BLASTP 2.2.1 [Apr-13-2001]


Reference:
Altschul, Stephen F., Thomas L. Madden, Alejandro A. Schäffer, 
Jinghui Zhang, Zheng Zhang, Webb Miller, and David J. Lipman (1997), 
"Gapped BLAST and PSI-BLAST: a new generation of protein database search
programs",  Nucleic Acids Res. 25:3389-3402.

Query= gi|15645950|ref|NP_208129.1| conserved hypothetical
protein [Helicobacter pylori 26695]
         (174 letters)

Database: /var/www/html/HP/blast_new/blast/db/pdbaa
           13,198 sequences; 2,899,336 total letters

Searching...........................done


                                                                   Score     E
Sequences producing significant alignments:                        (bits)  Value

pdb|1KAM|A  Chain A, Structure Of Bacillus Subtilis Nicotini...    61  8e-11
pdb|1K4K|A  Chain A, Crystal Structure Of E. Coli Nicotinic ...    56  3e-09
pdb|1QJC|A  Chain A, Phosphopantetheine Adenylytransferase F...    32  0.031
pdb|1GN8|A  Chain A, Phosphopantetheine Adenylyltransferase ...    32  0.031
pdb|1AUI|A  Chain A, Human Calcineurin Heterodimer                 27  1.3
pdb|1TCO|A  Chain A, Ternary Complex Of A Calcineurin A Frag...    27  1.3
pdb|1MF8|A  Chain A, Crystal Structure Of Human Calcineurin ...    27  1.3
pdb|1M63|A  Chain A, Crystal Structure Of Calcineurin-Cyclop...    27  1.3
pdb|1KKU|A  Chain A, Crystal Structure Of Nuclear Human Nico...    27  1.7
pdb|1I2D|A  Chain A, Crystal Structure Of Atp Sulfurylase Fr...    27  1.7
pdb|1GZU|A  Chain A, Crystal Structure Of Human Nicotinamide...    26  2.9
pdb|1FXO|B  Chain B, The Structural Basis Of The Catalytic M...    25  3.8
pdb|1F9A|F  Chain F, Crystal Structure Analysis Of Nmn Adeny...    25  3.8
pdb|1G23|A  Chain A, The Structural Basis Of The Catalytic M...    25  6.4
>pdb|1KAM|A Chain A, Structure Of Bacillus Subtilis Nicotinic Acid
           Mononucleotide Adenylyl Transferase
 pdb|1KAM|B Chain B, Structure Of Bacillus Subtilis Nicotinic Acid
           Mononucleotide Adenylyl Transferase
 pdb|1KAM|C Chain C, Structure Of Bacillus Subtilis Nicotinic Acid
           Mononucleotide Adenylyl Transferase
 pdb|1KAM|D Chain D, Structure Of Bacillus Subtilis Nicotinic Acid
           Mononucleotide Adenylyl Transferase
 pdb|1KAQ|A Chain A, Structure Of Bacillus Subtilis Nicotinic Acid
           Mononucleotide Adenylyl Transferase
 pdb|1KAQ|B Chain B, Structure Of Bacillus Subtilis Nicotinic Acid
           Mononucleotide Adenylyl Transferase
 pdb|1KAQ|C Chain C, Structure Of Bacillus Subtilis Nicotinic Acid
           Mononucleotide Adenylyl Transferase
 pdb|1KAQ|D Chain D, Structure Of Bacillus Subtilis Nicotinic Acid
           Mononucleotide Adenylyl Transferase
 pdb|1KAQ|E Chain E, Structure Of Bacillus Subtilis Nicotinic Acid
           Mononucleotide Adenylyl Transferase
 pdb|1KAQ|F Chain F, Structure Of Bacillus Subtilis Nicotinic Acid
           Mononucleotide Adenylyl Transferase
          Length = 194

