ID Q5ZJT4_CHICK Unreviewed; 442 AA.
AC Q5ZJT4;
DT 23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 129.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
DE EC=5.2.1.8 {ECO:0000256|PROSITE-ProRule:PRU00277};
GN ORFNames=RCJMB04_15n8 {ECO:0000313|EMBL:CAG32009.1};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000313|EMBL:CAG32009.1};
RN [1] {ECO:0000313|EMBL:CAG32009.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CB {ECO:0000313|EMBL:CAG32009.1};
RC TISSUE=Bursa {ECO:0000313|EMBL:CAG32009.1};
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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; AJ720350; CAG32009.1; -; mRNA.
DR RefSeq; NP_001006250.1; NM_001006250.1.
DR AlphaFoldDB; Q5ZJT4; -.
DR GeneID; 418261; -.
DR KEGG; gga:418261; -.
DR CTD; 2288; -.
DR VEuPathDB; HostDB:geneid_418261; -.
DR PhylomeDB; Q5ZJT4; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005528; F:FK506 binding; IDA:AgBase.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 2.
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 Pfam; PF00254; FKBP_C; 2.
DR Pfam; PF00515; TPR_1; 1.
DR Pfam; PF13174; TPR_6; 1.
DR SMART; SM00028; TPR; 2.
DR SUPFAM; SSF54534; FKBP-like; 2.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 2.
DR PROSITE; PS50005; TPR; 2.
PE 2: Evidence at transcript level;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
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 43..131
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT DOMAIN 160..246
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT REPEAT 312..345
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 346..379
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 415..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 442 AA; 50431 MW; 0D8BFBC21EDB92B8 CRC64;
MTADEMKADG APLEGTDITP KRDEGVLKVV KREGTGTESP MIGDKVTVHY TGWLLDGTKF
DSSLDRRDKF SFDLGKGEVI KAWDIAVATM KVGEICQITC KPEYAYGLAG SPPKIPPNAT
LIFEIELFEF KGEDLTDDED GGIIRRIRKK GEGYLKPNEG ALVEIQFEGR YRDRAFDKRE
LRFEIGEGDN YDLPHGLEKA IQKMEKSEES IFYLKPNYGF GSTGKEKFQI PPDAELQYEV
KLKSFEKAKE SWEMNTEEKL EQSCMVKERG TQYFKEGKYK RAALQYKKIV LWLEHESGLS
DEEDTKAKSL RLAAHLNLAM CHLKLKEYSQ ALENCNKALE LDSSNEKGLF RRGEAHLAVN
DFELARGDFQ KVIQLYPSNK AAKVQLVTCQ QKIREQHEKE KKMYANMFQR LADKELKPAT
TLQTSHTEDA EMKDEQNGVD DK
//
