RPS-BLAST 2.2.9 [May-01-2004]
Query= local sequence: lcl|tmpseq_0 unnamed protein product
(806 letters)
Database: cdd.v2.00
.. This CD alignment includes 3D structure. To display structure, download
Cn3D!
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PSSMs producing significant alignments: |
Score (bits) |
E value |
  |
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gnl|CDD|17769 |
cd00075, HATPase_c, Histidine kinase-like ATPases; This family... |
62.3 |
2e-10 |
|
gnl|CDD|24279 |
smart00433, TOP2c, TopoisomeraseII; Eukaryotic DNA topoisomera... |
678 |
0.0 |
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gnl|CDD|24279 |
smart00433, TOP2c, TopoisomeraseII; Eukaryotic DNA topoisomera... |
114 |
5e-26 |
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gnl|CDD|25316 |
smart00387, HATPase_c, Histidine kinase-like ATPases; Histidin... |
68.4 |
3e-12 |
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gnl|CDD|25440 |
pfam00204, DNA_gyraseB, DNA gyrase B. This family represents t... |
197 |
4e-51 |
|
gnl|CDD|25662 |
pfam00986, DNA_gyraseB_C, DNA gyrase B subunit, carboxyl termi... |
121 |
2e-28 |
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gnl|CDD|25917 |
pfam02518, HATPase_c, Histidine kinase-, DNA gyrase B-, and HS... |
68.9 |
2e-12 |
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gnl|CDD|8119 |
pfam01751, Toprim, Toprim domain. This is a conserved region f... |
38.0 |
0.005 |
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gnl|CDD|10062 |
COG0187, GyrB, Type IIA topoisomerase (DNA gyrase/topo II, top... |
900 |
0.0 |
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gnl|CDD|10062 |
COG0187, GyrB, Type IIA topoisomerase (DNA gyrase/topo II, top... |
135 |
2e-32 |
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gnl|CDD|10197 |
COG0323, MutL, DNA mismatch repair enzyme (predicted ATPase) [... |
37.6 |
0.005 |
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gnl|CDD|17769, cd00075, HATPase_c, Histidine kinase-like ATPases; This family includes several ATP-binding proteins for example: histidine kinase, DNA gyrase B, topoisomerases, heat shock protein HSP90, phytochrome-like ATPases and DNA mismatch repair proteins
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CD-Length = 103 residues, 85.4% aligned
Score = 62.3 bits (151), Expect = 2e-10
Query: 38 LHHMVFEVVDNSIDEALAGYCSEISITIHTDE---SITVRDNGRGIPVDIHKEEGVSAAE 94
Sbjct: 1 LQQVLLNLLSNAIKHTPEG-GGRITISVERDGDHLEIRVEDNGPGIPEEDLE-------- 51
Query: 95 VIMTVLHAGGKFDDNTYKVSGGLHGVGVSVVNALSHELRLTIR 137
Sbjct: 52 ------RIFERFSDGSRSRKGGGTGLGLSIVKKLVELHGGRIE 88
gnl|CDD|24279, smart00433, TOP2c, TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE
CD-Length = 594 residues, 87.7% aligned
Score = 678 bits (1751), Expect = 0.0
Query: 37 GLHHMVFEVVDNSIDEALAGYCSEISITIHTDESITVRDNGRGIPVDIHKEEGVSAAEVI 96
Sbjct: 1 GLHHLVDEIVDNAADEALAGYMDTIKVTIDKDNSISVEDNGRGIPVEIHPKEKKYAPEVI 60
Query: 97 MTVLHAGGKFDDNTYKVSGGLHGVGVSVVNALSHELRLTIRRHNKVWEQVYH-HGVPQFP 155
Sbjct: 61 FTVLHAGGKFDDDEYKVSGGLHGVGASVVNALSTEFEVEVARDGKEYKQSFSNNGKPLSE 120
Query: 156 LREVGETDGSGTEVHFKPSPETFSNI-HFSWDILAKRIRELSFLNSGVGILLRDERTGKE 214
Sbjct: 121 PKIIGDTKKDGTKVTFKPDLEIFGMTTDDDFELLKRRLRELAFLNKGVKITLNDERSDEE 180
