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Database: UniProt
Entry: C4R2G3_KOMPG
LinkDB: C4R2G3_KOMPG
Original site: C4R2G3_KOMPG 
ID   C4R2G3_KOMPG            Unreviewed;       411 AA.
AC   C4R2G3;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=FK506-binding protein {ECO:0000256|PIRNR:PIRNR001473};
DE            EC=5.2.1.8 {ECO:0000256|PIRNR:PIRNR001473};
GN   OrderedLocusNames=PAS_chr2-2_0476 {ECO:0000313|EMBL:CAY69687.1};
OS   Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=644223 {ECO:0000313|EMBL:CAY69687.1, ECO:0000313|Proteomes:UP000000314};
RN   [1] {ECO:0000313|EMBL:CAY69687.1, ECO:0000313|Proteomes:UP000000314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GS115 / ATCC 20864 {ECO:0000313|Proteomes:UP000000314};
RX   PubMed=19465926; DOI=10.1038/nbt.1544;
RA   De Schutter K., Lin Y.C., Tiels P., Van Hecke A., Glinka S.,
RA   Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT   "Genome sequence of the recombinant protein production host Pichia
RT   pastoris.";
RL   Nat. Biotechnol. 27:561-566(2009).
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; FN392320; CAY69687.1; -; Genomic_DNA.
DR   RefSeq; XP_002491967.1; XM_002491922.1.
DR   AlphaFoldDB; C4R2G3; -.
DR   SMR; C4R2G3; -.
DR   STRING; 644223.C4R2G3; -.
DR   EnsemblFungi; CAY69687; CAY69687; PAS_chr2-2_0476.
DR   GeneID; 8198636; -.
DR   KEGG; ppa:PAS_chr2-2_0476; -.
DR   eggNOG; KOG0552; Eukaryota.
DR   HOGENOM; CLU_022297_3_1_1; -.
DR   InParanoid; C4R2G3; -.
DR   OMA; DEPNGGP; -.
DR   OrthoDB; 25281at2759; -.
DR   Proteomes; UP000000314; Chromosome 2.
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:UP000000314};
KW   Rotamase {ECO:0000256|PIRNR:PIRNR001473, ECO:0000256|PROSITE-
KW   ProRule:PRU00277}.
FT   DOMAIN          325..411
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          37..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          172..299
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..81
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..106
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..134
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..230
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        231..299
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   411 AA;  45679 MW;  7CB57D64E8809296 CRC64;
     MSSLIPLSSY NLALEPFNPT PALEEDFPVT IRITLAALDP EAIDEKAEPS TLRILKKSNL
     FGDESDSEDE SDEEDAEEEE EEEPKKKIQP KKVSKKSKKD DKLVDDSAEE SENDDEESDE
     DGSDLEDDEE IEEFVLCTLG PKIQYQQTID LTITPDEEVY FVVTGSYPIH LTGNYVEHPY
     DDESDQDDED DSDEDYDLTP DEDEIISDGG DYEIDDLDDV DDVEGKIEEI VEEEEEKKKN
     KEEIKSPKKD KKRPAEPVEA PVEEPKKSKK AKKEKNVEFT KDLEQGPTSK KETSGDKKKF
     PTKTLAGGLV IEDRTIGKGQ TAKSGNKVGV RYIGKLKNGK VFDKNTSGKP FVFGLGKGEV
     IKGWDVGVAG MAIGGERRII VPASMAYGKK SLPGIPANSE LTFDVKLVSL K
//
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