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|15645119|ref|NP_207289.1| hypothetical protein
[Helicobacter pylori 26695]
(278 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|1DII|A Chain A, Crystal Structure Of P-Cresol Methylhyd... 34 0.016
pdb|1J91|A Chain A, Crystal Structure Of Z. Mays Ck2 Kinase... 26 4.4
pdb|1DAW|A Chain A, Crystal Structure Of A Binary Complex O... 26 4.4
pdb|1RPA| Prostatic Acid Phosphatase (E.C.3.1.3.2) Comple... 26 5.7
pdb|1LT7|A Chain A, Oxidized Homo Sapiens Betaine-Homocyste... 26 5.7
pdb|1OAC|B Chain B, Oxidoreductase, Copper, Tpq, Periplasmi... 25 9.8
pdb|1HBN|A Chain A, Methyl-Coenzyme M Reductase >gi|1582679... 25 9.8
pdb|1MRO|A Chain A, Methyl-Coenzyme M Reductase >gi|3891381... 25 9.8
pdb|1QAL|B Chain B, The Active Site Base Controls Cofactor ... 25 9.8
pdb|1QAF|B Chain B, The Active Site Base Controls Cofactor ... 25 9.8
pdb|1QAK|B Chain B, The Active Site Base Controls Cofactor ... 25 9.8
pdb|1JRQ|B Chain B, X-Ray Structure Analysis Of The Role Of... 25 9.8
pdb|1QGX|A Chain A, X-Ray Structure Of Yeast Hal2p >gi|1697... 25 9.8
>pdb|1DII|A Chain A, Crystal Structure Of P-Cresol Methylhydroxylase At 2.5 A
Resolution
pdb|1DII|B Chain B, Crystal Structure Of P-Cresol Methylhydroxylase At 2.5 A
Resolution
pdb|1DIQ|A Chain A, Crystal Structure Of P-Cresol Methylhydroxylase With
Substrate Bound
pdb|1DIQ|B Chain B, Crystal Structure Of P-Cresol Methylhydroxylase With
Substrate Bound
Length = 521
Score = 34.3 bits (77), Expect = 0.016
Identities = 24/68 (35%), Positives = 32/68 (46%), Gaps = 11/68 (16%)
Query: 66 NYPIHIVQAPQN-HHVVGILTPRIQVSDNLKPYIDKFQDALINQIQTIFEKRGYQV---- 120
+Y + AP++ HHV+ +L D P K DA N++ FEK GY V
Sbjct: 423 DYVAEFIVAPRDMHHVIDVLY------DRTNPEETKRADACFNELLDEFEKEGYAVYRVN 476
Query: 121 LRFQDEKA 128
RFQD A
Sbjct: 477 TRFQDRVA 484
>pdb|1J91|A Chain A, Crystal Structure Of Z. Mays Ck2 Kinase Alpha Subunit In
Complex With The Atp-Competitive Inhibitor 4,5,6,7-
Tetrabromobenzotriazole
pdb|1J91|B Chain B, Crystal Structure Of Z. Mays Ck2 Kinase Alpha Subunit In
Complex With The Atp-Competitive Inhibitor 4,5,6,7-
Tetrabromobenzotriazole
pdb|1JAM|A Chain A, Crystal Structure Of Apo-Form Of Z. Mays Ck2 Protein
Kinase Alpha Subunit
pdb|1LP4|A Chain A, Crystal Structure Of A Binary Complex Of The Catalytic
Subunit Of Protein Kinase Ck2 With Mg-Amppnp
pdb|1LPU|A Chain A, Low Temperature Crystal Structure Of The Apo-Form Of The
Catalytic Subunit Of Protein Kinase Ck2 From Zea Mays
pdb|1LR4|A Chain A, Room Temperature Crystal Structure Of The Apo-Form Of The
Catalytic Subunit Of Protein Kinase Ck2 From Zea Mays
pdb|1F0Q|A Chain A, Crystal Structure Of The Alpha Subunit Of Protein Kinase
Ck2 In Complex With The Nucleotide Competitive Inhibitor
Emodin
pdb|1DS5|A Chain A, Dimeric Crystal Structure Of The Alpha Subunit In Complex
With Two Beta Peptides Mimicking The Architecture Of The
Tetrameric Protein Kinase Ck2 Holoenzyme.
pdb|1DS5|B Chain B, Dimeric Crystal Structure Of The Alpha Subunit In Complex
With Two Beta Peptides Mimicking The Architecture Of The
Tetrameric Protein Kinase Ck2 Holoenzyme.
pdb|1DS5|C Chain C, Dimeric Crystal Structure Of The Alpha Subunit In Complex
With Two Beta Peptides Mimicking The Architecture Of The
Tetrameric Protein Kinase Ck2 Holoenzyme.
