ID M7XDC5_RHOT1 Unreviewed; 389 AA.
AC M7XDC5;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=FK506-binding protein {ECO:0000256|PIRNR:PIRNR001473};
DE EC=5.2.1.8 {ECO:0000256|PIRNR:PIRNR001473};
GN ORFNames=RHTO_06642 {ECO:0000313|EMBL:EMS18148.1};
OS Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS18148.1, ECO:0000313|Proteomes:UP000016926};
RN [1] {ECO:0000313|EMBL:EMS18148.1, ECO:0000313|Proteomes:UP000016926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP11 {ECO:0000313|EMBL:EMS18148.1,
RC ECO:0000313|Proteomes:UP000016926};
RX PubMed=23047670; DOI=10.1038/ncomms2112;
RA Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA Ye M., Zou H., Zou H., Zhao Z.K.;
RT "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL Nat. Commun. 3:1112-1112(2012).
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 Evidence={ECO:0000256|ARBA:ARBA00000971,
CC ECO:0000256|PIRNR:PIRNR001473, ECO:0000256|PROSITE-ProRule:PRU00277};
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP3/4 subfamily.
CC {ECO:0000256|ARBA:ARBA00007838}.
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DR EMBL; KB722687; EMS18148.1; -; Genomic_DNA.
DR RefSeq; XP_016269267.1; XM_016420302.1.
DR AlphaFoldDB; M7XDC5; -.
DR GeneID; 27370655; -.
DR eggNOG; KOG0552; Eukaryota.
DR HOGENOM; CLU_022297_3_0_1; -.
DR OrthoDB; 25281at2759; -.
DR Proteomes; UP000016926; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 1.
DR Gene3D; 2.60.120.340; Nucleoplasmin core domain; 1.
DR InterPro; IPR041232; NPL.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR023566; PPIase_Fpr3/Fpr4-like.
DR PANTHER; PTHR43811:SF19; 39 KDA FK506-BINDING NUCLEAR PROTEIN; 1.
DR PANTHER; PTHR43811; FKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKPA; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR Pfam; PF17800; NPL; 1.
DR PIRSF; PIRSF001473; FK506-bp_FPR3; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|PIRNR:PIRNR001473, ECO:0000256|PROSITE-
KW ProRule:PRU00277};
KW Rotamase {ECO:0000256|PIRNR:PIRNR001473, ECO:0000256|PROSITE-
KW ProRule:PRU00277}.
FT DOMAIN 292..378
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT REGION 46..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..75
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..183
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 389 AA; 42150 MW; 21FCC9FED089166D CRC64;
MAQPLILGLW SIVLEPGKTY SQNTSPAIQI TNVSYGAEVK GNARSAVTMK YPEFEQDSDD
EEDDEEEEDE DEDDENIKLP KIITKEPVLA VLRPNAIEQA SINVTLVEDV EVVEFSVTGE
NPVHLVGHYV RQEDFDQPPS DYDSEEEYGS DFDDEDDFDS EGMSGLIDDD EEDDEDMEDA
ADRIQEIEEP KKAASKKRPA DETPAGADDS TVSAASVAGL SKNQKKKLAK KQKAENGEAV
APAAEEKKAA EPKKAEAKKD EPKKDTRKTQ VLAGGLEITD FKEGTGPAAK AGSKVGMRYI
GKLDNGKVFD SNTKGAPLVF NLGRGQVIKG WDLGVVGMKV GGERKLVIPA ALAYGKQKIP
GIPPNSRLTF DVKLLSLSPS SSSSSSSRR
//
