pir

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                P R O T E I N  S E Q U E N C E  D A T A B A S E
                             of PIR-International
 
                      Section 1. Fully Classified Entries
                        Release 63.00, December 30, 1999
                       20032 sequences, 7820966 residues
 
                       Protein Information Resource (PIR)*
                    National Biomedical Research Foundation
                          3900 Reservoir Road, N.W.,
                          Washington, DC  20007, USA
 
International Protein Information         Munich Information Center for
    Database in Japan (JIPID)               Protein Sequences (MIPS)
   Science University of Tokyo    GSF-Forschungszentrum f. Umwelt und Gesundheit
 2669 Yamazaki, Noda 278, Japan         am Max-Planck-Instut f. Biochemie
                                   Am Klopferspitz 18, D-82152 Martinsried, FRG
 
   This database may be redistributed without prior consent, provided that
   this notice be given to each user and that the words "Derived from" shall
   precede this notice if the database has been altered by the redistributor.
 
                       *PIR is a registered mark of NBRF.
 
 
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ENTRY            CCHU       #type complete
TITLE            cytochrome c - human
ORGANISM         #formal_name Homo sapiens #common_name man
DATE             24-Apr-1984 #sequence_revision 30-Sep-1991 #text_change
                   28-Jun-1999
ACCESSIONS       A31764; A05676; I55192; A00001
REFERENCE        A31764
   #authors      Evans, M.J.; Scarpulla, R.C.
   #journal      Proc. Natl. Acad. Sci. U.S.A. (1988) 85:9625-9629
   #title        The human somatic cytochrome c gene: two classes of processed
                   pseudogenes demarcate a period of rapid molecular
                   evolution.
   #cross-references MUID:89071748
   #accession    A31764
      ##molecule_type DNA
      ##residues      1-105 ##label EVA
      ##cross-references GB:M22877; NID:g181241; PIDN:AAA35732.1; PID:g181242
REFERENCE        A05676
   #authors      Matsubara, H.; Smith, E.L.
   #journal      J. Biol. Chem. (1963) 238:2732-2753
   #title        Human heart cytochrome c. Chymotryptic peptides, tryptic
                   peptides, and the complete amino acid sequence.
   #accession    A05676
      ##molecule_type protein
      ##residues      2-28;29-46;47-100;101-105 ##label MATS
REFERENCE        A00001
   #authors      Matsubara, H.; Smith, E.L.
   #journal      J. Biol. Chem. (1962) 237:3575-3576
   #title        The amino acid sequence of human heart cytochrome c.
   #contents     annotation
   #note         66-Leu is found in 10% of the molecules in pooled protein
REFERENCE        I55192
   #authors      Tanaka, Y.; Ashikari, T.; Shibano, Y.; Amachi, T.; Yoshizumi,
                   H.; Matsubara, H.
   #journal      J. Biochem. (1988) 103:954-961
   #title        Construction of a human cytochrome c gene and its functional
                   expression in Saccharomyces cerevisiae.
   #cross-references MUID:89008207
   #accession    I55192
      ##status        translated from GB/EMBL/DDBJ
      ##molecule_type mRNA
      ##residues      78-105 ##label RES
      ##cross-references GB:D00265; NID:g2897691; PIDN:BAA00187.1;
                         PID:d1000635; PID:g219557
GENETICS
   #introns      57/1
CLASSIFICATION   #superfamily cytochrome c; cytochrome c homology
KEYWORDS         acetylated amino end; chromoprotein; electron transfer; heme;
                   iron; mitochondrion; oxidative phosphorylation;
                   polymorphism; respiratory chain
FEATURE
   2-105              #product cytochrome c #status experimental #label MAT\
   5-99               #domain cytochrome c homology #label CYC\
   2                  #modified_site acetylated amino end (Gly) (in mature
                        form) #status experimental\
   15,18              #binding_site heme (Cys) (covalent) #status
                        experimental\