pdb|1DS5|D Chain D, Dimeric Crystal Structure Of The Alpha Subunit In Complex
With Two Beta Peptides Mimicking The Architecture Of The
Tetrameric Protein Kinase Ck2 Holoenzyme
Length = 332
Score = 26.2 bits (56), Expect = 4.4
Identities = 22/92 (23%), Positives = 37/92 (39%), Gaps = 9/92 (9%)
Query: 136 KIFSVLDLKGWVGILEDLKMNLKDPNNPNLDTLVDQSSGSVWFNFYEPESNRVVHDFAVE 195
KI VL G L ++ L +P L+ LV + S W F ++ +V A++
Sbjct: 239 KIAKVLGTDGLNVYLNKYRIEL----DPQLEALVGRHSRKPWLKFMNADNQHLVSPEAID 294
Query: 196 VGTFQAMTYTYKHNNSGGLNSSNSIIHEYLEK 227
F Y H L + ++ H Y ++
Sbjct: 295 ---FLDKLLRYDHQER--LTALEAMTHPYFQQ 321
>pdb|1DAW|A Chain A, Crystal Structure Of A Binary Complex Of Protein Kinase
Ck2 (Alpha-Subunit) And Mg-Amppnp
pdb|1DAY|A Chain A, Crystal Structure Of A Binary Complex Of Protein Kinase
Ck2 (Alpha-Subunit) And Mg-Gmppnp
Length = 327
Score = 26.2 bits (56), Expect = 4.4
Identities = 22/92 (23%), Positives = 37/92 (39%), Gaps = 9/92 (9%)
Query: 136 KIFSVLDLKGWVGILEDLKMNLKDPNNPNLDTLVDQSSGSVWFNFYEPESNRVVHDFAVE 195
KI VL G L ++ L +P L+ LV + S W F ++ +V A++
Sbjct: 238 KIAKVLGTDGLNVYLNKYRIEL----DPQLEALVGRHSRKPWLKFMNADNQHLVSPEAID 293
Query: 196 VGTFQAMTYTYKHNNSGGLNSSNSIIHEYLEK 227
F Y H L + ++ H Y ++
Sbjct: 294 ---FLDKLLRYDHQER--LTALEAMTHPYFQQ 320
>pdb|1RPA| Prostatic Acid Phosphatase (E.C.3.1.3.2) Complexed With Tartaric
Acid
pdb|1RPT| Prostatic Acid Phosphatase (E.C.3.1.3.2) Complexed With Vanadate
Length = 342
Score = 25.8 bits (55), Expect = 5.7
Identities = 14/42 (33%), Positives = 19/42 (44%), Gaps = 1/42 (2%)
Query: 163 PNLDTLVDQSSGSVWFNFYEPESNRVVHDFAVEV-GTFQAMT 203
P+L DQ +W Y+P VH+F + T AMT
Sbjct: 160 PSLSGFEDQDLFEIWSRLYDPLYCESVHNFTLPTWATEDAMT 201
>pdb|1LT7|A Chain A, Oxidized Homo Sapiens Betaine-Homocysteine S-
Methyltransferase In Complex With Four Sm(Iii) Ions
pdb|1LT7|B Chain B, Oxidized Homo Sapiens Betaine-Homocysteine S-
Methyltransferase In Complex With Four Sm(Iii) Ions
pdb|1LT8|A Chain A, Reduced Homo Sapiens Betaine-Homocysteine S-
Methyltransferase In Complex With
S-(Delta-Carboxybutyl)-L- Homocysteine
pdb|1LT8|B Chain B, Reduced Homo Sapiens Betaine-Homocysteine S-
Methyltransferase In Complex With
S-(Delta-Carboxybutyl)-L- Homocysteine
Length = 406
Score = 25.8 bits (55), Expect = 5.7
Identities = 16/54 (29%), Positives = 25/54 (45%), Gaps = 4/54 (7%)
Query: 211 SGGLNSSNSIIHEYLEKNKEDAIHKILNRMYAVVMKKAVTELTKENIDKYREAI 264
+GG++ + S YL E + K+ + V MKK V L E + EA+
Sbjct: 119 AGGVSQTPS----YLSAKSETEVKKVFLQQLEVFMKKNVDFLIAEYFEHVEEAV 168
>pdb|1OAC|B Chain B, Oxidoreductase, Copper, Tpq, Periplasmic, Signal Mol_id:
1; Molecule: Copper Amine Oxidase; Chain: A, B; Ec:
1.4.3.6
pdb|1OAC|A Chain A, Oxidoreductase, Copper, Tpq, Periplasmic, Signal Mol_id:
1; Molecule: Copper Amine Oxidase; Chain: A, B; Ec:
1.4.3.6
pdb|1SPU|B Chain B, Structure Of Oxidoreductase
pdb|1DYU|B Chain B, The Active Site Base Controls Cofactor Reactivity In
Escherichia Coli Amine Oxidase: X-Ray Crystallographic
Studies With Mutational Variants.