 Score = 60.8 bits (146), Expect = 8e-11
 Identities = 43/163 (26%), Positives = 79/163 (48%), Gaps = 8/163 (4%)

Query: 11  KELALYGGSFDPLHKAHLAIIEQTLELLPSAKLIVLPAYQNPFKK-PCFLDAQTRFKELE 69
           K++ ++GG+FDP H  HL +  + L      ++  +P    P K+   + D+  R + L+
Sbjct: 7   KKIGIFGGTFDPPHNGHLLMANEVLYQAGLDEIWFMPNQIPPHKQNEDYTDSFHRVEMLK 66

Query: 70  RALKGIDRVLLSDFEIKQERAVPTIESVLHFQKLYHPQTLYLVIGADCLRHLSSWTNAKE 129
            A++      L   E+++E    T ++V   ++ Y    L+ +IGAD + +L  W    E
Sbjct: 67  LAIQSNPSFKLELVEMEREGPSYTFDTVSLLKQRYPNDQLFFIIGADMIEYLPKWYKLDE 126

Query: 130 LLKRVELVVFERIGYEEIQFKGHYHPLKGIDAP---ISSSAIR 169
           LL  ++ +  +R G+         +PL   D P   +SS+ IR
Sbjct: 127 LLNLIQFIGVKRPGFH----VETPYPLLFADVPEFEVSSTMIR 165
>pdb|1K4K|A Chain A, Crystal Structure Of E. Coli Nicotinic Acid Mononucleotide
           Adenylyltransferase
 pdb|1K4K|B Chain B, Crystal Structure Of E. Coli Nicotinic Acid Mononucleotide
           Adenylyltransferase
 pdb|1K4K|C Chain C, Crystal Structure Of E. Coli Nicotinic Acid Mononucleotide
           Adenylyltransferase
 pdb|1K4K|D Chain D, Crystal Structure Of E. Coli Nicotinic Acid Mononucleotide
           Adenylyltransferase
 pdb|1K4M|A Chain A, Crystal Structure Of E.Coli Nicotinic Acid Mononucleotide
           Adenylyltransferase Complexed To Deamido-Nad
 pdb|1K4M|B Chain B, Crystal Structure Of E.Coli Nicotinic Acid Mononucleotide
           Adenylyltransferase Complexed To Deamido-Nad
 pdb|1K4M|C Chain C, Crystal Structure Of E.Coli Nicotinic Acid Mononucleotide
           Adenylyltransferase Complexed To Deamido-Nad
          Length = 213

 Score = 55.8 bits (133), Expect = 3e-09
 Identities = 35/132 (26%), Positives = 62/132 (46%), Gaps = 1/132 (0%)

Query: 14  ALYGGSFDPLHKAHLAIIEQTLELLPSAKLIVLPAYQNPFKKPCFLDAQTRFKELERALK 73
           AL+GG+FDP+H  HL  +E    L+   ++ ++P    P +     ++  R   LE A+ 
Sbjct: 6   ALFGGTFDPVHYGHLKPVETLANLIGLTRVTIIPNNVPPHRPQPEANSVQRKHMLELAIA 65

Query: 74  GIDRVLLSDFEIKQERAVPTIESVLHFQKLYHPQT-LYLVIGADCLRHLSSWTNAKELLK 132
                 L + E+K+     T +++  +++   P   L  +IG D L    +W   + +L 
Sbjct: 66  DKPLFTLDERELKRNAPSYTAQTLKEWRQEQGPDVPLAFIIGQDSLLTFPTWYEYETILD 125

Query: 133 RVELVVFERIGY 144
              L+V  R GY
Sbjct: 126 NAHLIVCRRPGY 137
>pdb|1QJC|A Chain A, Phosphopantetheine Adenylytransferase From Escherichia
          Coli In Complex With 4'-Phosphopantetheine
 pdb|1QJC|B Chain B, Phosphopantetheine Adenylytransferase From Escherichia
          Coli In Complex With 4'-Phosphopantetheine
          Length = 158

