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|15645228|ref|NP_207398.1| hypothetical protein
[Helicobacter pylori 26695]
(189 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|1L1Y|A Chain A, The Crystal Structure And Catalytic Mec... 26 2.5
pdb|1J6U|A Chain A, Crystal Structure Of Udp-N-Acetylmurama... 25 4.3
pdb|1GOW|A Chain A, Beta-Glycosidase From Sulfolobus Solfat... 25 7.3
pdb|1DWA|M Chain M, Study On Radiation Damage On A Cryocool... 24 9.6
pdb|1MYR| Myrosinase From Sinapis Alba 24 9.6
pdb|1E4M|M Chain M, Myrosinase From Sinapis Alba >gi|130967... 24 9.6
>pdb|1L1Y|A Chain A, The Crystal Structure And Catalytic Mechanism Of
Cellobiohydrolase Cels, The Major Enzymatic Component Of
The Clostridium Thermocellum Cellulosome
pdb|1L1Y|B Chain B, The Crystal Structure And Catalytic Mechanism Of
Cellobiohydrolase Cels, The Major Enzymatic Component Of
The Clostridium Thermocellum Cellulosome
pdb|1L1Y|C Chain C, The Crystal Structure And Catalytic Mechanism Of
Cellobiohydrolase Cels, The Major Enzymatic Component Of
The Clostridium Thermocellum Cellulosome
pdb|1L1Y|D Chain D, The Crystal Structure And Catalytic Mechanism Of
Cellobiohydrolase Cels, The Major Enzymatic Component Of
The Clostridium Thermocellum Cellulosome
pdb|1L1Y|E Chain E, The Crystal Structure And Catalytic Mechanism Of
Cellobiohydrolase Cels, The Major Enzymatic Component Of
The Clostridium Thermocellum Cellulosome
pdb|1L1Y|F Chain F, The Crystal Structure And Catalytic Mechanism Of
Cellobiohydrolase Cels, The Major Enzymatic Component Of
The Clostridium Thermocellum Cellulosome
pdb|1L2A|A Chain A, The Crystal Structure And Catalytic Mechanism Of
Cellobiohydrolase Cels, The Major Enzymatic Component Of
The Clostridium Thermocellum Cellulosome
pdb|1L2A|B Chain B, The Crystal Structure And Catalytic Mechanism Of
Cellobiohydrolase Cels, The Major Enzymatic Component Of
The Clostridium Thermocellum Cellulosome
pdb|1L2A|C Chain C, The Crystal Structure And Catalytic Mechanism Of
Cellobiohydrolase Cels, The Major Enzymatic Component Of
The Clostridium Thermocellum Cellulosome
pdb|1L2A|D Chain D, The Crystal Structure And Catalytic Mechanism Of
Cellobiohydrolase Cels, The Major Enzymatic Component Of
The Clostridium Thermocellum Cellulosome
pdb|1L2A|E Chain E, The Crystal Structure And Catalytic Mechanism Of
Cellobiohydrolase Cels, The Major Enzymatic Component Of
The Clostridium Thermocellum Cellulosome
pdb|1L2A|F Chain F, The Crystal Structure And Catalytic Mechanism Of
Cellobiohydrolase Cels, The Major Enzymatic Component Of
The Clostridium Thermocellum Cellulosome
Length = 678
Score = 26.2 bits (56), Expect = 2.5
Identities = 13/31 (41%), Positives = 16/31 (50%)
Query: 59 GFQVGFVLKKKALLGGYLDAGMGDSYFMSAG 89
G V V+ K A +G +L M D YFM G
Sbjct: 277 GSAVASVVSKAAKMGDFLRNDMFDKYFMKIG 307
>pdb|1J6U|A Chain A, Crystal Structure Of Udp-N-Acetylmuramate--Alanine Ligase
(Tm0231) From Thermotoga Maritima At 2.3 A Resolution
Length = 469
Score = 25.4 bits (54), Expect = 4.3
Identities = 16/52 (30%), Positives = 25/52 (47%), Gaps = 2/52 (3%)
Query: 124 NIQSAVGSVGLFFNAAKNFGLSIEARGGIPFYFIQSRFSKAFGTPRLNIYSV 175
N+ +A+ + LF + + +EA F + RFS AF P NIY +
Sbjct: 278 NVLNALAVIALFDSLGYDLAPVLEALE--EFRGVHRRFSIAFHDPETNIYVI 327
>pdb|1GOW|A Chain A, Beta-Glycosidase From Sulfolobus Solfataricus
pdb|1GOW|B Chain B, Beta-Glycosidase From Sulfolobus Solfataricus
Length = 489
Score = 24.6 bits (52), Expect = 7.3
Identities = 23/95 (24%), Positives = 36/95 (37%), Gaps = 12/95 (12%)
