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Database: UniProt
Entry: M1D260_SOLTU
LinkDB: M1D260_SOLTU
Original site: M1D260_SOLTU 
ID   M1D260_SOLTU            Unreviewed;       485 AA.
AC   M1D260;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   RecName: Full=FK506-binding protein {ECO:0000256|PIRNR:PIRNR001473};
DE            EC=5.2.1.8 {ECO:0000256|PIRNR:PIRNR001473};
GN   Name=102579636 {ECO:0000313|EnsemblPlants:PGSC0003DMT400079626};
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400079626, ECO:0000313|Proteomes:UP000011115};
RN   [1] {ECO:0000313|Proteomes:UP000011115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX   PubMed=21743474; DOI=10.1038/nature10158;
RG   The Potato Genome Sequencing Consortium;
RT   "Genome sequence and analysis of the tuber crop potato.";
RL   Nature 475:189-195(2011).
RN   [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400079626}
RP   IDENTIFICATION.
RC   STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400079626};
RG   EnsemblPlants;
RL   Submitted (JUN-2015) to UniProtKB.
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.
CC       {ECO:0000256|PIRNR:PIRNR001473}.
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DR   RefSeq; XP_006348066.1; XM_006348004.2.
DR   AlphaFoldDB; M1D260; -.
DR   STRING; 4113.M1D260; -.
DR   PaxDb; 4113-PGSC0003DMT400079626; -.
DR   EnsemblPlants; PGSC0003DMT400079626; PGSC0003DMT400079626; PGSC0003DMG400031007.
DR   GeneID; 102579636; -.
DR   Gramene; PGSC0003DMT400079626; PGSC0003DMT400079626; PGSC0003DMG400031007.
DR   KEGG; sot:102579636; -.
DR   eggNOG; KOG0552; Eukaryota.
DR   HOGENOM; CLU_022297_1_1_1; -.
DR   InParanoid; M1D260; -.
DR   OMA; GESEDCC; -.
DR   OrthoDB; 317095at2759; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; M1D260; baseline.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR   Gene3D; 3.10.50.40; -; 1.
DR   Gene3D; 2.60.120.340; Nucleoplasmin core domain; 1.
DR   InterPro; IPR041232; NPL.
DR   InterPro; IPR036824; Nucleoplasmin_core_dom_sf.
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   SUPFAM; SSF69203; Nucleoplasmin-like core domain; 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:UP000011115};
KW   Rotamase {ECO:0000256|PIRNR:PIRNR001473, ECO:0000256|PROSITE-
KW   ProRule:PRU00277}.
FT   DOMAIN          397..485
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
FT   REGION          104..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..142
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..197
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..329
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        338..366
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   485 AA;  53613 MW;  4AFD4814B834E8EF CRC64;
     MAFWGVELKS GKPFTHNFEK ERGRLHISQA TLGSGSSNKK SIVQCKVGDK EPIYVCSLLP
     EKLETCPLNL EFEEDEDVTF SVIGSHNVHL SGFFYGESED CCGDEHGSDY EEGASETDSA
     SDDSFEFNYD TEDEDEDGST DNDDFIMYPP SPIPNSGVRI EEILEDEKPT DENGTSKKPK
     KKKNQSKGID DSERQIVVKG NTDSPQMESE DEDGFPISAP SENKTKSVRS QKSDGTKDQD
     TGEEAGEKKG LKKRLRDDTG KANDQQREDN AKQNKKNKKK KVVDGEESVR EDVLKSSANP
     EHVEGNDEAV SVGKTEDGQK PTNEKDTEKK KKKKKNKKNQ QDGEAVTEVE KDKKNESHEV
     QEENAGTKPS HARTFGNGLV IEELAMGKPD GKKASPGKKV GVRYTGKLKK NGKIFDSNIG
     KRPFEFRLGI GQVIKGWDVG VNGMRVGDKR RITIPPAMGY GAKGAGRDIP PNSWLVFDVE
     LVNVN
//
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