 Score = 32.3 bits (72), Expect = 0.031
 Identities = 14/45 (31%), Positives = 25/45 (55%), Gaps = 3/45 (6%)

Query: 14 ALYGGSFDPLHKAHLAIIEQTLELLPSAKLIVLPAYQNPFKKPCF 58
          A+Y G+FDP+   H+ I+ +  ++      ++L    +P KKP F
Sbjct: 4  AIYPGTFDPITNGHIDIVTRATQMFDH---VILAIAASPSKKPMF 45
>pdb|1GN8|A Chain A, Phosphopantetheine Adenylyltransferase In Complex With
          Mn2+ Atp From Escherichia Coli
 pdb|1GN8|B Chain B, Phosphopantetheine Adenylyltransferase In Complex With
          Mn2+ Atp From Escherichia Coli
 pdb|1B6T|A Chain A, Phosphopantetheine Adenylyltransferase In Complex With
          3'- Dephospho-Coa From Escherichia Coli
 pdb|1B6T|B Chain B, Phosphopantetheine Adenylyltransferase In Complex With
          3'- Dephospho-Coa From Escherichia Coli
          Length = 159

 Score = 32.3 bits (72), Expect = 0.031
 Identities = 14/45 (31%), Positives = 25/45 (55%), Gaps = 3/45 (6%)

Query: 14 ALYGGSFDPLHKAHLAIIEQTLELLPSAKLIVLPAYQNPFKKPCF 58
          A+Y G+FDP+   H+ I+ +  ++      ++L    +P KKP F
Sbjct: 5  AIYPGTFDPITNGHIDIVTRATQMFDH---VILAIAASPSKKPMF 46
>pdb|1AUI|A Chain A, Human Calcineurin Heterodimer
          Length = 521

 Score = 26.9 bits (58), Expect = 1.3
 Identities = 16/47 (34%), Positives = 27/47 (57%), Gaps = 2/47 (4%)

Query: 88  ERAVPTIESVLHFQ--KLYHPQTLYLVIGADCLRHLSSWTNAKELLK 132
           +R   +IE VL+    K+ +P+TL+L+ G    RHL+ +   K+  K
Sbjct: 121 DRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECK 167
>pdb|1TCO|A Chain A, Ternary Complex Of A Calcineurin A Fragment, Calcineurin
           B, Fkbp12 And The Immunosuppressant Drug Fk506
           (Tacrolimus)
          Length = 375

 Score = 26.9 bits (58), Expect = 1.3
 Identities = 16/47 (34%), Positives = 27/47 (57%), Gaps = 2/47 (4%)

Query: 88  ERAVPTIESVLHFQ--KLYHPQTLYLVIGADCLRHLSSWTNAKELLK 132
           +R   +IE VL+    K+ +P+TL+L+ G    RHL+ +   K+  K
Sbjct: 104 DRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECK 150
>pdb|1MF8|A Chain A, Crystal Structure Of Human Calcineurin Complexed With
           Cyclosporin A And Human Cyclophilin
          Length = 373

 Score = 26.9 bits (58), Expect = 1.3
 Identities = 16/47 (34%), Positives = 27/47 (57%), Gaps = 2/47 (4%)

Query: 88  ERAVPTIESVLHFQ--KLYHPQTLYLVIGADCLRHLSSWTNAKELLK 132
           +R   +IE VL+    K+ +P+TL+L+ G    RHL+ +   K+  K
Sbjct: 102 DRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECK 148
>pdb|1M63|A Chain A, Crystal Structure Of Calcineurin-Cyclophilin-Cyclosporin
           Shows Common But Distinct Recognition Of
           Immunophilin-Drug Complexes
 pdb|1M63|E Chain E, Crystal Structure Of Calcineurin-Cyclophilin-Cyclosporin
           Shows Common But Distinct Recognition Of
           Immunophilin-Drug Complexes
          Length = 372