Query: 6 WNFFKP--LEPTKKYFGSFKIGYLYQHAETTKRSPIRPKNRPPILMDKTYHDASLGFQVG 63
W FF + KY+ + +LY + + RP L+ Y QV
Sbjct: 361 WEFFPEGLYDVLTKYWNRY---HLYMYVTENGIADDADYQRPYYLVSHVY-------QVH 410
Query: 64 FVLKKKALLGGYLDAGMGDSYFMSAGFMAGVRLFK 98
+ A + GYL + D+Y ++GF L K
Sbjct: 411 RAINSGADVRGYLHWSLADNYEWASGFSMRFGLLK 445
>pdb|1DWA|M Chain M, Study On Radiation Damage On A Cryocooled Crystal. Part 1:
Structure Prior To Irradiation
pdb|1DWF|M Chain M, Study On Radiation Damage On A Cryocooled Crystal. Part 2:
Structure After Irradiation With 9.110e15 Photons
pdb|1DWG|M Chain M, Study On Radiation Damage On A Cryocooled Crystal: Part 3:
Structure After Irradiation With 18.210e15 Photons
pdb|1DWH|M Chain M, Study On Radiation Damage On A Cryocooled Crystal. Part 4:
Structure After Irradiation With 27.210e15 Photons
pdb|1DWI|M Chain M, Study On Radiation Damage On A Cryocooled Crystal. Part 5:
Structure After Irradiation With 54.010e15 Photons
pdb|1DWJ|M Chain M, Study On Radiation Damage On A Cryocooled Crystal. Refined
Part 6: Structure After A Radiation Dose Of 5410e15
Photon
Length = 499
Score = 24.3 bits (51), Expect = 9.6
Identities = 16/52 (30%), Positives = 26/52 (49%), Gaps = 3/52 (5%)
Query: 42 KNRPPILMDKTYHD---ASLGFQVGFVLKKKALLGGYLDAGMGDSYFMSAGF 90
+NR ++D T D + L F + +K + GYL +GD+Y + GF
Sbjct: 416 ENRNQSMLDYTRIDYLCSHLCFLNKVIKEKDVNVKGYLAWALGDNYEFNKGF 467
>pdb|1MYR| Myrosinase From Sinapis Alba
Length = 501
Score = 24.3 bits (51), Expect = 9.6
Identities = 16/52 (30%), Positives = 26/52 (49%), Gaps = 3/52 (5%)
Query: 42 KNRPPILMDKTYHD---ASLGFQVGFVLKKKALLGGYLDAGMGDSYFMSAGF 90
+NR ++D T D + L F + +K + GYL +GD+Y + GF
Sbjct: 418 ENRKESMLDYTRIDYLCSHLCFLNKVIKEKDVNVKGYLAWALGDNYEFNNGF 469
>pdb|1E4M|M Chain M, Myrosinase From Sinapis Alba
pdb|1E6S|M Chain M, Myrosinase From Sinapis Alba With Bound
Gluco-Hydroximolactam And Sulfate
pdb|1E6Q|M Chain M, Myrosinase From Sinapis Alba With The Bound Transition
State Analogue Gluco-Tetrazole
pdb|1E73|M Chain M, 2-F-Glucosylated Myrosinase From Sinapis Alba With Bound
L-Ascorbate
pdb|1E71|M Chain M, Myrosinase From Sinapis Alba With Bound Ascorbate
pdb|1E72|M Chain M, Myrosinase From Sinapis Alba With Bound
Gluco-Hydroximolactam And Sulfate Or Ascorbate
pdb|1E6X|M Chain M, Myrosinase From Sinapis Alba With A Bound Transition State
Analogue,D-Glucono-1,5-Lactone
pdb|1E70|M Chain M, 2-F-Glucosylated Myrosinase From Sinapis Alba
Length = 501
Score = 24.3 bits (51), Expect = 9.6
Identities = 16/52 (30%), Positives = 26/52 (49%), Gaps = 3/52 (5%)
Query: 42 KNRPPILMDKTYHD---ASLGFQVGFVLKKKALLGGYLDAGMGDSYFMSAGF 90
+NR ++D T D + L F + +K + GYL +GD+Y + GF
Sbjct: 418 ENRNQSMLDYTRIDYLCSHLCFLNKVIKEKDVNVKGYLAWALGDNYEFNKGF 469
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
0.326 0.145 0.444
Gapped
Lambda K H
0.267 0.0410 0.140
Matrix: BLOSUM62
Gap Penalties: Existence: 11, Extension: 1
Number of Hits to DB: 1,137,560
Number of Sequences: 13198
Number of extensions: 45747
Number of successful extensions: 112
Number of sequences better than 10.0: 6
Number of HSP's better than 10.0 without gapping: 2
Number of HSP's successfully gapped in prelim test: 4
Number of HSP's that attempted gapping in prelim test: 110
Number of HSP's gapped (non-prelim): 6
length of query: 189
length of database: 2,899,336
effective HSP length: 83
effective length of query: 106
effective length of database: 1,803,902
effective search space: 191213612
effective search space used: 191213612
T: 11
A: 40
X1: 15 ( 7.1 bits)
X2: 38 (14.6 bits)
X3: 64 (24.7 bits)
S1: 40 (21.6 bits)
S2: 51 (24.3 bits)