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Database: UniProt
Entry: T1HUG5_RHOPR
LinkDB: T1HUG5_RHOPR
Original site: T1HUG5_RHOPR 
ID   T1HUG5_RHOPR            Unreviewed;       309 AA.
AC   T1HUG5;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=peptidylprolyl isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
DE            EC=5.2.1.8 {ECO:0000256|PROSITE-ProRule:PRU00277};
DE   Flags: Fragment;
OS   Rhodnius prolixus (Triatomid bug).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC   Cimicomorpha; Reduviidae; Triatominae; Rhodnius.
OX   NCBI_TaxID=13249 {ECO:0000313|EnsemblMetazoa:RPRC007685-PA, ECO:0000313|Proteomes:UP000015103};
RN   [1] {ECO:0000313|Proteomes:UP000015103}
RP   NUCLEOTIDE SEQUENCE.
RA   Wilson R.K., Warren W., Dotson E., Oliveira P.L.;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:RPRC007685-PA}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (MAY-2015) to UniProtKB.
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; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU00277};
CC   -!- SIMILARITY: Belongs to the FKBP6 family.
CC       {ECO:0000256|ARBA:ARBA00009648}.
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DR   EMBL; ACPB03005527; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; T1HUG5; -.
DR   STRING; 13249.T1HUG5; -.
DR   EnsemblMetazoa; RPRC007685-RA; RPRC007685-PA; RPRC007685.
DR   VEuPathDB; VectorBase:RPRC007685; -.
DR   eggNOG; KOG0543; Eukaryota.
DR   HOGENOM; CLU_013615_13_2_1; -.
DR   InParanoid; T1HUG5; -.
DR   OMA; ACYVEER; -.
DR   OrthoDB; 7173at2759; -.
DR   Proteomes; UP000015103; Unassembled WGS sequence.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.50.40; -; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 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; INACTIVE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKBP6; 1.
DR   PANTHER; PTHR46674:SF1; INACTIVE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKBP6; 1.
DR   Pfam; PF00254; FKBP_C; 1.
DR   Pfam; PF07719; TPR_2; 1.
DR   SMART; SM00028; TPR; 2.
DR   SUPFAM; SSF54534; FKBP-like; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
DR   PROSITE; PS50005; TPR; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015103};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00277};
KW   TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW   ProRule:PRU00339}.
FT   REPEAT          240..273
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ   SEQUENCE   309 AA;  35330 MW;  F1FBE6A92E9D865F CRC64;
     IQPYREISKI MMDLFDNGKI KKLIIEHGTG EVVPFNASVY LHYACYVEER KDPFDASMFR
     SSIPKHYQMG GGYLFAGFEI ALSSMKEYEV AQFLIHPDYA FGALGCPPRI PGNAPVMLVL
     TVTGFIDCGF VTLQKRDKPL EPCSFSEKLK IAKSHSALAK DYYKHDRIKM AFNHFREAQY
     SLDKEADLKS EEEERKAFLL KSFINQMMCL SHPKYLKPKK LIETADRAEK ELSYLLQKNA
     KYHYCLGIAY THLQDFSAAA KSFRKAQAIS PFLPRLSQAV KFLHEKAGKA LKDEKVMWQG
     AFNKLGYSS
//
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