 Score = 26.9 bits (58), Expect = 1.3
 Identities = 16/47 (34%), Positives = 27/47 (57%), Gaps = 2/47 (4%)

Query: 88  ERAVPTIESVLHFQ--KLYHPQTLYLVIGADCLRHLSSWTNAKELLK 132
           +R   +IE VL+    K+ +P+TL+L+ G    RHL+ +   K+  K
Sbjct: 121 DRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECK 167
>pdb|1KKU|A Chain A, Crystal Structure Of Nuclear Human Nicotinamide
           Mononucleotide Adenylyltransferase
          Length = 279

 Score = 26.6 bits (57), Expect = 1.7
 Identities = 26/105 (24%), Positives = 45/105 (42%), Gaps = 7/105 (6%)

Query: 4   MNSVLKYKELALYGGSFDPLHKAHLAIIEQTLELLPS------AKLIVLPAYQNPFKKPC 57
           M +  K + + L  GSF+P+   HL + E   + +         K I+ P   + +KK  
Sbjct: 1   MENSEKTEVVLLACGSFNPITNMHLRLFELAKDYMNGTGRYTVVKGIISPV-GDAYKKKG 59

Query: 58  FLDAQTRFKELERALKGIDRVLLSDFEIKQERAVPTIESVLHFQK 102
            + A  R    E A K    V +  +E  Q+    T++ + H Q+
Sbjct: 60  LIPAYHRVIMAELATKNSKWVEVDTWESLQKEWKETLKVLRHHQE 104
>pdb|1I2D|A Chain A, Crystal Structure Of Atp Sulfurylase From Penicillium
           Chrysogenum
 pdb|1I2D|B Chain B, Crystal Structure Of Atp Sulfurylase From Penicillium
           Chrysogenum
 pdb|1I2D|C Chain C, Crystal Structure Of Atp Sulfurylase From Penicillium
           Chrysogenum
          Length = 573

 Score = 26.6 bits (57), Expect = 1.7
 Identities = 20/66 (30%), Positives = 29/66 (43%), Gaps = 4/66 (6%)

Query: 51  NPFKKPCFLDAQTRFKELERALKGIDRVLLSDFEIKQERAVPTIESVLHFQKLYHPQTLY 110
           N F  P  LDA     + E+ L+   R+ L DF   +  A+ TI+ +    K    +   
Sbjct: 77  NVFSMPITLDASQEVID-EKKLQAGSRITLRDFRDDRNLAILTIDDIYRPDKTKEAK--- 132

Query: 111 LVIGAD 116
           LV G D
Sbjct: 133 LVFGGD 138
>pdb|1GZU|A Chain A, Crystal Structure Of Human Nicotinamide Mononucleotide
           Adenylyltransferase In Complex With Nmn
 pdb|1GZU|B Chain B, Crystal Structure Of Human Nicotinamide Mononucleotide
           Adenylyltransferase In Complex With Nmn
 pdb|1GZU|C Chain C, Crystal Structure Of Human Nicotinamide Mononucleotide
           Adenylyltransferase In Complex With Nmn
          Length = 290

 Score = 25.8 bits (55), Expect = 2.9
 Identities = 25/100 (25%), Positives = 42/100 (42%), Gaps = 7/100 (7%)

Query: 9   KYKELALYGGSFDPLHKAHLAIIEQTLELLPS------AKLIVLPAYQNPFKKPCFLDAQ 62
           K + + L  GSF+P+   HL + E   +           K I+ P   + +KK   + A 
Sbjct: 17  KTEVVLLACGSFNPITNXHLRLFELAKDYXNGTGRYTVVKGIISPV-GDAYKKKGLIPAY 75

