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Database: UniProt
Entry: F4WK86_ACREC
LinkDB: F4WK86_ACREC
Original site: F4WK86_ACREC 
ID   F4WK86_ACREC            Unreviewed;       162 AA.
AC   F4WK86;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU363014};
DE            EC=5.2.1.8 {ECO:0000256|RuleBase:RU363014};
GN   ORFNames=G5I_06137 {ECO:0000313|EMBL:EGI65389.1};
OS   Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS   echinatior).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Acromyrmex.
OX   NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN   [1] {ECO:0000313|EMBL:EGI65389.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Nygaard S., Zhang G.;
RT   "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT   adaptations to social evolution and fungus farming.";
RL   Submitted (FEB-2011) 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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000971,
CC         ECO:0000256|RuleBase:RU363014};
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DR   EMBL; GL888197; EGI65389.1; -; Genomic_DNA.
DR   RefSeq; XP_011054548.1; XM_011056246.1.
DR   AlphaFoldDB; F4WK86; -.
DR   STRING; 103372.F4WK86; -.
DR   EnsemblMetazoa; XM_011056246.1; XP_011054548.1; LOC105146160.
DR   GeneID; 105146160; -.
DR   KEGG; aec:105146160; -.
DR   eggNOG; KOG3259; Eukaryota.
DR   InParanoid; F4WK86; -.
DR   OrthoDB; 417859at2759; -.
DR   Proteomes; UP000007755; Unassembled WGS sequence.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR   GO; GO:0051171; P:regulation of nitrogen compound metabolic process; IEA:UniProt.
DR   GO; GO:0080090; P:regulation of primary metabolic process; IEA:UniProt.
DR   CDD; cd00201; WW; 1.
DR   Gene3D; 2.20.70.10; -; 1.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR000297; PPIase_PpiC.
DR   InterPro; IPR023058; PPIase_PpiC_CS.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   PANTHER; PTHR10657; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR   PANTHER; PTHR10657:SF4; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-RELATED; 1.
DR   Pfam; PF00639; Rotamase; 1.
DR   Pfam; PF00397; WW; 1.
DR   SMART; SM00456; WW; 1.
DR   SUPFAM; SSF54534; FKBP-like; 1.
DR   SUPFAM; SSF51045; WW domain; 1.
DR   PROSITE; PS01096; PPIC_PPIASE_1; 1.
DR   PROSITE; PS50198; PPIC_PPIASE_2; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
PE   4: Predicted;
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW   ECO:0000256|RuleBase:RU363014};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007755};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW   ECO:0000256|RuleBase:RU363014}.
FT   DOMAIN          4..38
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          51..162
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
FT   REGION          28..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   162 AA;  17954 MW;  C780AD858888D68A CRC64;
     MADEELPAGW EKRLSRSTGQ HYYLNIYTKE SQWDRPDKPA DPSGNGKTDG PEEVQCSHLL
     VKHSGSRRPS SWREENITRS KEEALDLVKS YREQIASGKA TFAELASKYS DCSSAKRGGD
     LGPFSRGAMQ KPFEQAAFAL KVGELSSPVH TDSGIHIIQR TA
//
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