   19,81              #binding_site heme iron (His, Met) (axial ligands)
                        #status predicted
SUMMARY          #length 105  #molecular-weight 11749  #checksum 3247
SEQUENCE
                 5        10        15        20        25        30
       1 M G D V E K G K K I F I M K C S Q C H T V E K G G K H K T G
      31 P N L H G L F G R K T G Q A P G Y S Y T A A N K N K G I I W
      61 G E D T L M E Y L E N P K K Y I P G T K M I F V G I K K K E
      91 E R A D L I A Y L K K A T N E
///
ENTRY            CCCZ       #type complete
TITLE            cytochrome c - chimpanzee (tentative sequence)
ORGANISM         #formal_name Pan troglodytes #common_name chimpanzee
DATE             17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change
                   25-Apr-1997
ACCESSIONS       A00002
REFERENCE        A94601
   #authors      Needleman, S.B.
   #submission   submitted to the Atlas, October 1968
   #accession    A00002
      ##molecule_type protein
      ##residues      1-104 ##label NEE
REFERENCE        A94455
   #authors      Needleman, S.B.; Margoliash, E.
   #citation     unpublished results, 1966, cited by Margoliash, E., and
                   Fitch, W.M., Ann. N.Y. Acad. Sci. 151, 359-381, 1968
   #contents     annotation; compositions of chymotryptic peptides
CLASSIFICATION   #superfamily cytochrome c; cytochrome c homology
KEYWORDS         acetylated amino end; chromoprotein; electron transfer; heme;
                   iron; mitochondrion; oxidative phosphorylation; respiratory
                   chain
FEATURE
   4-98               #domain cytochrome c homology #label CYC\
   1                  #modified_site acetylated amino end (Gly) #status
                        predicted\
   14,17              #binding_site heme (Cys) (covalent) #status predicted\
   18,80              #binding_site heme iron (His, Met) (axial ligands)
                        #status predicted
SUMMARY          #length 104  #molecular-weight 11617  #checksum 9501
SEQUENCE
                 5        10        15        20        25        30
       1 G D V E K G K K I F I M K C S Q C H T V E K G G K H K T G P
      31 N L H G L F G R K T G Q A P G Y S Y T A A N K N K G I I W G
      61 E D T L M E Y L E N P K K Y I P G T K M I F V G I K K K E E
      91 R A D L I A Y L K K A T N E
///
ENTRY            CCMQR      #type complete
TITLE            cytochrome c - rhesus macaque (tentative sequence)
ORGANISM         #formal_name Macaca mulatta #common_name rhesus macaque
DATE             17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change
                   25-Apr-1997
ACCESSIONS       A00003
REFERENCE        A00003
   #authors      Rothfus, J.A.; Smith, E.L.
   #journal      J. Biol. Chem. (1965) 240:4277-4283
   #title        Amino acid sequence of rhesus monkey heart cytochrome c.
   #cross-references MUID:66045191
   #contents     compositions of chymotryptic peptides; sequences of residues
                   55-61 and 68-70
   #accession    A00003
      ##molecule_type protein
      ##residues      1-104 ##label ROT
CLASSIFICATION   #superfamily cytochrome c; cytochrome c homology
KEYWORDS         acetylated amino end; chromoprotein; electron transfer; heme;
                   iron; mitochondrion; oxidative phosphorylation; respiratory
                   chain
FEATURE
   4-98               #domain cytochrome c homology #label CYC\
   1                  #modified_site acetylated amino end (Gly) #status
                        experimental\
   14,17              #binding_site heme (Cys) (covalent) #status predicted\
   18,80              #binding_site heme iron (His, Met) (axial ligands)
                        #status predicted
SUMMARY          #length 104  #molecular-weight 11605  #checksum 9512
SEQUENCE
                 5        10        15        20        25        30
       1 G D V E K G K K I F I M K C S Q C H T V E K G G K H K T G P
      31 N L H G L F G R K T G Q A P G Y S Y T A A N K N K G I T W G
      61 E D T L M E Y L E N P K K Y I P G T K M I F V G I K K K E E
      91 R A D L I A Y L K K A T N E
///