pdb|1D6Z|B Chain B, Crystal Structure Of The Aerobically Freeze Trapped Rate-
Determining Catalytic Intermediate Of E. Coli Copper-
Containing Amine Oxidase.
pdb|1D6Y|B Chain B, Crystal Structure Of E. Coli Copper-Containing Amine
Oxidase Anaerobically Reduced With Beta-Phenylethylamine
And Complexed With Nitric Oxide.
pdb|1D6U|B Chain B, Crystal Structure Of E. Coli Amine Oxidase Anaerobically
Reduced With Beta-Phenylethylamine
pdb|1SPU|A Chain A, Structure Of Oxidoreductase
pdb|1DYU|A Chain A, The Active Site Base Controls Cofactor Reactivity In
Escherichia Coli Amine Oxidase: X-Ray Crystallographic
Studies With Mutational Variants.
pdb|1D6Z|A Chain A, Crystal Structure Of The Aerobically Freeze Trapped Rate-
Determining Catalytic Intermediate Of E. Coli Copper-
Containing Amine Oxidase.
pdb|1D6Y|A Chain A, Crystal Structure Of E. Coli Copper-Containing Amine
Oxidase Anaerobically Reduced With Beta-Phenylethylamine
And Complexed With Nitric Oxide.
pdb|1D6U|A Chain A, Crystal Structure Of E. Coli Amine Oxidase Anaerobically
Reduced With Beta-Phenylethylamine
Length = 727
Score = 25.0 bits (53), Expect = 9.8
Identities = 13/41 (31%), Positives = 21/41 (50%)
Query: 195 EVGTFQAMTYTYKHNNSGGLNSSNSIIHEYLEKNKEDAIHK 235
E + AM K N +GG +S +++Y N++DA K
Sbjct: 539 ENNSLVAMDPVVKPNTAGGPRTSTMQVNQYNIGNEQDAAQK 579
>pdb|1HBN|A Chain A, Methyl-Coenzyme M Reductase
pdb|1HBN|D Chain D, Methyl-Coenzyme M Reductase
pdb|1HBO|A Chain A, Methyl-Coenzyme M Reductase Mcr-Red1-Silent
pdb|1HBO|D Chain D, Methyl-Coenzyme M Reductase Mcr-Red1-Silent
pdb|1HBM|A Chain A, Methyl-Coenzyme M Reductase Enzyme Product Complex
pdb|1HBM|D Chain D, Methyl-Coenzyme M Reductase Enzyme Product Complex
pdb|1HBU|A Chain A, Methyl-Coenzyme M Reductase In The Mcr-Red1-Silent State
In Complex With Coenzyme M
pdb|1HBU|D Chain D, Methyl-Coenzyme M Reductase In The Mcr-Red1-Silent State
In Complex With Coenzyme M
Length = 549
Score = 25.0 bits (53), Expect = 9.8
Identities = 11/29 (37%), Positives = 17/29 (57%)
Query: 237 LNRMYAVVMKKAVTELTKENIDKYREAID 265
LN +AV+ K+ E+T E I Y E ++
Sbjct: 108 LNHAHAVIEKRLGKEVTPETITHYLETVN 136
>pdb|1MRO|A Chain A, Methyl-Coenzyme M Reductase
pdb|1MRO|D Chain D, Methyl-Coenzyme M Reductase
Length = 548
Score = 25.0 bits (53), Expect = 9.8
Identities = 11/29 (37%), Positives = 17/29 (57%)
Query: 237 LNRMYAVVMKKAVTELTKENIDKYREAID 265
LN +AV+ K+ E+T E I Y E ++
Sbjct: 108 LNHAHAVIEKRLGKEVTPETITHYLETVN 136
>pdb|1QAL|B Chain B, The Active Site Base Controls Cofactor Reactivity In
Escherichia Coli Amine Oxidase : X-Ray Crystallographic
Studies With Mutational Variants
pdb|1QAL|A Chain A, The Active Site Base Controls Cofactor Reactivity In
Escherichia Coli Amine Oxidase : X-Ray Crystallographic
Studies With Mutational Variants
Length = 721
Score = 25.0 bits (53), Expect = 9.8
Identities = 13/41 (31%), Positives = 21/41 (50%)
Query: 195 EVGTFQAMTYTYKHNNSGGLNSSNSIIHEYLEKNKEDAIHK 235
E + AM K N +GG +S +++Y N++DA K
Sbjct: 534 ENNSLVAMDPVVKPNTAGGPRTSTMQVNQYNIGNEQDAAQK 574
>pdb|1QAF|B Chain B, The Active Site Base Controls Cofactor Reactivity In
Escherichia Coli Amine Oxidase : X-Ray Crystallographic
