ID   CYP1_BRUMA              Reviewed;         843 AA.
AC   Q27450;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 57.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase 1;
DE            Short=PPIase 1;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin;
DE   AltName: Full=BmCYP-1;
GN   Name=CYP-1;
OS   Brugia malayi (Filarial nematode worm).
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Spirurida; Filarioidea;
OC   Onchocercidae; Brugia.
OX   NCBI_TaxID=6279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=96009642; PubMed=7547885; DOI=10.1021/bi00036a030;
RA   Page A.P., Landry D., Wilson G.G., Carlow C.K.S.;
RT   "Molecular characterization of a cyclosporin A-insensitive cyclophilin
RT   from the parasitic nematode Brugia malayi.";
RL   Biochemistry 34:11545-11550(1995).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-177.
RX   MEDLINE=98218582; PubMed=9559680; DOI=10.1016/S0014-5793(98)00264-6;
RA   Taylor P., Page A.P., Kontopidis G., Husi H., Walkinshaw M.D.;
RT   "The X-ray structure of a divergent cyclophilin from the nematode
RT   parasite Brugia malayi.";
RL   FEBS Lett. 425:361-366(1998).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-177.
RC   STRAIN=ATCC 75593 / Bmcyp-1;
RX   MEDLINE=98318040; PubMed=9655334;
RA   Mikol V., Ma D., Carlow C.K.S.;
RT   "Crystal structure of the cyclophilin-like domain from the parasitic
RT   nematode Brugia malayi.";
RL   Protein Sci. 7:1310-1316(1998).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.47 ANGSTROMS) OF 1-177 IN COMPLEX WITH
RP   CYCLOSPORIN A.
RX   MEDLINE=20108543; PubMed=10642184; DOI=10.1021/bi991730q;
RA   Ellis P.J., Carlow C.K.S., Ma D., Kuhn P.;
RT   "Crystal structure of the complex of Brugia malayi cyclophilin and
RT   cyclosporin A.";
RL   Biochemistry 39:592-598(2000).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
CC       the cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides.
CC   -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC       (omega=0).
CC   -!- ENZYME REGULATION: Relatively insensitive to inhibition by
CC       cyclosporin A (CsA).
CC   -!- SIMILARITY: Contains 1 PPIase cyclophilin-type domain.
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DR   EMBL; L37292; AAC37249.1; -; mRNA.
DR   PDB; 1A33; X-ray; 2.15 A; A=1-177.
DR   PDB; 1A58; X-ray; 1.95 A; A=1-177.
DR   PDB; 1C5F; X-ray; 2.47 A; A/C/E/G/I/K/M/O=1-177.
DR   PDBsum; 1A33; -.
DR   PDBsum; 1A58; -.
DR   PDBsum; 1C5F; -.
DR   BRENDA; 5.2.1.8; 27.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-KW.
DR   InterPro; IPR002130; PPIase_cyclophilin.
DR   Gene3D; G3DSA:2.40.100.10; PPIase_cyclophilin; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Isomerase; Rotamase.
FT   CHAIN         1    843       Peptidyl-prolyl cis-trans isomerase 1.
FT                                /FTId=PRO_0000064215.
FT   DOMAIN       10    175       PPIase cyclophilin-type.
FT   COMPBIAS    700    709       Poly-Arg.
FT   COMPBIAS    713    716       Poly-Arg.
FT   COMPBIAS    800    815       Poly-Ser.
FT   COMPBIAS    828    837       Poly-Ser.
FT   STRAND        7     15
FT   STRAND       18     27
FT   TURN         29     31
FT   HELIX        33     44
FT   TURN         51     53
FT   STRAND       63     68
FT   TURN         69     71
FT   STRAND       72     75
FT   TURN         78     80
FT   STRAND       81     84
FT   STRAND      108    111
FT   STRAND      123    128
FT   HELIX       131    133
FT   TURN        134    136
FT   STRAND      139    145
FT   HELIX       147    154
FT   STRAND      164    166
FT   STRAND      168    175
SQ   SEQUENCE   843 AA;  97818 MW;  3C34EC90A32EDBDC CRC64;
     MSKKDRRRVF LDVTIDGNLA GRIVMELYND IAPRTCNNFL MLCTGMAGTG KISGKPLHYK
     GSTFHRVIKN FMIQGGDFTK GDGTGGESIY GGMFDDEEFV MKHDEPFVVS MANKGPNTNG
     SQFFITTTPA PHLNNIHVVF GKVVSGQEVV TKIEYLKTNS KNRPLADVVI LNCGELVRRK
     KRQHSSRSNE SVSSSTSTEK SHKKTKKTKM KEKKRKESDE VEQLEIGTVV PEAELQLSSV
     KAEDLPDEPD HQNKYLMRRS KTPENSRKGK KEKQRQSPHR FSRRDIGHRL NRMRRTRTGH
     KIKGRGALRF RTPEGSSDHD GSRTPPHWRR EQNRVITLDE LHRLQEKRKA YELEELENPK
     NDVVDKAKTG ILLNTSEKIE DKEERYRGKS EKKENRHERS RHTTRRSPEH VTRHFVKEKN
     RHKVDEVGNS EDMKQTKRDR RGRADEKEKV EVNGEKAAAM DELNLDEPTV EVTLDSAEDI
     RDSDDEAIRI HLLKAKKMAE EKTKQEAKML EKTGDKEGRD QKTISEAKQK DSAEKDRQHR
     EHKNDELEKR AIEKQDKDQI VERDTGSKQR RKSDSKEHRG KTDRKHRSKS IEEDGRRSTS
     REKLDDLKRK ETSGQKSQAD SEQTVEAKTN VVDSNSDNSK MSVNGKLKEV SSTNKENEVS
     EQKDLKAEST KSEEIKQQVN EVSRKQKGGE KPKEHKRNER SRSRRRRSRS NGRRRRSSSR
     RSRSRDRRHK SRSRSRGYVR RFEGWSRSRR PTRRELYDER MRRERERRRS FDRYSDRRRT
     RSRSARRDSD RHSRRSRKRS PSSSSSSSES SSSDSRSTAS SSASSKRSSS SDSSRSSRSR
     SSN
//