLNT 303
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
233-627 |
4.98e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.00 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 233 EELEKEIAELRQQTEELTALAEEAQ-SLKDEIDVLRHSSDKVAKLESQVESYKKKLED----LGDLRRQVKLLEEKNTMY 307
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDkNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKnkdkINKLNSDLSKINSEIKND 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 308 MQNTVSLEEELRKAnaaRSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERDSLKETIEEL 387
Cdd:TIGR04523 116 KEQKNKLEVELNKL---EKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 388 RcvqAQEGQLTTTGLMPLGRQEPSDSLAAEIVtpEIKEKLIRLqhENKILKLNQEgsDNEKIALLQSLLDDANLRKNELE 467
Cdd:TIGR04523 193 K---NKLLKLELLLSNLKKKIQKNKSLESQIS--ELKKQNNQL--KDNIEKKQQE--INEKTTEISNTQTQLNQLKDEQN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 468 TENRLVNQRLLEVQsQVEELQKSLQDQDSKAEDAISVLLKKKLEEHLEKLHEannELQKKRAIIEDLEPRCNNSSLKIEE 547
Cdd:TIGR04523 264 KIKKQLSEKQKELE-QNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKS---ELKNQEKKLEEIQNQISQNNKIISQ 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 548 LQEA---LRKKEEEMKQMEERYKKYLEKAKSVIRTLDpKQNQGAAPEIQALKNQLQERDRMF------------------ 606
Cdd:TIGR04523 340 LNEQisqLKKELTNSESENSEKQRELEEKQNEIEKLK-KENQSYKQEIKNLESQINDLESKIqnqeklnqqkdeqikklq 418
|
410 420
....*....|....*....|....
gi 2024431993 607 ---HSLEKEYEKTKNQREMEEKFI 627
Cdd:TIGR04523 419 qekELLEKEIERLKETIIKNNSEI 442
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
231-548 |
5.99e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.06 E-value: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 231 RCEELEKEIAELRQQTEELTALaEEAQSLKDEIDVLRHSSDKVAKLESQVESYKKKLEdlGDLRRQVKLLEEKNTMY--M 308
Cdd:COG5022 860 RFSLLKKETIYLQSAQRVELAE-RQLQELKIDVKSISSLKLVNLELESEIIELKKSLS--SDLIENLEFKTELIARLkkL 936
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 309 QNTVSLEEELRKanaarsQLETYKrQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQKEKDRLRTERDSLKETIEELR 388
Cdd:COG5022 937 LNNIDLEEGPSI------EYVKLP-ELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYG 1009
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 389 CVQAQEGQLTTtglmplgRQEPSDSLAAEIVtpeikekliRLQHENKILKLNQEGSDNEKIALLQSLLDDANLRKNELET 468
Cdd:COG5022 1010 ALQESTKQLKE-------LPVEVAELQSASK---------IISSESTELSILKPLQKLKGLLLLENNQLQARYKALKLRR 1073
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 469 ENRLVNQRLLEVQSQVEELQKSLQDQDSKAEDAISVLLKKKLEEHLEKLHEANNELQKK---RAIIEDLEPRCNNSSLKI 545
Cdd:COG5022 1074 ENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISkflSQLVNTLEPVFQKLSVLQ 1153
|
...
gi 2024431993 546 EEL 548
Cdd:COG5022 1154 LEL 1156
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
104-303 |
6.95e-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: 39.36 E-value: 6.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 104 ESVQHMVMAAIQELMSKESPVSVGNDAYVDLDRQLKKTTEELNEALSTKEEIAQRCHELDMQVAALQ---EEKSSLLAEN 180
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRaelEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 181 QILMERLNQSDSIE---DPNSPAGrrhlQLQTQLEQLQEETFRLEAAkDDYRIRCEELEKEIAELRQQTEELTALAEEAQ 257
Cdd:COG4942 110 LRALYRLGRQPPLAlllSPEDFLD----AVRRLQYLKYLAPARREQA-EELRADLAELAALRAELEAERAELEALLAELE 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2024431993 258 SLKDEIDVLRHSSDK-VAKLESQVESYKKKLEDL----GDLRRQVKLLEEK 303
Cdd:COG4942 185 EERAALEALKAERQKlLARLEKELAELAAELAELqqeaEELEALIARLEAE 235
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
142-401 |
7.45e-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: 39.36 E-value: 7.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 142 TEELNEALSTKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQsdsiedpnspAGRRHLQLQTQLEqlqeetfrl 221
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA----------LARRIRALEQELA--------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 222 eaakddyrirceELEKEIAELRQQTEELTA-LAEEAQSLKDEIDVL-RHSSDKVAKLESQVESYKKKLEDLGDLRRQVKL 299
Cdd:COG4942 80 ------------ALEAELAELEKEIAELRAeLEAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 300 LEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQAVELQNRLSEESKKADKLDyecKRLKEKVDSLQKEKDRLRTERDS 379
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLL---ARLEKELAELAAELAELQQEAEE 224
|
250 260
....*....|....*....|..
