FKB1A_ASPFU
ID FKB1A_ASPFU Reviewed; 112 AA.
AC Q4WLV6;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=FK506-binding protein 1A;
DE Short=FKBP;
DE EC=5.2.1.8;
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase;
DE Short=PPIase;
DE AltName: Full=Rapamycin-binding protein;
GN Name=fpr1A; ORFNames=AFUA_6G12170;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides (By similarity). {ECO:0000250}.
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 -!- ACTIVITY REGULATION: Inhibited by both FK506 and rapamycin.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AAHF01000006; EAL89058.1; -; Genomic_DNA.
DR RefSeq; XP_751096.1; XM_746003.1.
DR PDB; 5HWB; X-ray; 2.31 A; A/B=1-112.
DR PDB; 5HWC; X-ray; 2.05 A; A=1-112.
DR PDB; 5J6E; X-ray; 3.20 A; A/B=1-111.
DR PDB; 6TZ7; X-ray; 2.50 A; C=2-112.
DR PDB; 6VCV; X-ray; 1.60 A; A/B=1-112.
DR PDBsum; 5HWB; -.
DR PDBsum; 5HWC; -.
DR PDBsum; 5J6E; -.
DR PDBsum; 6TZ7; -.
DR PDBsum; 6VCV; -.
DR AlphaFoldDB; Q4WLV6; -.
DR SMR; Q4WLV6; -.
DR STRING; 746128.CADAFUBP00007619; -.
DR EnsemblFungi; EAL89058; EAL89058; AFUA_6G12170.
DR GeneID; 3508401; -.
DR KEGG; afm:AFUA_6G12170; -.
DR VEuPathDB; FungiDB:Afu6g12170; -.
DR eggNOG; KOG0544; Eukaryota.
DR HOGENOM; CLU_013615_12_1_1; -.
DR InParanoid; Q4WLV6; -.
DR OMA; GQTFPKT; -.
DR OrthoDB; 1328688at2759; -.
DR Proteomes; UP000002530; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:AspGD.
DR GO; GO:0005634; C:nucleus; IDA:AspGD.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR Pfam; PF00254; FKBP_C; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Isomerase; Reference proteome; Rotamase.
FT CHAIN 1..112
FT /note="FK506-binding protein 1A"
FT /id="PRO_0000233318"
FT DOMAIN 20..108
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:6VCV"
FT STRAND 22..31
FT /evidence="ECO:0007829|PDB:6VCV"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:6VCV"
FT TURN 40..44
FT /evidence="ECO:0007829|PDB:6VCV"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:6VCV"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:6VCV"
FT HELIX 58..63
FT /evidence="ECO:0007829|PDB:6VCV"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:6VCV"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:6VCV"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:6VCV"
FT TURN 82..86
FT /evidence="ECO:0007829|PDB:6VCV"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:6VCV"
FT STRAND 98..107
FT /evidence="ECO:0007829|PDB:6VCV"
SQ SEQUENCE 112 AA; 12130 MW; FE59C09795C8E07E CRC64;
MGVTKELKSP GNGVDFPKKG DFVTIHYTGR LTDGSKFDSS VDRNEPFQTQ IGTGRVIKGW
DEGVPQMSLG EKAVLTITPD YGYGARGFPP VIPGNSTLIF EVELLGINNK RA
