ID A0A2G5C363_AQUCA Unreviewed; 572 AA.
AC A0A2G5C363;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
DE EC=5.2.1.8 {ECO:0000256|PROSITE-ProRule:PRU00277};
GN ORFNames=AQUCO_10800020v1 {ECO:0000313|EMBL:PIA25734.1};
OS Aquilegia coerulea (Rocky mountain columbine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC Aquilegia.
OX NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA25734.1, ECO:0000313|Proteomes:UP000230069};
RN [1] {ECO:0000313|EMBL:PIA25734.1, ECO:0000313|Proteomes:UP000230069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT "WGS assembly of Aquilegia coerulea Goldsmith.";
RL Submitted (SEP-2017) 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};
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DR EMBL; KZ305124; PIA25734.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5C363; -.
DR STRING; 218851.A0A2G5C363; -.
DR InParanoid; A0A2G5C363; -.
DR OrthoDB; 25281at2759; -.
DR Proteomes; UP000230069; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 3.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR46512; PEPTIDYLPROLYL ISOMERASE; 1.
DR PANTHER; PTHR46512:SF9; TETRATRICOPEPTIDE REPEAT DOMAIN 9; 1.
DR Pfam; PF00254; FKBP_C; 3.
DR Pfam; PF00515; TPR_1; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF54534; FKBP-like; 3.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 3.
DR PROSITE; PS50005; TPR; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
KW Reference proteome {ECO:0000313|Proteomes:UP000230069};
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 58..146
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT DOMAIN 174..263
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT DOMAIN 291..382
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT REPEAT 482..515
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 572 AA; 63989 MW; 069479CD8EC5151C CRC64;
MDEDFDFAGA GPEAMNEDMD FGDETPMFKV GEEKEIGKQG LKKKLIKEGE RFDTPDNGDE
VEVHYTGTLL DGTKFDSSRD RGTPFKFKLG QGQVIKGWDQ GIKTMKKGEN ALFTIPPELA
YGESGSPPTI PPNATLQFDV ELLSWSSVKD ICKDGGIFKK IVTEGEKWEN PKDLDEVFVK
YEARLEDGTL VSKSEGAEFT VKDGHFCPAL SKAVKTMKKG EKVILTVKPQ YGFGEMGRPA
SGAEGAVPPN ATLLITLELV SWKTVTEVTD DKKVIKKILK EGEGYERPND GTVAKVKLIG
KLQDGTVFFK KGHDDELFEF KTDEEQVITG LDRAVMTMKK GEVALLTIDP EYAFGSSESK
QDLAVVPPNS TVYYEVELES FVKEKESWDM NTPEKIEAAG KKKEEGNALF KAGKYARASK
RYEKAAKYID YDTNFSEEEK KQSKALKVSC NLNNAACKLK LKDYKQAEKL CTKVLEIEAQ
NVKALYRRAQ AYIQLVDLDL AELDIKKALE IDPNNRDVKL EYKVLKEKMK EYNKKDAQFY
GNIFAKMSKL ETLESNKATT KAAEPMTIDS KA
//
