ID K1VC32_TRIAC Unreviewed; 400 AA.
AC K1VC32;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=FK506-binding protein {ECO:0000256|PIRNR:PIRNR001473};
DE EC=5.2.1.8 {ECO:0000256|PIRNR:PIRNR001473};
GN ORFNames=A1Q2_07389 {ECO:0000313|EMBL:EKC98375.1};
OS Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Trichosporon.
OX NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKC98375.1, ECO:0000313|Proteomes:UP000006757};
RN [1] {ECO:0000313|EMBL:EKC98375.1, ECO:0000313|Proteomes:UP000006757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 8904 {ECO:0000313|EMBL:EKC98375.1,
RC ECO:0000313|Proteomes:UP000006757};
RX PubMed=23193141; DOI=10.1128/EC.00264-12;
RA Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT "Genome sequence of the Trichosporon asahii environmental strain CBS
RT 8904.";
RL Eukaryot. Cell 11:1586-1587(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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKC98375.1}.
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DR EMBL; AMBO01000391; EKC98375.1; -; Genomic_DNA.
DR AlphaFoldDB; K1VC32; -.
DR STRING; 1220162.K1VC32; -.
DR eggNOG; KOG0552; Eukaryota.
DR HOGENOM; CLU_022297_3_0_1; -.
DR InParanoid; K1VC32; -.
DR OMA; KVEMRYI; -.
DR OrthoDB; 25281at2759; -.
DR Proteomes; UP000006757; 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; 2.
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}; Reference proteome {ECO:0000313|Proteomes:UP000006757};
KW Rotamase {ECO:0000256|PIRNR:PIRNR001473, ECO:0000256|PROSITE-
KW ProRule:PRU00277}.
FT DOMAIN 314..400
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT REGION 56..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..123
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..191
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 400 AA; 43974 MW; E9E6F38843AFDB6F CRC64;
MSRLLAQEHP ANIQSLTLIP GEPIPLYVNR DFQITNAALA EDLLSETGRS VVKVTHNPIS
QSAFEEDSEF DSDEDDESFE GPEGDDDDEE SEDSEEQEGE DDDEEDDDED MEDDSDDEDD
LEETSVLCSL TAGKCEQAVL NLTFVEGEVV IFEVTGENAV HLMGNYVNQF PADDYSDSDS
EYESDDYDDL SLDDEDEFDV EEFDEEVEVA PKGKIELIEP ESKPSKQDKK RKAEEEAPAA
EEQELSKSQK KKLAKKAKLE EAAAANVKKE KEAAPKKESK KLSSPVSQLT PQTLPSGLII
EDVKQGNGPV AKPGKRLGMR YVGKLENGKQ FDANTSGKPF SFVLGRGEVI AGWDQGLAGM
AVGGERRLTI PAKLAYGKQR LPGIPPNSTL KFDVKLVSVN
//
