ID   FKBP6_BOMMO             Reviewed;         437 AA.
AC   H9IWW7;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2012, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=Inactive peptidyl-prolyl cis-trans isomerase shutdown;
GN   Name=shu;
OS   Bombyx mori (Silk moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Bombycidae; Bombycinae; Bombyx.
OX   NCBI_TaxID=7091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=p50T;
RX   PubMed=19121390; DOI=10.1016/j.ibmb.2008.11.004;
RG   International Silkworm Genome Consortium;
RT   "The genome of a lepidopteran model insect, the silkworm Bombyx mori.";
RL   Insect Biochem. Mol. Biol. 38:1036-1045(2008).
RN   [2]
RP   INTERACTION WITH HSP83.
RX   PubMed=22902560; DOI=10.1016/j.molcel.2012.07.019;
RA   Xiol J., Cora E., Koglgruber R., Chuma S., Subramanian S., Hosokawa M.,
RA   Reuter M., Yang Z., Berninger P., Palencia A., Benes V., Penninger J.,
RA   Sachidanandam R., Pillai R.S.;
RT   "A role for Fkbp6 and the chaperone machinery in piRNA amplification and
RT   transposon silencing.";
RL   Mol. Cell 47:970-979(2012).
CC   -!- FUNCTION: Co-chaperone required during oogenesis to repress
CC       transposable elements and prevent their mobilization, which is
CC       essential for the germline integrity. Acts via the piRNA metabolic
CC       process, which mediates the repression of transposable elements during
CC       meiosis by forming complexes composed of piRNAs and Piwi proteins and
CC       govern the methylation and subsequent repression of transposons. Acts
CC       as a co-chaperone via its interaction with Hsp83/HSP90 and is required
CC       for the biogenesis of all three piRNA major populations (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with Hsp83. {ECO:0000269|PubMed:22902560}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FKBP6 family. {ECO:0000305}.
CC   -!- CAUTION: Although it contains a PPIase FKBP-type domain, does not show
CC       peptidyl-prolyl cis-trans isomerase activity. {ECO:0000305}.
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DR   AlphaFoldDB; H9IWW7; -.
DR   SMR; H9IWW7; -.
DR   STRING; 7091.BGIBMGA001750-TA; -.
DR   EnsemblMetazoa; BGIBMGA001750-RA; BGIBMGA001750-TA; BGIBMGA001750.
DR   eggNOG; KOG0543; Eukaryota.
DR   HOGENOM; CLU_047759_0_0_1; -.
DR   InParanoid; H9IWW7; -.
DR   OMA; GCPPRIK; -.
DR   Proteomes; UP000005204; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051879; F:Hsp90 protein binding; IPI:UniProtKB.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR   GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0034587; P:piRNA metabolic process; IEA:InterPro.
DR   Gene3D; 1.25.40.10; -; 1.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR042282; FKBP6/shu.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR013105; TPR_2.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR46674; PTHR46674; 1.
DR   Pfam; PF00254; FKBP_C; 1.
DR   Pfam; PF07719; TPR_2; 1.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
DR   PROSITE; PS50005; TPR; 2.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Differentiation; Meiosis; Oogenesis; Reference proteome; Repeat;
KW   RNA-mediated gene silencing; TPR repeat.
FT   CHAIN           1..437
FT                   /note="Inactive peptidyl-prolyl cis-trans isomerase
FT                   shutdown"
FT                   /id="PRO_0000428728"
FT   DOMAIN          92..178
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT   REPEAT          209..242
FT                   /note="TPR 1"
FT   REPEAT          258..294
FT                   /note="TPR 2"
FT   REPEAT          295..327
FT                   /note="TPR 3"
SQ   SEQUENCE   437 AA;  49155 MW;  32F0E70DD326BB18 CRC64;
     MEFQIDVDFQ NRKTEMFING DDDLFPEMGD EDDSDGEDTL RNIEETTKKM MLASPDYLSF
     EELGANMIDC MSTGDVKMLI IEEGKGPLVP VDSEVTIHYA AYWEKAVIPF DSTLTMNMGA
     PKRLRLGTGK IIPGLEIGLT MVKGPQARLN LLVQPAAAWG PRGVPPRIRP EPALFVIVLY
     DVKDNYAATR FNDLPMAEQT KYEVTLRTVN ALRADAKELY KKKKYVKAIK NYQQAISVLR
     LSRPGTADEE LDIKNNKVNA YLNLAVCYYK TNKPKHVLNM CECLDRLIDT EKHCKALYYY
     GKAHEMLGKT EMAIKYYKKA LKLEPKNKEI GKILADLDTK TKDFAVNEKA MWLKAFNVEV
     PATNAVYDVD ATFQSDVLDM CQSLAGRSEF AKFDLPVGLT KNEVDCIKGI VSDFGCLSVD
     VSGEGRNKKV CIVKKIV