FKBP4_EMENI
ID FKBP4_EMENI Reviewed; 479 AA.
AC P0C1B0; C8V696; Q5B6C2;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 2.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=FK506-binding protein 4;
DE EC=5.2.1.8 {ECO:0000250|UniProtKB:Q06205};
DE AltName: Full=Histone proline isomerase {ECO:0000250|UniProtKB:Q06205};
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase;
DE Short=PPIase;
DE AltName: Full=Rotamase;
GN Name=fpr4; ORFNames=AN10489;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP REVISION OF GENE MODEL.
RA Pemberton T.J.;
RL Submitted (FEB-2006) to UniProtKB.
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:0000250|UniProtKB:Q06205}.
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:0000250|UniProtKB:Q06205};
CC -!- ACTIVITY REGULATION: Inhibited by both FK506 and rapamycin.
CC {ECO:0000250}.
CC -!- SUBUNIT: Binds to histones H3 and H4. {ECO:0000250|UniProtKB:Q06205}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q06205}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP3/4 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA59217.1; Type=Erroneous gene model prediction; Note=The predicted gene AN3908 has been split into 2 genes: AN10489 and AN10485.; Evidence={ECO:0000305};
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DR EMBL; AACD01000064; EAA59217.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001302; CBF75117.1; -; Genomic_DNA.
DR RefSeq; XP_661512.1; XM_656420.1.
DR AlphaFoldDB; P0C1B0; -.
DR SMR; P0C1B0; -.
DR STRING; 162425.CADANIAP00004789; -.
DR EnsemblFungi; CBF75117; CBF75117; ANIA_10489.
DR EnsemblFungi; EAA59217; EAA59217; AN3908.2.
DR GeneID; 2873328; -.
DR KEGG; ani:AN3908.2; -.
DR VEuPathDB; FungiDB:AN10489; -.
DR eggNOG; KOG0552; Eukaryota.
DR HOGENOM; CLU_005146_1_0_1; -.
DR InParanoid; P0C1B0; -.
DR OMA; CPPHMAY; -.
DR OrthoDB; 402681at2759; -.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 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 Pfam; PF00254; FKBP_C; 1.
DR Pfam; PF17800; NPL; 1.
DR PIRSF; PIRSF001473; FK506-bp_FPR3; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 3: Inferred from homology;
KW Chaperone; Isomerase; Nucleus; Reference proteome; Rotamase.
FT CHAIN 1..479
FT /note="FK506-binding protein 4"
FT /id="PRO_0000233081"
FT DOMAIN 393..479
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT REGION 39..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..94
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..255
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 479 AA; 52428 MW; B05A74B7F9C61A0B CRC64;
MMSGVQPVAV YALRVPADGA LVPAVPDAAA MFRVSMAAID PDEAPEFDDD SSRRPRATLR
IIRAPPGLDE EDSDDDYEDE DDSEDDSEDD EEVNGGPSDK EKARKLKEAA YLKELEDAMS
EDDESDEGEE FDLKAAISKL VKGKAPATDD DDEDAESDEG LDLDEMVVCT LDPERNYQQP
LDITVAEGER VFFKVTGTHT IYLTGNYVMP IDEPRDDYDE DDDEDEEDYD LSPDEDELDM
DELMMGEDDE SDDLDGLENP RITEIDTDEE EAPKLVDAKG KKKRGADEAA LEAKDDKAKS
AANGESKKQQ KKLKKNNGEA SAVEAKPEQK ETKKVQFAKN LEQGPTPSKE RKPDEKKPAD
KAEKTTGTLG VKEVKGVIID DKKLGKGPAA ASGNTVAMRY IGKLENGKVF DSNKKGKPFT
FKLGKGEVIK GWDIGVAGMA VGGERRITIP SHLAYGKKGV PGIPGNSKLI FDVKLLEIK
