ID H1W3Q0_COLHI Unreviewed; 474 AA.
AC H1W3Q0;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=FK506-binding protein {ECO:0000256|PIRNR:PIRNR001473};
DE EC=5.2.1.8 {ECO:0000256|PIRNR:PIRNR001473};
GN ORFNames=CH063_04047 {ECO:0000313|EMBL:CCF47113.1};
OS Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum destructivum species complex.
OX NCBI_TaxID=759273 {ECO:0000313|EMBL:CCF47113.1, ECO:0000313|Proteomes:UP000007174};
RN [1] {ECO:0000313|Proteomes:UP000007174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000007174};
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(2012).
CC -!- FUNCTION: PPIase that acts as a histone chaperone. Histone proline
CC isomerase that increases the rate of cis-trans isomerization at
CC prolines on the histone H3 N-terminal tail. Proline isomerization
CC influences H3 methylation thereby regulating gene expression.
CC {ECO:0000256|ARBA:ARBA00002221}.
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 -!- SUBUNIT: Binds to histones H3 and H4. {ECO:0000256|ARBA:ARBA00011865}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP3/4 subfamily.
CC {ECO:0000256|ARBA:ARBA00007838}.
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DR EMBL; CACQ02009379; CCF47113.1; -; Genomic_DNA.
DR STRING; 759273.H1W3Q0; -.
DR EnsemblFungi; CCF47113; CCF47113; CH063_04047.
DR VEuPathDB; FungiDB:CH63R_01064; -.
DR eggNOG; KOG0552; Eukaryota.
DR HOGENOM; CLU_022297_3_1_1; -.
DR Proteomes; UP000007174; 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 388..474
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT REGION 66..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..174
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..272
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 474 AA; 51274 MW; 3E585E00C018B20A CRC64;
MAQLPVALYG LEIPPGEVLI PASPDFPATF RITMAAIDPT EAPEADADGN IPTIPRSTLR
LVKQRFGDDL EANEDDEIDE DYLKSLLAAN GDEESSDDDD EPNGGPSDPS KKQKQAESLK
KLIEAXTAEE SDEDMDDAKP NGKSSKKGKA KASDDDDEED EEDSEDEDDD GLDLENFVLC
TLDTERNYQQ PLDITVQEGE KVFFVVSGTH TVHLTGNYVI DDEEEGSDED EDDEDGEYDL
SPDELEYGMD GLSDEDSDEL DDTADPRVME VDTDEEEAPK LVEAGKKGKK RAAESLDDLI
KADAADSKLS KKDKKKLKNN KGEAVATEEK TTPKSDKKVQ FAKNLEQGPT GSAEKAKQAS
KPAAGVKVVQ GVTIDDRKVG SGRAVKSGDT VGVRYIGKLD DGKVFDANKK GKPFSFKAGK
GQVIKGWDIG VLGMTIGGER RLTIPAHLAY GSKSLPGIPA NSTLTFDVKL LEIK
//
