ID A0A2P6VMA6_9CHLO Unreviewed; 580 AA.
AC A0A2P6VMA6;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
DE EC=5.2.1.8 {ECO:0000256|PROSITE-ProRule:PRU00277};
GN ORFNames=C2E20_1809 {ECO:0000313|EMBL:PSC75187.1};
OS Micractinium conductrix.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Micractinium.
OX NCBI_TaxID=554055 {ECO:0000313|EMBL:PSC75187.1, ECO:0000313|Proteomes:UP000239649};
RN [1] {ECO:0000313|EMBL:PSC75187.1, ECO:0000313|Proteomes:UP000239649}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAG 241.80 {ECO:0000313|EMBL:PSC75187.1,
RC ECO:0000313|Proteomes:UP000239649};
RX PubMed=29178410; DOI=10.1111/tpj.13789;
RA Arriola M.B., Velmurugan N., Zhang Y., Plunkett M.H., Hondzo H.,
RA Barney B.M.;
RT "Genome sequences of Chlorella sorokiniana UTEX 1602 and Micractinium
RT conductrix SAG 241.80: implications to maltose excretion by a green alga.";
RL Plant J. 93:566-586(2018).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PSC75187.1}.
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DR EMBL; LHPF02000003; PSC75187.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P6VMA6; -.
DR STRING; 554055.A0A2P6VMA6; -.
DR Proteomes; UP000239649; 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; 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 SMART; SM00028; TPR; 2.
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 ECO:0000313|EMBL:PSC75187.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000239649};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00277};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT DOMAIN 60..148
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT DOMAIN 176..263
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT DOMAIN 291..375
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT REPEAT 392..425
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 545..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 580 AA; 61537 MW; 3D52731342F70873 CRC64;
MDGHFKTASQ LMAEGGAGSD IEDALSQPDA PGKVVKITED GGVVKEIVKP GTGWEEPEKG
DKVQVHYVGT LTDGTKFDSS RDRGDPFEFD LGMGSVIKGW DLGVATMKKG EISKLTITAD
YGYGASGSPP TIPGGATLVF EVELLSWKSV KDIAGDGGVI KTIVKEGTGW AKPLPADEVC
VHFSARVQGA AEPFYASPEQ GEEFSLSESL FCPAIGTAAK TMKKGEEVKL VVKPEYCFGD
EGRGSEVPPG AALEIDMTLL GWKKVEKVTD DGLILRKTLE DTEEWAKPNA GSKVTVTYTA
RVLPDGPVFD QKTAEEPLTF TTDEGEAPEA LELAVSKMKK GERCLVTVAP QYAQRLAAVP
PGASVEYDLT LVDFVKAKDS WEMDPAEKLA AAATLKDKGN ATFKAGEYSR AIGRYDKALQ
CIEHDDNFSS DEKKQARDVK KSCNLNLAAA HLKLNAPIAA RKAADKVLES DGANVKALYR
RAQAWLATAD FVEAEQDIRA GLAEDPNSTD FKLLLKKWKS AQAAAAKKEK GLWAGMMRGL
SVAGGEPKAE AAPTDAAAAE AEENAAANGD AGAAAEPMAA
//