printsextract.input

emboss的linux版本的源代码

<a name="input.1"></a>
<h3>Input files for usage example </h3>
<p><h3>File: prints.test</h3>
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<pre>
gc; ACHEFISH
gx; PR00879
gn; COMPOUND(4)
ga; 06-JUL-1998; UPDATE 06-JUN-1999
gt; Fish acetylcholinesterase signature
gp; PRINTS; PR00878 CHOLNESTRASE; PR00880 ACHEINSECT
gp; INTERPRO; IPR000908
gp; PDB; 2ACE
gp; SCOP; 2ACE
gp; CATH; 2ACE
bb;
gr; 1. VOET, D. AND VOET, J.G.
gr; Biochemical communications: Hormones and neurotransmission.
gr; BIOCHEMISTRY 34(4) 1298-1299 (1995).
gr; 
gr; 2. COUSIN, X., HOTELIER, T., GILES, K., TOUTANT, J.P. AND CHATONNET, A.
gr; aCHEdb: the database system for ESTHER, the a/b fold family of proteins and
gr; the cholinesterase gene server.
gr; NUCLEIC ACIDS RES. 26 226-228 (1998).
gr; 
gr; 3. THE ESTHER DATABASE
gr; http://meleze.ensam.inra.fr/cholinesterase/definitions.html
gr; 
gr; 4. CHOLINESTERASES
gr; http://bnlstb.bio.bnl.gov:8000/disk$3/giles/che.html
bb;
bb;
gd; Acetylcholine is involved in the transfer of messages across a variety of
gd; synapses in vertebrates and invertebrates. The diverse physiological effects
gd; attributable to this molecule arise from the presence of specific receptors
gd; in the postsynaptic cell membranes. Several classes of receptor are known, 
gd; most of which translate the binding of acetylcholine into the opening of 
gd; channels for the passage of ions, such as sodium and potassium.
gd;
gd; Acetylcholinesterase is an enzyme that catalyses the hydrolysis of 
gd; acetylcholine to choline and acetate:
gd; 
gd;	     Acetylcholine + H(2)O -&gt; Choline + Acetate 	     
gd; 
gd; The enzyme also acts on a variety of acetic esters and catalyses trans-
gd; acetylations. It is found in, or attached to, cellular or basement membranes
gd; of presynaptic cholinergic neurons and postsynaptic cholinoceptive cells.
gd; To prevent continuous firing of nerve impulses, acetylcholinesterase has a
gd; high K(cat) (~14000/s), to ensure that acetylcholine is broken down quickly.
gd;
gd; Cholinesterases constitute a family of enzymes that fall into two main
gd; types, depending on their substrate preference: enzymes that preferentially
gd; hydrolyse acetyl esters are termed acetylcholinesterase (AChE) (EC 3.1.1.7); 
gd; and those that prefer other types of ester, such as butyrylcholine are 
gd; termed butyrylcholinesterase (BChE) (EC 3.1.1.8). 


