FKBP5_DICDI
ID FKBP5_DICDI Reviewed; 1622 AA.
AC Q54G21;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=FK506-binding protein 5;
DE EC=5.2.1.8;
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase;
DE Short=PPIase;
DE AltName: Full=Rotamase;
GN Name=fkbp5; ORFNames=DDB_G0290433;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP PROTEIN SEQUENCE OF 311-317; 588-597; 661-672; 699-708 AND 876-889,
RP METHYLATION AT ARG-314, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Bienvenut W.V., Veltman D.M., Insall R.H.;
RL Submitted (JAN-2010) to UniProtKB.
CC -!- FUNCTION: PPIases accelerate the folding of proteins by catalyzing the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. {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 -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
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DR EMBL; AAFI02000163; EAL62232.1; -; Genomic_DNA.
DR RefSeq; XP_635751.1; XM_630659.1.
DR AlphaFoldDB; Q54G21; -.
DR SMR; Q54G21; -.
DR STRING; 44689.DDB0233865; -.
DR PaxDb; Q54G21; -.
DR EnsemblProtists; EAL62232; EAL62232; DDB_G0290433.
DR GeneID; 8627670; -.
DR KEGG; ddi:DDB_G0290433; -.
DR dictyBase; DDB_G0290433; -.
DR eggNOG; KOG0552; Eukaryota.
DR eggNOG; KOG4725; Eukaryota.
DR HOGENOM; CLU_243514_0_0_1; -.
DR InParanoid; Q54G21; -.
DR OMA; AGWLENN; -.
DR PhylomeDB; Q54G21; -.
DR PRO; PR:Q54G21; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005527; F:macrolide binding; IBA:GO_Central.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; 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 Coiled coil; Direct protein sequencing; Isomerase; Methylation;
KW Reference proteome; Rotamase.
FT CHAIN 1..1622
FT /note="FK506-binding protein 5"
FT /id="PRO_0000331284"
FT DOMAIN 178..269
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT REGION 268..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1043..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1122..1622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 607..827
FT /evidence="ECO:0000255"
FT COILED 854..961
FT /evidence="ECO:0000255"
FT COMPBIAS 273..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1096
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1150..1172
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1184..1200
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1263
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1264..1293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1294..1308
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1309..1324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1354..1368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1381..1405
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1416..1453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1454..1468
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1480..1507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1545..1570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1577..1608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 314
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|Ref.2"
SQ SEQUENCE 1622 AA; 181595 MW; D573095ABECAA4C1 CRC64;
MNFSEEEEYS NRNAASSQKL GSLFKDNNAM SGNQSLQYTN NKTQSSANSN SPDVLISFPI
HLYKFDNNKN EYVSSGSIAT AIVGYKSSGK YQLLAYDNNK NYIVTVNITA QFNYSVTTIY
GSFTDGNGQN WSMTFNSAEE STKYATHVAI AKCASGGYQQ ITFVDINNQS KTKPVANGDR
VSIKYAGWLE NNQRVGSLFD SNLQSETPFR FVVGEGKVIK GWDLGVIGMR KSAKRILVIP
SELAYGKKGH STIPPNTNLI FDLEVTGSKK KEGSEPSLPS LNGQPSNAPQ QSLPTQLFDN
SPVPQDDKAN LLQRVAKLGR ATGFTSPPPS DSENESNSRN SHSNNSHNNN NNNNSNSNNN
SNSNSNNNNN NNNQNNNNNN NNQNNNQNNN NNNNYNNNNN NNNGYNNNNN NNGYNNNNNY
NNNMNNNNGF NNGMNNGFGN NSMNGMNNGF NNGMNGMNNG MNGGFGMNGN MYTSSQSPQF
NPMGTFGSAY NQQQALIGSG ALVPIMPQHQ QPSIIVASPP PPVQQAPPPT PAPAPPPPTP
VIVQAPPAPV QSTTETIQIL VEEKQFKKEI KHSIDQFNSK LDQVSSKFDS LAQPIVKGDV
PISGVLLVQT LHRLVEDNEK LIKENVEKEN RMVTLKENIA TLHKKNEQFL EENTKMMESR
NEAITDNVAQ MRRQIIDLQK QKTLVEDDLA DKQMLHTKSQ SVINQLKRDY NTLQEELNSA
KEENQKSIQD QEALKQAEKD YALKIRAFKK SLLDEKNARK SDIEKINSLE DELKDAQDSL
TQAEKSNEES LKRLKLDMVR IKKRNDDKVS QLTLEITTLK DTLETERSAL SSVQTLVENT
RLETESKFNL LLIKKEEAIA AAELSLSEEQ SKYNKLVQSN NQQIDQLQKL IDDAKKKLDH
EKEEVIKSYK KGFAEGIEST KQENDLITTL QQQIQQLTTQ YDDTKKSLIE TKEKLSTLES
QPPKTIVKEV IVKVPSDGTT VAVASSNNVD VAKEVKVCMQ KVFVQVSESF DEDEEYSTDS
IMSTFKDVIK RVTVEYIQEQ KEKQQQQQEK EEEEVVEEEE KEEEEKEEEE KEEEEKEEEK
EEEKEQEEEE EEKEVVVEEI VTIAEEVKEE EVVVEEPVTV VEEVKEEKPT PAIEEPVVAK
SQTVVDPLST KDDEDDDDDE DDYDDINEED LKNIDAEIEK MQQEMGDELE DDDDEEEEKE
KETAPVVTKS EVVDPLSSTK EESEEEEEEE TKVEVPVLEE EKEEEETKVE VPVLEDEQED
KVESDVEEKI VEPPTLDEDD FEKVEVPVLG DDEQDEKVVE EPAPEEEEET KVEVPVLNKD
DDEDNEKDVA SDSEETPSTP PPIDDVEEEE EKEEKVVEQV KEEINETKFE SSPFAVDEPT
TTEEKEEEKE EEKVEEEEEK VVEPPTIDDD ETTAPVIPSI DNSPRQTTTE EEESSTTAAT
TSTTTTSSTP VKPDEADTTK KTPKKTSFFD FDDSPFSAET ETETKSTAAS SDPFADTTSS
TPTSTKKKDF FSTDDDSLFG NSSDIFDKPS TTTKKDPFDT DSTDDLFGSI KTNKESTSTA
SSTSNGGLFD SDSLFGGISV AKSNNNTPSR QKQDFSSLFG SDPTISPLTE TEPEEKEIVL
PL
