FKBP5_RHIO9
ID FKBP5_RHIO9 Reviewed; 385 AA.
AC P0C1J7; I1CE33;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=FK506-binding protein 5;
DE EC=5.2.1.8;
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase;
DE Short=PPIase;
DE AltName: Full=Rotamase;
GN Name=FKBP5; Synonyms=fpr5; ORFNames=RO3G_11424;
OS Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL
OS 43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=246409;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880;
RX PubMed=19578406; DOI=10.1371/journal.pgen.1000549;
RA Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M.,
RA Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E.,
RA Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., Kodira C.D.,
RA Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S.,
RA Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., Ruiz-Herrera J.,
RA Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., Cuomo C.A., Wickes B.L.;
RT "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a
RT whole-genome duplication.";
RL PLoS Genet. 5:E1000549-E1000549(2009).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides (By similarity). {ECO:0000250}.
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: Inhibited by both FK506 and rapamycin.
CC {ECO:0000250}.
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DR EMBL; CH476740; EIE86713.1; -; Genomic_DNA.
DR AlphaFoldDB; P0C1J7; -.
DR SMR; P0C1J7; -.
DR STRING; 936053.P0C1J7; -.
DR EnsemblFungi; EIE86713; EIE86713; RO3G_11424.
DR VEuPathDB; FungiDB:RO3G_11424; -.
DR eggNOG; KOG0543; Eukaryota.
DR InParanoid; P0C1J7; -.
DR OMA; LWNCEPE; -.
DR OrthoDB; 897391at2759; -.
DR Proteomes; UP000009138; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00254; FKBP_C; 1.
DR Pfam; PF13181; TPR_8; 2.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 3: Inferred from homology;
KW Isomerase; Reference proteome; Repeat; Rotamase; TPR repeat.
FT CHAIN 1..385
FT /note="FK506-binding protein 5"
FT /id="PRO_0000244730"
FT DOMAIN 26..115
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT REPEAT 128..161
FT /note="TPR 1"
FT REPEAT 177..210
FT /note="TPR 2"
FT REPEAT 211..244
FT /note="TPR 3"
SQ SEQUENCE 385 AA; 43987 MW; BD242C221B24E785 CRC64;
MEQLTPDGGV TKRIIKAGLG QRPEPTNFVS VHYDAYLLDT SEKFDSSRDR NTEFTFQLRD
SKVIEAWELA IPTMQVGELA EIICTSDYGY GDQGRQYIVP PRAQLRFEVE LIGFWEKPKS
ASERIRLAEK KKNEGNALFK LDAIESALFA YRKGREYIQD LWDCEPEELE EARQLIVSIQ
LNIGACHLKL KHYDHAIEVC QKALDRDMTK IKAYYRIGQA YMEKGDYESS LTFIRIGLET
AIGLLAQSID LIENTLTDNE QFIHESKVMP SSTIVTVLNY DKRDRNIPAE NDRWAAKERI
IKIQKTIEEN SKISLDTPLV LSATIDASDS HQYQFQSSFG RELFYCSIHA IHHYASIKAI
CIELGLSVPS HFGLAPSTLQ HIKKQ