ID F7IM70_CALJA Unreviewed; 296 AA.
AC F7IM70;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 2.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
DE EC=5.2.1.8 {ECO:0000256|PROSITE-ProRule:PRU00277};
GN Name=FKBP6 {ECO:0000313|Ensembl:ENSCJAP00000031178.2};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000031178.2, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000031178.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000031178.2}
RP IDENTIFICATION.
RG Ensembl;
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};
CC -!- SIMILARITY: Belongs to the FKBP6 family.
CC {ECO:0000256|ARBA:ARBA00009648}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; F7IM70; -.
DR Ensembl; ENSCJAT00000032948.3; ENSCJAP00000031178.2; ENSCJAG00000016944.5.
DR GeneTree; ENSGT00940000158514; -.
DR Proteomes; UP000008225; Chromosome 2.
DR Bgee; ENSCJAG00000016944; Expressed in ovary and 1 other cell type or tissue.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR042282; FKBP6/shu.
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; PTHR46674; INACTIVE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKBP6; 1.
DR PANTHER; PTHR46674:SF1; INACTIVE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKBP6; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00277};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803}.
FT DOMAIN 28..113
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 296 AA; 33424 MW; F1803A8622BAD536 CRC64;
MGGSALNQGV LEGDDAPGQS PYERLSQRML DISGDRGVLK DVIREGAGDL VAPDATVLDI
TLWGMELGLL SMRRGELARF LFKPTYAYGT LGCPPLIPPD TTVLFEIELL DFLDSAESDK
FCALSAEQQD QFPLQKVLKV AATEREFGNY LFRQNRFYDA KVRYKRALLL LHRRSAPPDE
QHLTEAAKLL ILLNLSFTYL KLDRPTLALR YGEQALIIDQ KNAKALFRCG QACLLLTEYQ
KARDFLVRAQ KEQPFNHDIN NELKKLASYY KDYTDKEKEM CHRMFAPCGD GSTVGS
//
