ru1a_human

这是一个基于HMM 模型的生物多序列比对算法的linux实现版本。hmmer

ID   RU1A_HUMAN     STANDARD;      PRT;   282 AA.
AC   P09012;
DT   01-NOV-1988 (Rel. 09, Created)
DT   01-NOV-1988 (Rel. 09, Last sequence update)
DT   15-JUL-1998 (Rel. 36, Last annotation update)
DE   U1 SMALL NUCLEAR RIBONUCLEOPROTEIN A (U1 SNRNP A PROTEIN).
GN   SNRPA.
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Mammalia;
OC   Eutheria; Primates; Catarrhini; Hominidae; Homo.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=LIVER;
RX   MEDLINE; 91340152.
RA   NELISSEN R.L.H., SILLEKENS P.T.G., BEIJER R.P.,
RA   GEURTS VAN KESSEL A.H.M., VAN VENROOIJ W.J.;
RT   "Structure, chromosomal localization and evolutionary conservation of
RT   the gene encoding human U1 snRNP-specific A protein.";
RL   Gene 102:189-196(1991).
RN   [2]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 88111575.
RA   SILLEKENS P.T.G., HABETS W.J., BEIJER R.P., VAN VENROOIJ W.J.;
RT   "cDNA cloning of the human U1 snRNA-associated A protein: extensive
RT   homology between U1 and U2 snRNP-specific proteins.";
RL   EMBO J. 6:3841-3848(1987).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-95.
RX   MEDLINE; 91061907.
RA   NAGAI K., OUBRIDGE C., JESSEN T.-H., LI J., EVANS P.R.;
RT   "Crystal structure of the RNA-binding domain of the U1 small nuclear
RT   ribonucleoprotein A.";
RL   Nature 348:515-520(1990).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS).
RX   MEDLINE; 95075454.
RA   OUBRIDGE C., ITO N., EVANS P.R., TEO C.-H., NAGAI K.;
RT   "Crystal structure at 1.92-A resolution of the RNA-binding domain of
RT   the U1A spliceosomal protein complexed with an RNA hairpin.";
RL   Nature 372:432-438(1994).
RN   [5]
RP   STRUCTURE BY NMR OF 11-94.
RX   MEDLINE; 91172834.
RA   HOFFMAN D.W., QUERY C.C., GOLDEN B.L., WHITE S.W., KEENE J.D.;
RT   "RNA-binding domain of the A protein component of the U1 small
RT   nuclear ribonucleoprotein analyzed by NMR spectroscopy is
RT   structurally similar to ribosomal proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:2495-2499(1991).
RN   [6]
RP   STRUCTURE BY NMR OF 1-102.
RX   MEDLINE; 94349935.
RA   HOWE P.W.A., NAGAI K., NEUHAUS D., VARANI G.;
RT   "NMR studies of U1 snRNA recognition by the N-terminal RNP domain of
RT   the human U1A protein.";
RL   EMBO J. 13:3873-3881(1994).
RN   [7]
RP   STRUCTURE BY NMR OF 2-102.
RX   MEDLINE; 96186818.
RA   ALLAIN F.H.-T., GUBSER C.C., HOWE P.W.A., NAGAI K., NEUHAUS D.,
RA   VARANI G.;
RT   "Specificity of ribonucleoprotein interaction determined by RNA
RT   folding during complex formulation.";
RL   Nature 380:646-650(1996).
RN   [8]
RP   STRUCTURE BY NMR OF 1-117.
RX   MEDLINE; 96180024.
RA   AVIS J.M., ALLAIN F.H.-T., HOWE P.W.A., VARANI G., NAGAI K.,
RA   NEUHAUS D.;
RT   "Solution structure of the N-terminal RNP domain of U1A protein: the
RT   role of C-terminal residues in structure stability and RNA binding.";
RL   J. Mol. Biol. 257:398-411(1996).
RN   [9]
RP   STRUCTURE BY NMR OF 1-102.
RX   MEDLINE; 97459961.
RA   ALLAIN F.H.-T., HOWE P.W., NEUHAUS D., VARANI G.;
RT   "Structural basis of the RNA-binding specificity of human U1A
RT   protein.";
RL   EMBO J. 16:5764-5772(1997).
RN   [10]
RP   STRUCTURE BY NMR OF 195-282.
RX   MEDLINE; 97410326.