ENTRY            CCMKP      #type complete
TITLE            cytochrome c - spider monkey
ORGANISM         #formal_name Ateles sp. #common_name spider monkey
DATE             17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change
                   25-Apr-1997
ACCESSIONS       A00004
REFERENCE        A00004
   #authors      Margoliash, E.
   #citation     unpublished results, cited by Shelnutt, J.A., Rousseau, D.L.,
                   Dethmers, J.K., and Margoliash, E., Biochemistry 20,
                   6485-6497, 1981
   #accession    A00004
      ##molecule_type protein
      ##residues      1-104 ##label MAR
CLASSIFICATION   #superfamily cytochrome c; cytochrome c homology
KEYWORDS         acetylated amino end; chromoprotein; electron transfer; heme;
                   iron; mitochondrion; oxidative phosphorylation; respiratory
                   chain
FEATURE
   4-98               #domain cytochrome c homology #label CYC\
   1                  #modified_site acetylated amino end (Gly) #status
                        predicted\
   14,17              #binding_site heme (Cys) (covalent) #status predicted\
   18,80              #binding_site heme iron (His, Met) (axial ligands)
                        #status predicted
SUMMARY          #length 104  #molecular-weight 11710  #checksum 9066
SEQUENCE
                 5        10        15        20        25        30
       1 G D V F K G K R I F I M K C S Q C H T V E K G G K H K T G P
      31 N L H G L F G R K T G Q A S G F T Y T E A N K N K G I I W G
      61 E D T L M E Y L E N P K K Y I P G T K M I F V G I K K K E E
      91 R A D L I A Y L K K A T N E
///
ENTRY            CCMS       #type complete
TITLE            cytochrome c - mouse
ORGANISM         #formal_name Mus musculus #common_name house mouse
DATE             31-Dec-1990 #sequence_revision 30-Sep-1991 #text_change
                   11-Jun-1999
ACCESSIONS       A23057; A04604; A00009
REFERENCE        A23057
   #authors      Limbach, K.J.; Wu, R.
   #journal      Nucleic Acids Res. (1985) 13:617-630
   #title        Characterization of a mouse somatic cytochrome c gene and
                   three cytochrome c pseudogenes.
   #cross-references MUID:85215501
   #accession    A23057
      ##molecule_type DNA
      ##residues      1-105 ##label LIM
      ##cross-references EMBL:X01756; NID:g50618; PIDN:CAA25899.1; PID:g50619
      ##experimental_source strain BALB/c
REFERENCE        A04604
   #authors      Carlson, S.S.; Mross, G.A.; Wilson, A.C.; Mead, R.T.; Wolin,
                   L.D.; Bowers, S.F.; Foley, N.T.; Muijsers, A.O.;
                   Margoliash, E.
   #journal      Biochemistry (1977) 16:1437-1442
   #title        Primary structure of mouse, rat, and guinea pig cytochrome c.
   #cross-references MUID:77134768
   #accession    A04604
      ##molecule_type protein
      ##residues      2-105 ##label CAR
      ##experimental_source strain BALB/c
GENETICS
   #introns      57/1
CLASSIFICATION   #superfamily cytochrome c; cytochrome c homology
KEYWORDS         acetylated amino end; chromoprotein; electron transfer; heme;
                   iron; mitochondrion; oxidative phosphorylation; respiratory
                   chain
FEATURE
   2-105              #product cytochrome c #status experimental #label MAT\
   5-99               #domain cytochrome c homology #label CYC\
   2                  #modified_site acetylated amino end (Gly) (in mature
                        form) #status experimental\
   15,18              #binding_site heme (Cys) (covalent) #status
                        experimental\
   19,81              #binding_site heme iron (His, Met) (axial ligands)
                        #status predicted
SUMMARY          #length 105  #molecular-weight 11605  #checksum 1273
SEQUENCE
                 5        10        15        20        25        30
       1 M G D V E K G K K I F V Q K C A Q C H T V E K G G K H K T G
      31 P N L H G L F G R K T G Q A A G F S Y T D A N K N K G I T W
      61 G E D T L M E Y L E N P K K Y I P G T K M I F A G I K K K G
      91 E R A D L I A Y L K K A T N E
///