GenomeNet

Database: UniProt
Entry: A0A2B4S7R4_STYPI
LinkDB: A0A2B4S7R4_STYPI
Original site: A0A2B4S7R4_STYPI 
ID   A0A2B4S7R4_STYPI        Unreviewed;       685 AA.
AC   A0A2B4S7R4;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE            EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
GN   Name=Nktr {ECO:0000313|EMBL:PFX24562.1};
GN   ORFNames=AWC38_SpisGene10823 {ECO:0000313|EMBL:PFX24562.1};
OS   Stylophora pistillata (Smooth cauliflower coral).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC   Astrocoeniina; Pocilloporidae; Stylophora.
OX   NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX24562.1, 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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000971};
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:PFX24562.1}.
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   EMBL; LSMT01000173; PFX24562.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B4S7R4; -.
DR   STRING; 50429.A0A2B4S7R4; -.
DR   EnsemblMetazoa; XM_022936594.1; XP_022792329.1; LOC111331472.
DR   OrthoDB; 2919818at2759; -.
DR   Proteomes; UP000225706; Unassembled WGS sequence.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   CDD; cd01926; cyclophilin_ABH_like; 1.
DR   Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR   PANTHER; PTHR11071:SF561; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE H; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; Cyclophilin-like; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   4: Predicted;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Reference proteome {ECO:0000313|Proteomes:UP000225706};
KW   Rotamase {ECO:0000256|ARBA:ARBA00023110}.
FT   DOMAIN          14..179
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50072"
FT   REGION          186..685
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..255
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..270
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        300..325
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        349..373
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        399..436
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        437..466
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        477..515
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        532..549
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        557..597
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        605..643
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        660..679
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   685 AA;  78212 MW;  31066D1E356D2F86 CRC64;
     MAVPKAKGYR PRCFFDVEIN GSLVGRVIFE LFADICPKTC DNFRALCTGE NGLSKVSGKT
     LHYKGSPFHR VIKNFMVQGG DFTKGNGTGG ESIYGGMFDD ESFEAKHDRA MLLSMANRGP
     NTNGSQFFIT TQPTPHLDGI HVVFGHVLQG HEVVSEIENQ KVDDKSRPQV DVKIANCGEL
     IPKAKAKAMA KKAEKKKKKR KESSTASESS SESDTDSEGE SSSDEKRKKK RSKKKKKEKR
     KDSAKKKGKK NKAKDKKMKE MKDGSDNEKS QKSPEPFSTV AADEIPDVPN NSFLFRRSRT
     PSPVREKRIA EGKDRRSKSP TTEKTSLRKS RVSQSGRILR GRGNMRYRTP PPSNESNSSV
     TRITPPWNRS LQRRSRSPPR RARSPRGRSR SPRDSSRSPR RRVSHRSNSP RSSRRRFKSP
     QRRSNSPRRS PKSPRRRSRS PQRELEKESQ AKQESSLKEI SKQTDHSSPD HTNPSNLTRT
     YRERDSGKRY DSEDSEPVTP HKNSFKKREI EEHGTTSPVT DSYKQVRNQK KRGLKSSSSS
     DSDEQQGNGN DGVLYLKRKR ANLELRSHSN STGRHSRSET RDYVEDSKTK QSLNEEGRIG
     HTDGPNVSIK HDEGKREYGE SNRDSVPQNR QQYKEDKHTN SDSSYSSDSD SDDSSERNRK
     SRHRHHRHRH HHHRHRHDRE RNSSL
//
DBGET integrated database retrieval system