CYP1_BRUMA
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 03-AUG-2022, entry version 106.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase 1;
DE Short=PPIase 1;
DE EC=5.2.1.8;
DE AltName: Full=BmCYP-1;
DE AltName: Full=Cyclophilin;
DE AltName: Full=Rotamase 1;
GN Name=CYP-1;
OS Brugia malayi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6279;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX 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 from
RT the parasitic nematode Brugia malayi.";
RL Biochemistry 34:11545-11550(1995).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-177.
RX 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 parasite
RT 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 PubMed=9655334; DOI=10.1002/pro.5560070606;
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 CYCLOSPORIN
RP A.
RX 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 the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC -!- ACTIVITY REGULATION: Relatively insensitive to inhibition by
CC cyclosporin A (CsA).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 AlphaFoldDB; Q27450; -.
DR SMR; Q27450; -.
DR STRING; 6279.Q27450; -.
DR PRIDE; Q27450; -.
DR EnsemblMetazoa; Bm12304.1; Bm12304.1; WBGene00232565.
DR WBParaSite; Bm12304.1; Bm12304.1; WBGene00232565.
DR EvolutionaryTrace; Q27450; -.
DR Proteomes; UP000006672; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isomerase; Reference proteome; Rotamase.
FT CHAIN 1..843
FT /note="Peptidyl-prolyl cis-trans isomerase 1"
FT /id="PRO_0000064215"
FT DOMAIN 10..175
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REGION 178..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..306
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..697
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..736
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..789
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..843
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:1A58"
FT STRAND 7..15
FT /evidence="ECO:0007829|PDB:1A58"
FT STRAND 18..27
FT /evidence="ECO:0007829|PDB:1A58"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:1A58"
FT HELIX 33..44
FT /evidence="ECO:0007829|PDB:1A58"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:1A58"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:1C5F"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:1A58"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:1A58"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:1A58"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:1A58"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:1A58"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1C5F"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:1A58"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:1A58"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:1A58"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:1A58"
FT HELIX 147..154
FT /evidence="ECO:0007829|PDB:1A58"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:1A58"
FT STRAND 168..176
FT /evidence="ECO:0007829|PDB:1A58"
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