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fd; YFISGFLFYLATIINPIAYNLASSRFR          Q18701    323    17
fd; FIISMLLASLNSCCNPWIYMFFAGHLF          Q90334    311    13
fd; YKITRPLASANSCLDPVLYFLAGQRLV        P2UR_RAT    287    20
fd; AAMPAYFAKSATIYNPIIYVFMNRQFR      OPSR_CARAU    301    13
fd; AQWFIVLAVLNSAMNPVIYTLASKEMR      EDG3_HUMAN    280    14
fd; YKVTRPLASANSCLDPVLYFLAGQRLV      P2UR_HUMAN    288    20
fd; YKITRPLASANSCLDPVLYFLAGQRLV      P2UR_MOUSE    288    20
fd; AAMPAYFAKSATIYNPVIYVFMNRQFR      OPSR_ORYLA    301    13
fd; MAIPSFFSKSSALFNPIIYILLNKQFR      OPSG_ORYLA    289    13
fd; THFAFALQYINSAANPFLYVFLSDSFQ          Q23033    401    16
fd; FTAITWISFSSSASKPTLYSIYNANFR      GPRJ_HUMAN    312    13
fd; AALPAYFAKSATIYNPIIYVFMNRQFR      OPSR_CAPHI    304    13
fd; YINIYWLGMSSTVFNPVIYYFMNKRFR          O44148    323    16
fd; LHFTVCLMNFNCCMDPFIYFFACKGYK      EBI2_HUMAN    290    23
fd; FTAVTWVSFSSSASKPTLYSIYNANFR      GPRJ_MOUSE    306    13
fd; NYTGINMASLNSCIGPVALYFVSRKFK      ET3R_XENLA    365    36
fd; TIWGSVFAKANSCYNPIVYGISHPRYK      OPS2_LIMPO    310    13
fd; YLVALCLSTLNSCIDPFVYYFVSKDFR      PAR2_MOUSE    328    16
fd; YIVALCLSTLNSCIDPFVYYFVSHDFR      PAR2_HUMAN    326    16
fd; YLVALCLSTLNSCIDPFVYYFVSKDFR        PAR2_RAT    326    16
fd; YILSACVGSVSCCLDPLIYYYASSQCQ      THRR_XENLA    348    13
fd; TIWGSVFAKANAVYNPIVYGISHPKYR          O76125    317    12
fd; TIWGSVFAKANSCYNPIVYGISHPRYK      OPS1_LIMPO    310    13
fd; YLIALCLGSLNSCLDPFLYFVMSKVVD      PAR3_MOUSE    339    16
fd; TIWGSVFAKANAVYNPIVYGISHPKYR          O76123    317    12
fd; YLLCVCVTSVASCIDPLIYYYASSECQ        THRR_RAT    360    17
fd; VHVAEIVSLCHCFINPLIYAFCSREFT      VQ3L_CAPVK    337    21
fd; TIWGSLFAKANAVFNPIVYGISHPKYR      OPS1_SCHGR    315    12
fd; AAAPAFFSKTAAVYNPVIYVFMNKQVS      OPSO_SALSA    286    13
fd; YHFSLLLTSFNCVADPVLYCFVSETTH          O46685    268    17
fd; KILLVLFYPINSCANPFLYAIFTKNFR      FSHR_HORSE    607    13
fd; YIFCHLVGISSTCVNPIVYALVNESFR          O44690    308    12
fd; YLLCVCVSSISSCIDPLIYYYASSECQ      THRR_HUMAN    353    17
fd; AALPAYFAKSATIYNPIIYVFMNRQFR      OPSR_XENLA    303    13
fd; ITFSETISLARCCINPIIYTLIGEHVR      VK02_SPVKA    312    24
fd; YHSSLAFTSLNCVADPILYCLVNEGAR      GPR4_HUMAN    268    21
fd; YHFSLLLTSFNCVADPVLYCFVSETTH      OGR1_HUMAN    268    17
fd; YHSSLAFTSLNCVADPILYCLVNEGAR        GPR4_PIG    268    21
fd; TIWGSLFAKANAVYNPIVYGISHPKYR      OPSD_CAMAB    315    12
fd; TIWGSLFAKANAVYNPIVYGISHPKYR      OPSD_CATBO    315    12
fd; KILLVFFYPLNSCADPYLYAILTSQYR          Q94979    738    13
fd; TIWGACFAKSAACYNPIVYGISHPKYG      OPS1_CALVI    309    12
fd; KILLVLFYPINSCANPFLYAIFTKTFR      FSHR_CHICK    608    13
fd; KILLVLFYPINSCANPFLYAIFTKNFR      FSHR_EQUAS    600    13
fd; TMLPAVFAKTVSCIDPWIYAINHPRYR      OPSB_APIME    318    13
fd; TMIPAVTAKIVSCIDPWVYAINHPRFR      OPS2_SCHGR    315    13
fd; TIWGACFAKSAACYNPIVYGISHPKYR      OPS1_DROME    311    12
fd; TIWGSLFAKANAVYNPIVYGISHPKYR      OPSD_APIME    313    12
fd; SMLPCLACKSVSCLDPWVYATSHPKYR      OPS5_DROME    314    13
fd; TICGSVFAKANAVCNPIVYGLSHPKYK      OPS6_DROME    309    12
bb;
</pre>
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