gi 2024431993 380 LKETIEELRCVQAQEGQLTTTG 401
Cdd:COG4942 225 LEALIARLEAEAAAAAERTPAA 246
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
224-393 |
7.74e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.04 E-value: 7.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 224 AKDDYRIRCEELEKEIAELRQQTEELTALAEEAQSLKDEIDVLRhssDKVAKLESQVESYKKKLEDL-GDLRRQVKLLEE 302
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQ---AELEALQAEIDKLQAEIAEAeAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 303 K-NTMYMQ-NTVSLEEELRKAN---------AARSQLETYKRQAVELQNRLSEESKKADkldyecKRLKEKVDSLQKEKD 371
Cdd:COG3883 91 RaRALYRSgGSVSYLDVLLGSEsfsdfldrlSALSKIADADADLLEELKADKAELEAKK------AELEAKLAELEALKA 164
|
170 180
....*....|....*....|..
gi 2024431993 372 RLRTERDSLKETIEELRCVQAQ 393
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQ 186
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
233-534 |
7.84e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 39.62 E-value: 7.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 233 EELEKEIAELRQQTEELTALAEEAQSLKDEIDVLRH--SSDKVAKLESQVESYKKKLEDL-----------GDLRRQVKL 299
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNqkEQDWNKELKSELKNQEKKLEEIqnqisqnnkiiSQLNEQISQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 300 LEEKNTMYMQNTVSLEEELRKANAA-----------RSQLETYKRQAVELQNRLSEESKKADKLDYECKRLKEKVDSLQK 368
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEieklkkenqsyKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 369 EKDRLRTERDSLKETIEEL---------------RCVQAQEGQLTTtglmpLGRQEPSDSLAAEIVTPEIKEKlirlqhE 433
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLtnqdsvkeliiknldNTRESLETQLKV-----LSRSINKIKQNLEQKQKELKSK------E 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 434 NKILKLNQEGSD-NEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQDSKAEdaisvllKKKLEE 512
Cdd:TIGR04523 496 KELKKLNEEKKElEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKE-------IDEKNK 568
|
330 340
....*....|....*....|..
gi 2024431993 513 HLEKLHEANNELQKKRAIIEDL 534
Cdd:TIGR04523 569 EIEELKQTQKSLKKKQEEKQEL 590
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
328-620 |
8.95e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 39.33 E-value: 8.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 328 LETYKRQAVELQNRLSEESKKADKLDYECKR----LKEKVDSLQKEKDRL----RTE-------RDSLKETIEEL---RC 389
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNELHEKQKFYLRQsvidLQTKLQEMQMERDAMadirRREsqsqedlRNQLQNTVHELeaaKC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 390 VQAQEGQLTTTGLMPLGRQepsdSLAAEIVTPEIKEKLIRLQhENKILKLNQEgsDNEKIALLQSLLDDANLRKNELETE 469
Cdd:pfam15921 160 LKEDMLEDSNTQIEQLRKM----MLSHEGVLQEIRSILVDFE-EASGKKIYEH--DSMSTMHFRSLGSAISKILRELDTE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 470 NRLVNQRLLEVQSQVEELQKSLQDQD----SKAEDAISVLLKKK------LEEHLEKLHEANNELQKKRAIIEDLEPRCN 539
Cdd:pfam15921 233 ISYLKGRIFPVEDQLEALKSESQNKIelllQQHQDRIEQLISEHeveitgLTEKASSARSQANSIQSQLEIIQEQARNQN 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431993 540 NSSLK--------IEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQgAAPEIQALKNQLQERDRMFHSLEK 611
Cdd:pfam15921 313 SMYMRqlsdlestVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQ-FSQESGNLDDQLQKLLADLHKREK 391
|
330
....*....|.
gi 2024431993 612 E--YEKTKNQR 620
Cdd:pfam15921 392 ElsLEKEQNKR 402
|
|
| |