Studies With Mutational Variants
pdb|1QAF|A Chain A, The Active Site Base Controls Cofactor Reactivity In
Escherichia Coli Amine Oxidase : X-Ray Crystallographic
Studies With Mutational Variants
Length = 721
Score = 25.0 bits (53), Expect = 9.8
Identities = 13/41 (31%), Positives = 21/41 (50%)
Query: 195 EVGTFQAMTYTYKHNNSGGLNSSNSIIHEYLEKNKEDAIHK 235
E + AM K N +GG +S +++Y N++DA K
Sbjct: 534 ENNSLVAMDPVVKPNTAGGPRTSTMQVNQYNIGNEQDAAQK 574
>pdb|1QAK|B Chain B, The Active Site Base Controls Cofactor Reactivity In
Escherichia Coli Amine Oxidase : X-Ray Crystallographic
Studies With Mutational Variants
pdb|1QAK|A Chain A, The Active Site Base Controls Cofactor Reactivity In
Escherichia Coli Amine Oxidase : X-Ray Crystallographic
Studies With Mutational Variants
Length = 722
Score = 25.0 bits (53), Expect = 9.8
Identities = 13/41 (31%), Positives = 21/41 (50%)
Query: 195 EVGTFQAMTYTYKHNNSGGLNSSNSIIHEYLEKNKEDAIHK 235
E + AM K N +GG +S +++Y N++DA K
Sbjct: 534 ENNSLVAMDPVVKPNTAGGPRTSTMQVNQYNIGNEQDAAQK 574
>pdb|1JRQ|B Chain B, X-Ray Structure Analysis Of The Role Of The Conserved
Tyrosine-369 In Active Site Of E. Coli Amine Oxidase
pdb|1JRQ|A Chain A, X-Ray Structure Analysis Of The Role Of The Conserved
Tyrosine-369 In Active Site Of E. Coli Amine Oxidase
Length = 727
Score = 25.0 bits (53), Expect = 9.8
Identities = 13/41 (31%), Positives = 21/41 (50%)
Query: 195 EVGTFQAMTYTYKHNNSGGLNSSNSIIHEYLEKNKEDAIHK 235
E + AM K N +GG +S +++Y N++DA K
Sbjct: 539 ENNSLVAMDPVVKPNTAGGPRTSTMQVNQYNIGNEQDAAQK 579
>pdb|1QGX|A Chain A, X-Ray Structure Of Yeast Hal2p
pdb|1KA0|A Chain A, The Papase Hal2p Complexed With A Sodium Ion And The
Reaction Product Amp
pdb|1K9Y|A Chain A, The Papase Hal2p Complexed With Magnesium Ions And
Reaction Products: Amp And Inorganic Phosphate
pdb|1KA1|A Chain A, The Papase Hal2p Complexed With Calcium And Magnesium Ions
And Reaction Substrate: Pap
pdb|1K9Z|A Chain A, The Papase Hal2p Complexed With Zinc Ions
Length = 357
Score = 25.0 bits (53), Expect = 9.8
Identities = 17/51 (33%), Positives = 25/51 (48%), Gaps = 2/51 (3%)
Query: 17 LVALGLSSVLIGCAMNPSAETKTPNDAKNQVQTHER--MKTSSEHVTPLDF 65
L+ALGL+ V + + S + K + A V HE + T + PLDF
Sbjct: 270 LLALGLADVYLRLPIKLSYQEKIWDHAAGNVIVHEAGGIHTDAMEDVPLDF 320
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
0.317 0.133 0.376
Gapped
Lambda K H
0.267 0.0410 0.140
Matrix: BLOSUM62
Gap Penalties: Existence: 11, Extension: 1
Number of Hits to DB: 1,541,333
Number of Sequences: 13198
Number of extensions: 62682
Number of successful extensions: 206
Number of sequences better than 10.0: 13
Number of HSP's better than 10.0 without gapping: 8
Number of HSP's successfully gapped in prelim test: 5
Number of HSP's that attempted gapping in prelim test: 198
Number of HSP's gapped (non-prelim): 13
length of query: 278
length of database: 2,899,336
effective HSP length: 87
effective length of query: 191
effective length of database: 1,751,110
effective search space: 334462010
effective search space used: 334462010
T: 11
A: 40
X1: 16 ( 7.3 bits)
X2: 38 (14.6 bits)
X3: 64 (24.7 bits)
S1: 41 (21.6 bits)
S2: 53 (25.0 bits)