ID A0A2B4RN23_STYPI Unreviewed; 381 AA.
AC A0A2B4RN23;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, 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 Name=FKBP6 {ECO:0000313|EMBL:PFX19011.1};
GN ORFNames=AWC38_SpisGene16607 {ECO:0000313|EMBL:PFX19011.1};
OS Stylophora pistillata (Smooth cauliflower coral).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC Astrocoeniina; Pocilloporidae; Stylophora.
OX NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX19011.1, ECO:0000313|Proteomes:UP000225706};
RN [1] {ECO:0000313|Proteomes:UP000225706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA Tambutte S., Allemand D., Aranda M.;
RT "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT digitifera provides evidence for extensive differences between species of
RT corals.";
RL bioRxiv 0:0-0(2017).
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 -!- 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:PFX19011.1}.
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DR EMBL; LSMT01000381; PFX19011.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B4RN23; -.
DR STRING; 50429.A0A2B4RN23; -.
DR EnsemblMetazoa; XM_022945274.1; XP_022801009.1; LOC111338750.
DR Proteomes; UP000225706; Unassembled WGS sequence.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 1.
DR Gene3D; 3.30.1370.50; R3H-like domain; 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; IPR036867; R3H_dom_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR013105; TPR_2.
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 Pfam; PF07719; TPR_2; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
DR PROSITE; PS50005; TPR; 2.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW ECO:0000313|EMBL:PFX19011.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000225706};
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 37..124
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT REPEAT 201..234
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 235..268
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ SEQUENCE 381 AA; 43880 MW; A7516D01E5BECC25 CRC64;
MYTPFQRLAR GMEDLTGDGG VFKRMIRKGT GPVVPEGATV RYHYNGYLEF NDEPFDSSRL
RNKPEIHKLE ENILGLYYGL RTMRKGEKSK FLVTPEYAYL EMGCTPRIPA SAKVLFEVEL
LSFIDHKAAD DFDAFTEEER KQASFEQLLE VANSEREAGN DFYKRKQVHR AVGKYLKAIK
LLENCHLQNA DQERWMNEVL LKLYLNAAHC FLELAEVKKV LTYARKALGI DPRNVKALYR
MGKALQKQGE FDSARDKFKK AQYYEPSNKA IKDALIELDR KVSHFQALEK QTFSRMFAPA
KKGKGKDEKS LQAPVNLKAG KKELLIKKLR EFKEDSYTQE ISFPTALTQQ ERAFIKQTAQ
ELGFKVEGKE GTNKELKVTK C
//