Query: 63  TRFKELERALKGIDRVLLSDFEIKQERAVPTIESVLHFQK 102
            R    E A K    V +  +E  Q+    T++ + H Q+
Sbjct: 76  HRVIXAELATKNSKWVEVDTWESLQKEWKETLKVLRHHQE 115
>pdb|1FXO|B Chain B, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Tmp Complex.
 pdb|1FXO|E Chain E, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Tmp Complex.
 pdb|1FXO|F Chain F, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Tmp Complex.
 pdb|1FXO|G Chain G, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Tmp Complex.
 pdb|1G1L|B Chain B, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Tdp-Glucose Complex.
 pdb|1G1L|F Chain F, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Tdp-Glucose Complex.
 pdb|1G0R|F Chain F, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). ThymidineGLUCOSE-1-Phosphate Complex.
 pdb|1FZW|C Chain C, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Apo Enzyme.
 pdb|1FZW|F Chain F, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Apo Enzyme.
 pdb|1G3L|D Chain D, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Tdp-L-Rhamnose Complex.
 pdb|1FXO|A Chain A, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Tmp Complex.
 pdb|1FXO|C Chain C, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Tmp Complex.
 pdb|1FXO|D Chain D, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Tmp Complex.
 pdb|1FXO|H Chain H, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Tmp Complex.
 pdb|1G1L|A Chain A, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Tdp-Glucose Complex.
 pdb|1G1L|C Chain C, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Tdp-Glucose Complex.
 pdb|1G1L|D Chain D, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Tdp-Glucose Complex.
 pdb|1G1L|E Chain E, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Tdp-Glucose Complex.
 pdb|1G1L|G Chain G, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Tdp-Glucose Complex.
 pdb|1G1L|H Chain H, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Tdp-Glucose Complex.
 pdb|1G0R|A Chain A, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). ThymidineGLUCOSE-1-Phosphate Complex.
 pdb|1G0R|B Chain B, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). ThymidineGLUCOSE-1-Phosphate Complex.
 pdb|1G0R|C Chain C, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). ThymidineGLUCOSE-1-Phosphate Complex.
 pdb|1G0R|D Chain D, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). ThymidineGLUCOSE-1-Phosphate Complex.
 pdb|1G0R|E Chain E, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). ThymidineGLUCOSE-1-Phosphate Complex.
 pdb|1G0R|G Chain G, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). ThymidineGLUCOSE-1-Phosphate Complex.
 pdb|1G0R|H Chain H, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). ThymidineGLUCOSE-1-Phosphate Complex.
 pdb|1FZW|A Chain A, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Apo Enzyme.
 pdb|1FZW|B Chain B, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Apo Enzyme.
 pdb|1FZW|D Chain D, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Apo Enzyme.
 pdb|1FZW|E Chain E, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Apo Enzyme.
 pdb|1FZW|G Chain G, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Apo Enzyme.
 pdb|1FZW|H Chain H, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Apo Enzyme.
 pdb|1G2V|A Chain A, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Ttp Complex.
 pdb|1G2V|B Chain B, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Ttp Complex.
 pdb|1G2V|C Chain C, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Ttp Complex.
 pdb|1G2V|D Chain D, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Ttp Complex.
 pdb|1G2V|E Chain E, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Ttp Complex.
 pdb|1G2V|F Chain F, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Ttp Complex.
 pdb|1G2V|G Chain G, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Ttp Complex.
 pdb|1G2V|H Chain H, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Ttp Complex.
 pdb|1G3L|A Chain A, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Tdp-L-Rhamnose Complex.
 pdb|1G3L|B Chain B, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Tdp-L-Rhamnose Complex.
 pdb|1G3L|C Chain C, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Tdp-L-Rhamnose Complex
          Length = 293

 Score = 25.4 bits (54), Expect = 3.8
 Identities = 17/45 (37%), Positives = 21/45 (45%), Gaps = 11/45 (24%)