Query: 215 ELFKYEGGLKAFVEYLNTNKTAVNEVFHFNVQREEDGVGVEVALQWNDSFNENLLCFTNN 274
Sbjct: 181 VTFLFEGGIKDYVELLNKNKELLSPEPTYIEG-EKDNIRVEVAFQYTDGYSENIVSFVNN 239
Query: 275 IPQRDGGTHLAGFRSALTRNLNNYIEAEGLAKKFKIATTGDDAREGLTAIISVKVPDPKF 334
Sbjct: 240 IATTEGGTHENGFKDALTRVINEYAKKKKKLKEKNI--KGEDVREGLTAFISVKIPEPQF 297
Query: 335 SSQTKDKLVSSEVKTAVEQEMGKYFADFLLENPNEAKAVVGKMIDAARAREAARKAREMT 394
Sbjct: 298 EGQTKEKLGTSEVRFGVEKIVSECLLSFLEENPVLASKIVEKVLLAAKARAAAKKARELT 357
Query: 395 RRKGALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAKQGRNRRTQAILPLKGKILN 454
Sbjct: 358 RKKSKLSSISLPGKLADASSAGPKKCELFLVEGDSAGGSAKSGRDRDFQAILPLRGKLLN 417
Query: 455 VEKARFDKMLSSQEVGTLITALGCGIGREEYNIDKLRYHNIIIMTDADVDGSHIRTLLLT 514
Sbjct: 418 VEKASLDKILKNEEIQALITALGLGIG-KDFDIEKLRYGKIIIMTDADVDGSHIKGLLLT 476
Query: 515 FFFRQMPELIERGYIYIAQPPLYKVKRGKQEQYIKDDQAMEEYMTQ 560
Sbjct: 477 FFYRYMPPLIEAGFVYIAIPPLYKVTKGKKKYVYSFYS-LDEYEKW 521
gnl|CDD|24279, smart00433, TOP2c, TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE
CD-Length = 594 residues, only 15.7% aligned
Score = 114 bits (286), Expect = 5e-26
Query: 709 VQKGERKRPISAF--KDGLDWLMAEGTKRH-SIQRYKGLGEMNPEQLWETTMDPNVRRML 765
Sbjct: 501 VTKGKKKYVYSFYSLDEYEKWLETKGNKKKYEIQRYKGLGEMNADQLWETTMDPERRTLL 560
Query: 766 KVTIEDAIAADQIFNTLMGDAVEPRRDFIESNA 798
Sbjct: 561 FVTLDDADEADLIFSALMGDKVEPRKEWIEENA 593
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gnl|CDD|25316, smart00387, HATPase_c, Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
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CD-Length = 112 residues, 85.7% aligned
Score = 68.4 bits (167), Expect = 3e-12
Query: 34 DGTGLHHMVFEVVDNSIDEALAGYCSEISITIHTDE---SITVRDNGRGIPVDIHKEEGV 90
Sbjct: 2 DPDRLRQVLSNLLDNAIKYTPEG--GRITVTLEREGDHVEITVEDNGPGIP--------- 50
Query: 91 SAAEVIMTVLHAGGKFDDNTYKVSGGLHGVGVSVVNALSHELRLTIRRHNK 141
Sbjct: 51 --PEDLEKIFEPFFRTDKRSRKIGG--TGLGLSIVKKLVELHGGEISVESE 97
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gnl|CDD|25440, pfam00204, DNA_gyraseB, DNA gyrase B. This family represents the second domain of DNA gyrase B which has a ribosomal S5 domain 2-like fold. This family is structurally related to PF01119.
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CD-Length = 170 residues, 100.0% aligned
Score = 197 bits (503), Expect = 4e-51
Query: 222 GLKAFVEYLNTNKTAV-NEVFHFNVQREEDGVGVEVALQW-NDSFNENLLCFTNNIPQRD 279
Sbjct: 1 GIKLYVKYLNESKEPIHPEPIVYEG---ENGIRVEVALQWSNDGYFEQILSFNNNIPTTE 57
Query: 280 GGTHLAGFRSALTRNLNNYIEAEGLAKKFKIATTGDDAREGLTAIISVKVPDPKFSSQTK 339
Sbjct: 58 GGTHVNGFKDALTRALNEYAKKKNKLKK-KDKLTGEDVREGLTAVISVKIPNPQFEGQTK 116
Query: 340 DKLVSSEVKTAVEQEMGKYFADFLLENPNEAKAVVGKMIDAARAREAARKAREM 393
Sbjct: 117 EKLGSSEVRFGVECIVSEKLLFFLEENPVDAKAIIEKAADAAKAREAAKKAREL 170
gnl|CDD|25662, pfam00986, DNA_gyraseB_C, DNA gyrase B subunit, carboxyl terminus. The amino terminus of eukaryotic and prokaryotic DNA topoisomerase II are similar, but they have a different carboxyl terminus. The amino-terminal portion of the DNA gyrase B protein is thought to catalyse the ATP-dependent super-coiling of DNA. See pfam00204. The carboxyl-terminal end supports the complexation with the DNA gyrase A protein and the ATP-independent relaxation. This family also contains Topoisomerase IV. This is a bacterial enzyme that is closely related to DNA gyrase.
