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 27-MAR-2024, entry version 112. 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 EnsemblMetazoa; Bm12304.1; Bm12304.1; WBGene00232565. DR InParanoid; Q27450; -. DR OrthoDB; 5604991at2759; -. 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 Gene3D; 2.40.100.10; Cyclophilin-like; 1. DR InterPro; IPR029000; Cyclophilin-like_dom_sf. DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS. DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom. DR PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1. DR PANTHER; PTHR11071:SF561; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE H; 1. DR Pfam; PF00160; Pro_isomerase; 1. DR PRINTS; PR00153; CSAPPISMRASE. DR SUPFAM; SSF50891; Cyclophilin-like; 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 //