Query: 8  LKYKELALYGGSFDPLHKAHLAIIEQTLELLPSAKLIVLPAYQNP 52
          +K K + L GGS   LH A LAI +Q           +LP Y  P
Sbjct: 1  MKRKGIILAGGSGTRLHPATLAISKQ-----------LLPVYDKP 34
>pdb|1F9A|F Chain F, Crystal Structure Analysis Of Nmn Adenylyltransferase
          From Methanococcus Jannaschii
 pdb|1F9A|D Chain D, Crystal Structure Analysis Of Nmn Adenylyltransferase
          From Methanococcus Jannaschii
 pdb|1F9A|E Chain E, Crystal Structure Analysis Of Nmn Adenylyltransferase
          From Methanococcus Jannaschii
 pdb|1F9A|A Chain A, Crystal Structure Analysis Of Nmn Adenylyltransferase
          From Methanococcus Jannaschii
 pdb|1F9A|B Chain B, Crystal Structure Analysis Of Nmn Adenylyltransferase
          From Methanococcus Jannaschii
 pdb|1F9A|C Chain C, Crystal Structure Analysis Of Nmn Adenylyltransferase
          From Methanococcus Jannaschii
          Length = 168

 Score = 25.4 bits (54), Expect = 3.8
 Identities = 9/19 (47%), Positives = 12/19 (62%)

Query: 18 GSFDPLHKAHLAIIEQTLE 36
          G F P HK HL +I++  E
Sbjct: 7  GRFQPFHKGHLEVIKKIAE 25
>pdb|1G23|A Chain A, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Glucose-1-Phosphate Complex.
 pdb|1G23|B Chain B, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Glucose-1-Phosphate Complex.
 pdb|1G23|C Chain C, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Glucose-1-Phosphate Complex.
 pdb|1G23|D Chain D, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Glucose-1-Phosphate Complex.
 pdb|1G23|E Chain E, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Glucose-1-Phosphate Complex.
 pdb|1G23|F Chain F, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Glucose-1-Phosphate Complex.
 pdb|1G23|G Chain G, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Glucose-1-Phosphate Complex.
 pdb|1G23|H Chain H, The Structural Basis Of The Catalytic Mechanism And
          Regulation Of Glucose-1-Phosphate Thymidylyltransferase
          (Rmla). Glucose-1-Phosphate Complex
          Length = 293

 Score = 24.6 bits (52), Expect = 6.4
 Identities = 17/44 (38%), Positives = 20/44 (44%), Gaps = 11/44 (25%)

Query: 9  KYKELALYGGSFDPLHKAHLAIIEQTLELLPSAKLIVLPAYQNP 52
          K K + L GGS   LH A LAI +Q           +LP Y  P
Sbjct: 2  KRKGIILAGGSGTRLHPATLAISKQ-----------LLPVYDKP 34
  Database: /var/www/html/HP/blast_new/blast/db/pdbaa
    Posted date:  Dec 20, 2002 11:08 AM
  Number of letters in database: 2,899,336
  Number of sequences in database:  13,198
  
Lambda     K      H
   0.322    0.139    0.403 

Gapped
Lambda     K      H
   0.267   0.0410    0.140 


Matrix: BLOSUM62
Gap Penalties: Existence: 11, Extension: 1
Number of Hits to DB: 959,056
Number of Sequences: 13198
Number of extensions: 35663
Number of successful extensions: 114
Number of sequences better than 10.0: 14
Number of HSP's better than 10.0 without gapping: 11
Number of HSP's successfully gapped in prelim test: 3
Number of HSP's that attempted gapping in prelim test: 101
Number of HSP's gapped (non-prelim): 14
length of query: 174
length of database: 2,899,336
effective HSP length: 82
effective length of query: 92
effective length of database: 1,817,100
effective search space: 167173200
effective search space used: 167173200
T: 11
A: 40
X1: 16 ( 7.4 bits)
X2: 38 (14.6 bits)
X3: 64 (24.7 bits)
S1: 41 (21.9 bits)
S2: 51 (24.3 bits)