CD-Length = 67 residues, 97.0% aligned
Score = 121 bits (306), Expect = 2e-28
Query: 731 EGTKRHSIQRYKGLGEMNPEQLWETTMDPNVRRMLKVTIEDAIAADQIFNTLMGDAVEPR 790
Sbjct: 3 NKKGKYEIQRYKGLGEMNPEQLWETTMDPETRTLLQVTIEDAAEADELFSILMGDKVEPR 62
Query: 791 RDFIE 795
Sbjct: 63 REFIE 67
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gnl|CDD|25917, pfam02518, HATPase_c, Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase. This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.
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CD-Length = 111 residues, 87.4% aligned
Score = 68.9 bits (168), Expect = 2e-12
Query: 34 DGTGLHHMVFEVVDNSIDEALAGYCSEISITIHTDE---SITVRDNGRGIPVDIHKEEGV 90
Sbjct: 2 DEDRLRQVLSNLLDNAIKHAPAG--GEITVRLEREGGDVRITVEDNGIGIP--------- 50
Query: 91 SAAEVIMTVLHAGGKFDDNTYKVSGGLHGVGVSVVNALSHELRLTIRRHNKV 142
Sbjct: 51 --PEDLERIFEPFFTTDGDSRKIGG--TGLGLSIVKELVELHGGTITVESEP 98
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gnl|CDD|8119, pfam01751, Toprim, Toprim domain. This is a conserved region from DNA primase. This corresponds to the Toprim domain common to DnaG primases, topoisomerases, OLD family nucleases and RecR proteins. Both DnaG motifs IV and V are present in the alignment, the DxD (V) motif may be involved in Mg2+ binding and mutations to the conserved glutamate (IV) completely abolish DnaG type primase activity. DNA primase EC:2.7.7.6 is a nucleotidyltransferase it synthesises the oligoribonucleotide primers required for DNA replication on the lagging strand of the replication fork; it can also prime the leading stand and has been implicated in cell division. This family also includes the atypical archaeal A subunit from type II DNA topoisomerases. Type II DNA topoisomerases catalyse the relaxation of DNA supercoiling by causing transient double strand breaks.
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CD-Length = 84 residues, 91.7% aligned
Score = 38.0 bits (88), Expect = 0.005
Query: 450 GKILNVEKARFDKMLSS--QEVGTLITALGCGIGREEYNIDKLRYHN--IIIMTDADVDG 505
Sbjct: 1 KVLIIVEGPSDAIALEKAGGYRGNVVALLGHLLTKEQLKLLKKLAKKDEVILATDPDREG 60
Query: 506 SHIRTLLLTFFFRQMPE 522
Sbjct: 61 EAIAWKLLELLKPYGKK 77
gnl|CDD|10062, COG0187, GyrB, Type IIA topoisomerase (DNA gyrase/topo II, topoisomerase IV), B subunit [DNA replication, recombination, and repair]
CD-Length = 635 residues, 87.9% aligned
Score = 900 bits (2328), Expect = 0.0
Query: 2 SENNTYDSSSIKVLKGLDAVRKRPGMYIGDTDDGTGLHHMVFEVVDNSIDEALAGYCSEI 61
Sbjct: 1 SKTNNYDASSIQVLEGLEAVRKRPGMYIGSTGDGRGLHHLVWEVVDNSIDEALAGYADRI 60