RA   LU J., HALL K.B.;
RT   "Tertiary structure of RBD2 and backbone dynamics of RBD1 and RBD2 of
RT   the human U1A protein determined by NMR spectroscopy.";
RL   Biochemistry 36:10393-10405(1997).
RN   [11]
RP   MUTAGENESIS, AND DETAILED STUDIES OF RNA-BINDING.
RX   MEDLINE; 92007796.
RA   JESSEN T.-H., OUBRIDGE C., TEO C.H., PRITCHARD C., NAGAI K.;
RT   "Identification of molecular contacts between the U1 A small nuclear
RT   ribonucleoprotein and U1 RNA.";
RL   EMBO J. 10:3447-3456(1991).
CC   -!- FUNCTION: BINDS STEM LOOP II OF U1 SNRNA. IT IS THE FIRST SN-RNP
CC       TO INTERACT WITH PRE-MRNA. THIS INTERACTION IS REQUIRED FOR THE
CC       SUBSEQUENT BINDING OF U2 SN-RNP AND THE U4/U6/U5 TRI-SN-RNP.
CC   -!- SUBUNIT: BELONGS TO THE SPLICEOSOME WHERE IT IS ASSOCIATED WITH
CC       SN-RNP U1.
CC   -!- SUBCELLULAR LOCATION: NUCLEAR.
CC   -!- SIMILARITY: BELONGS TO THE U1 A/B" FAMILY.
CC   -!- SIMILARITY: CONTAINS 2 RNA RECOGNITION MOTIFS (RNP).
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to [e-mail]).
CC   --------------------------------------------------------------------------
DR   EMBL; M60784; AAA61245.1; -.
DR   EMBL; M60779; AAA61245.1; JOINED.
DR   EMBL; M60780; AAA61245.1; JOINED.
DR   EMBL; M60781; AAA61245.1; JOINED.
DR   EMBL; M60782; AAA61245.1; JOINED.
DR   EMBL; M60783; AAA61245.1; JOINED.
DR   EMBL; X06347; CAA29653.1; -.
DR   PIR; JQ1528; JQ1528.
DR   PDB; 1NRC; 31-JAN-94.
DR   PDB; 1FHT; 11-JUL-96.
DR   PDB; 1AUD; 25-FEB-98.
DR   PDB; 1URN; 08-MAR-96.
DR   PDB; 2U1A; 26-SEP-97.
DR   PDB; 3UTR; 03-APR-96.
DR   MIM; 182285; -.
DR   PFAM; PF00076; rrm; 2.
DR   PROSITE; PS00030; RNP_1; 1.
KW   Nuclear protein; RNA-binding; Ribonucleoprotein; Repeat;
KW   Spliceosome; 3D-structure.
FT   DOMAIN       12     17       RNA-BINDING (RNP2) (BY SIMILARITY).
FT   DOMAIN       52     59       RNA-BINDING (RNP1) (BY SIMILARITY).
FT   DOMAIN      210    215       RNA-BINDING (RNP2) (BY SIMILARITY).
FT   DOMAIN      244    251       RNA-BINDING (RNP1) (BY SIMILARITY).
FT   REPEAT        1     89
FT   REPEAT      199    282
FT   MUTAGEN      11     11       T->V: ABOLISHES RNA-BINDING.
FT   MUTAGEN      13     13       Y->F: SUBSTANTIALLY REDUCES RNA-BINDING.
FT   MUTAGEN      15     15       N->V: ABOLISHES RNA-BINDING.
FT   MUTAGEN      16     16       N->V: SUBSTANTIALLY REDUCES RNA-BINDING.
FT   MUTAGEN      52     52       R->Q: ABOLISHES RNA-BINDING.
SQ   SEQUENCE   282 AA;  31279 MW;  22427816 CRC32;
     MAVPETRPNH TIYINNLNEK IKKDELKKSL YAIFSQFGQI LDILVSRSLK MRGQAFVIFK
     EVSSATNALR SMQGFPFYDK PMRIQYAKTD SDIIAKMKGT FVERDRKREK RKPKSQETPA
     TKKAVQGGGA TPVVGAVQGP VPGMPPMTQA PRIMHHMPGQ PPYMPPPGMI PPPGLAPGQI
     PPGAMPPQQL MPGQMPPAQP LSENPPNHIL FLTNLPEETN ELMLSMLFNQ FPGFKEVRLV
     PGRHDIAFVE FDNEVQAGAA RDALQGFKIT QNNAMKISFA KK
//