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Database: UniProt
Entry: G5ELZ2_TOBAC
LinkDB: G5ELZ2_TOBAC
Original site: G5ELZ2_TOBAC 
ID   G5ELZ2_TOBAC            Unreviewed;       573 AA.
AC   G5ELZ2;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=peptidylprolyl isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
DE            EC=5.2.1.8 {ECO:0000256|PROSITE-ProRule:PRU00277};
GN   Name=FKBP62 {ECO:0000313|EMBL:BAL14273.1};
GN   Synonyms=LOC107824095 {ECO:0000313|RefSeq:XP_016506305.1};
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097 {ECO:0000313|EMBL:BAL14273.1};
RN   [1] {ECO:0000313|EMBL:BAL14273.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Ishikawa M., Iki T., Yoshikawa M., Meshi T.;
RT   "Cyclophilin 40 Facilitates HSP90-mediated RISC Assembly in Plants.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000084051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. TN90 {ECO:0000313|Proteomes:UP000084051};
RX   PubMed=24807620; DOI=10.1038/ncomms4833;
RA   Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA   Goepfert S., Peitsch M.C., Ivanov N.V.;
RT   "The tobacco genome sequence and its comparison with those of tomato and
RT   potato.";
RL   Nat. Commun. 5:3833-3833(2014).
RN   [3] {ECO:0000313|RefSeq:XP_016506305.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) 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};
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DR   EMBL; AB671736; BAL14273.1; -; mRNA.
DR   RefSeq; NP_001313055.1; NM_001326126.1.
DR   RefSeq; XP_016506305.1; XM_016650819.1.
DR   STRING; 4097.G5ELZ2; -.
DR   PaxDb; 4097-G5ELZ2; -.
DR   GeneID; 107824095; -.
DR   KEGG; nta:107824095; -.
DR   OMA; TVCQKKT; -.
DR   OrthoDB; 25281at2759; -.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW   ECO:0000313|RefSeq:XP_016506305.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000084051};
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          55..143
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
FT   DOMAIN          171..260
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
FT   DOMAIN          288..383
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
FT   REPEAT          483..516
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          553..573
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   573 AA;  63731 MW;  4B8166D810E8FF49 CRC64;
     MEEDFDIPPA EGMDEDMDLP DDPIMKVGEE KEIGNQGLKK KLVKEGEGWE TPEAGDEVEV
     HYTGTLLDGT KFDSSRDRGD PFKFTLGQGQ VIKGWDQGIK TMKKGENAIF TIPPELAYGE
     SGSPPTIPPN ATLQFDVELL SWVSVKDICK DGGIFKKILA EGEKWENPKD FDEVLVKYEA
     LLENGTVVGK SDGVEFTVQD GYFCPALAKA VKTMKKGEKV QLTVKPQYGF GEKGKPASSD
     GGAVPSNATL QINLELVSWK IVSSVTDDKK VVKKILKEGE GYEKPNEGAV VKLKLIGKLQ
     DGTVFIKKGH DGENEDELFE FKTDEEQVID GLDRAVMTMK KGEVALLTIA PEYAFGSSES
     KQDLAVIPPN STVHYEVELV SFVKDKESWD MNTPEKIEAA GKKKEEGNAL FKAGKYTRAS
     KRYEKAAKFI EYDTSFSEEE KKQSKALKIS CNLNNAACKL KLKDYKQAEK LCTKVLELES
     TNVKALYRRA QAYMNMADLD LAEFDIKKAL EIDPNNRDVK LEYKALKDKV KEFNKKDAKF
     YGNMFAKLNK LETANSSKSA PKEPEPMSID SKA
//
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