Query: 62 SITIHTDESITVRDNGRGIPVDIHKEEGVSAAEVIMTVLHAGGKFDDNTYKVSGGLHGVG 121
Sbjct: 61 DVTLHEDGSISVEDNGRGIPVDIHPKEKVSAVEVIFTVLHAGGKFDNDSYKVSGGLHGVG 120
Query: 122 VSVVNALSHELRLTIRRHNKVWEQVYHHGVPQFPLREVGETD--GSGTEVHFKPSPETFS 179
Sbjct: 121 VSVVNALSTWLEVEVKRDGKIYRQRFERGVPVTPLEVIGSTDTKKTGTKVRFKPDPEIFG 180
Query: 180 NIHFSWDILAKRIRELSFLNSGVGILLRDERTGKEEL-FKYEGGLKAFVEYLNTNKTAVN 238
Sbjct: 181 ETEFDYEILKRRLRELAFLNKGVKITLTDERTGEEKKEFHYEGGLKDYVEYLNKGKTPLH 240
Query: 239 EVFHFNVQREEDGVGVEVALQWNDSFNENLLCFTNNIPQRDGGTHLAGFRSALTRNLNNY 298
Sbjct: 241 EE-IFYFNGEKDGIAVEVALQWNDGYSENILSFVNNIPTREGGTHEAGFRSALTRAINEY 299
Query: 299 IEAEGLAKKFKIATTGDDAREGLTAIISVKVPDPKFSSQTKDKLVSSEVKTAVEQEMGKY 358
Sbjct: 300 AKKKNLLKEGDL--TGDDIREGLTAVISVKIPDPQFEGQTKEKLGNSEVRSIVEKLVSEA 357
Query: 359 FADFLLENPNEAKAVVGKMIDAARAREAARKAREMTRRKGALDIAGLPGKLADCQEKDPA 418
Sbjct: 358 FSLFLEENPQEAKKIVEKAIAAAKAREAARKARELTRRKSALDIPGLPGKLADCTSKDPE 417
Query: 419 LSELYIVEGDSAGGSAKQGRNRRTQAILPLKGKILNVEKARFDKMLSSQEVGTLITALGC 478
Sbjct: 418 KSELFLVEGDSAGGSAKQGRDREFQAILPLRGKILNVEKARLDKILKNEEIQTIITALGT 477
Query: 479 GIGREEYNIDKLRYHNIIIMTDADVDGSHIRTLLLTFFFRQMPELIERGYIYIAQPPLYK 538
Sbjct: 478 GIG-KDFDLEKLRYHKIIIMTDADVDGAHIRTLLLTFFYRYMPPLIENGHVYIAQPPLYK 536
Query: 539 VKRGKQEQYIKDDQAMEEYMTQ 560
Sbjct: 537 VKKGKKTFYAYDDEELEKLLER 558
gnl|CDD|10062, COG0187, GyrB, Type IIA topoisomerase (DNA gyrase/topo II, topoisomerase IV), B subunit [DNA replication, recombination, and repair]
CD-Length = 635 residues, only 11.5% aligned
Score = 135 bits (341), Expect = 2e-32
Query: 734 KRHSIQRYKGLGEMNPEQLWETTMDPNVRRMLKVTIEDAIAADQIFNTLMGDAVEPRRDF 793
Sbjct: 563 KGYEIQRYKGLGEMNPDQLWETTMDPETRRLLQVTIEDADEADEIFSTLMGDKVEPRRNF 622
Query: 794 IESNALAVSNLDV 806
Sbjct: 623 IEENALFVENLDI 635
gnl|CDD|10197, COG0323, MutL, DNA mismatch repair enzyme (predicted ATPase) [DNA replication, recombination, and repair]
CD-Length = 638 residues, only 6.4% aligned
Score = 37.6 bits (87), Expect = 0.005
Query: 41 MVFEVVDNSIDEALAGYCSEISITIHTD--ESITVRDNGRGIPVD 83
Sbjct: 27 VVKELVENSLD---AG-ATRIDIEVEGGGLKLIRVRDNGSGIDKE 67
Citing CD-Search:
Marchler-Bauer A, Anderson JB, DeWeese-Scott C, Fedorova ND, Geer LY, He S, Hurwitz DI, Jackson JD, Jacobs AR,
Lanczycki CJ, Liebert CA, Liu C, Madej T, Marchler GH, Mazumder R, Nikolskaya AN, Panchenko AR, Rao BS, Shoemaker BA,
Simonyan V, Song JS, Thiessen PA, Vasudevan S, Wang Y, Yamashita RA, Yin JJ, and Bryant SH (2003),
"CDD: a curated Entrez database of conserved domain alignments",
Nucleic Acids Res. 31:383-387.
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