FKBP4_ASPOR
ID FKBP4_ASPOR Reviewed; 470 AA.
AC Q2UN37;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=AO090001000519;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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}.
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DR EMBL; AP007154; BAE57028.1; -; Genomic_DNA.
DR RefSeq; XP_001819030.1; XM_001818978.2.
DR AlphaFoldDB; Q2UN37; -.
DR SMR; Q2UN37; -.
DR STRING; 510516.Q2UN37; -.
DR PRIDE; Q2UN37; -.
DR EnsemblFungi; BAE57028; BAE57028; AO090001000519.
DR GeneID; 5991001; -.
DR KEGG; aor:AO090001000519; -.
DR VEuPathDB; FungiDB:AO090001000519; -.
DR HOGENOM; CLU_022297_3_1_1; -.
DR OMA; CPPHMAY; -.
DR Proteomes; UP000006564; Chromosome 2.
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..470
FT /note="FK506-binding protein 4"
FT /id="PRO_0000233075"
FT DOMAIN 384..470
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT REGION 40..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..92
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..132
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..252
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 470 AA; 51307 MW; BD9AF00FAD4B8892 CRC64;
MSVQPVAVYA LKVPAGGALI PAVPDAAAMF RVSMAAIDPD EEPDFDGHDT NQRPRATLRI
VRAPPGLDLE DDSDDDYEDV DSDEESDDEE PNGGPSDKEK ARKLKELAAL KEMEEAMDED
DEDEDEDEDG EFDLKAAISK LVKGKGPATD SDEDDEEDEG LELDEMVVCT LDTEKNLQQP
LDITVSEDER VFFKVTGTHT VYLTGNYVMP IDPHFHGEDE DEEDEDDYDL SPDEDELALD
LMGDDDNESD ELDGLENPRI TEVDSDEEPP KLVDTKGKNK RSAPADEEKP AKQANGEESL
SKKQQKKLKK NNGDAAAVEQ KKEAKEGKEA KKVQFAKNLE QGPTPSGQDK KPAEQTTGTL
GVKEVKGVKI DDKKLGKGPA AKAGNTVAMR YIGKLEDGKV FDANKKGKPF TFKLGKGEVI
KGWDIGVAGM AVGGERRISI PPHLAYGKKA LPGIPGNSKL IFDVKLLEIK
