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Database: UniProt
Entry: A0A151WU13_9HYME
LinkDB: A0A151WU13_9HYME
Original site: A0A151WU13_9HYME 
ID   A0A151WU13_9HYME        Unreviewed;       444 AA.
AC   A0A151WU13;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=peptidylprolyl isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
DE            EC=5.2.1.8 {ECO:0000256|PROSITE-ProRule:PRU00277};
GN   ORFNames=ALC60_09615 {ECO:0000313|EMBL:KYQ51324.1};
OS   Trachymyrmex zeteki.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Trachymyrmex.
OX   NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ51324.1, ECO:0000313|Proteomes:UP000075809};
RN   [1] {ECO:0000313|EMBL:KYQ51324.1, ECO:0000313|Proteomes:UP000075809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ51324.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYQ51324.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Trachymyrmex zeteki WGS genome.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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; KQ982748; KYQ51324.1; -; Genomic_DNA.
DR   RefSeq; XP_018309319.1; XM_018453817.1.
DR   RefSeq; XP_018309320.1; XM_018453818.1.
DR   RefSeq; XP_018309321.1; XM_018453819.1.
DR   AlphaFoldDB; A0A151WU13; -.
DR   STRING; 64791.A0A151WU13; -.
DR   GeneID; 108726322; -.
DR   OrthoDB; 7173at2759; -.
DR   Proteomes; UP000075809; 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; 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; PF13181; TPR_8; 1.
DR   SUPFAM; SSF54534; FKBP-like; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
DR   PROSITE; PS50005; TPR; 1.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW   ECO:0000313|EMBL:KYQ51324.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075809};
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   DOMAIN          112..201
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
FT   REPEAT          307..340
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ   SEQUENCE   444 AA;  51410 MW;  CDA8E0107F1966D1 CRC64;
     MAKNINPLVD GFRIGDLINE DGVMFEIGDD INNNEDDEEF SYSPHVQFSN EEMLNMLNMN
     SIEDEDEDEK ETVSLCGMSF SKLKTKMTSL TPNGKVMKYV KQRGVGEIIP NNAQAIVHYI
     GYFEYRDEPF DSTYSIGKPR SLRLGQSFII PGLEIGIRSM QKHEIAIFLI HPDYAYKAVG
     CPPRIPPNEE VIFVVQLVDY IDDGCAQTYK NFTEEEKQSF RYVVQPVKHM FVAAKDYCTK
     FNYKQAIREY RKIADCLESI KLQNDLEEKE MSELLSRAYT NLGICHNKEN MPTKACLALR
     KVPKPTAKSY YHYGQALLNI GEYNEAMKAF QKAWVLEPHD DSIRKAIRIT NVKQREYLEI
     EKRLWKNCFR SNEEQIKVNE FRKAARDLCE RLINSNDAVR QNLSEGFTKE EYEIIREEAA
     ILGLNVVTSV RYGKETIFLQ KSKS
//
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