ID A0A194RMQ4_PAPMA Unreviewed; 783 AA.
AC A0A194RMQ4;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
GN ORFNames=RR48_10648 {ECO:0000313|EMBL:KPJ18704.1};
OS Papilio machaon (Old World swallowtail butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Papilionidae; Papilioninae; Papilio.
OX NCBI_TaxID=76193 {ECO:0000313|EMBL:KPJ18704.1, ECO:0000313|Proteomes:UP000053240};
RN [1] {ECO:0000313|EMBL:KPJ18704.1, ECO:0000313|Proteomes:UP000053240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ya'a_city_454_Pm {ECO:0000313|EMBL:KPJ18704.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KPJ18704.1};
RX PubMed=26354079; DOI=10.1038/ncomms9212;
RA Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA Wang W.;
RT "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL Nat. Commun. 6:8212-8212(2015).
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 ---------------------------------------------------------------------------
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; KQ459989; KPJ18704.1; -; Genomic_DNA.
DR RefSeq; XP_014371224.1; XM_014515738.1.
DR AlphaFoldDB; A0A194RMQ4; -.
DR STRING; 76193.A0A194RMQ4; -.
DR GeneID; 106720933; -.
DR KEGG; pmac:106720933; -.
DR InParanoid; A0A194RMQ4; -.
DR OrthoDB; 169228at2759; -.
DR Proteomes; UP000053240; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd01921; cyclophilin_RRM; 1.
DR CDD; cd12235; RRM_PPIL4; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR035542; CRIP.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR035538; Cyclophilin_PPIL4.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR45843; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-LIKE 4; 1.
DR PANTHER; PTHR45843:SF1; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-LIKE 4; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR Pfam; PF00076; RRM_1; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS50102; RRM; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:KPJ18704.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053240};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00176}; Rotamase {ECO:0000256|ARBA:ARBA00023110}.
FT DOMAIN 1..161
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT DOMAIN 240..318
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 164..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..666
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..690
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..783
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 783 AA; 89944 MW; BA173B453E7CB184 CRC64;
MAVVIETTLG DITVDLYLEQ RPVTCLNFLK LCKMKYYNYN LFHSIRSGFI AQTGDPTGEG
SGGVSIWGLI EGPQKRFFSG EKMPKIRHTD AGLLAMVCTD DMMVGSQFYF TLAPDLDSLD
GVHCVIGEVT EGREILSKLN EVICDETHRP YQDVRITHTV VLEDPFRDPP GLTPPSRSPS
PSAERLKGGR IAPDEEIDET QGRTAEEIQE MVEEKEAKAR ATILEIVGDL PDADIAPPEN
VLFVCKLNPV TTDDDLEIIF SRFGKIVSCE VIRDKKTGDS LQYAFIEFAD KQSCEDAYFK
MDNVLIDDRR IHVDFSQSVS KMKWLGKGRG VKYFNDNEPK TVKRGQDKSR SRSRERHLQS
RNDKEKYRSS SKYNKSQSSN NRDKRYSDDK DRSSQRDGKE RSRSKSRVKN YETSSKREKS
PYSSRKTSDT DKDRKEKHHS THNNDKNNYS HNKKEKHTKG NNRESSLSPI KHIEERKRHI
KNNNRQASPS STKYGNVEDR QSKDSRKRKS QSPTKNIDKR ERISNRAESP SPTRNVKESE
RHSKSNKREK SHPPMRYTED RDRNSESNRR ESHSPARLAN DSNRHTKINY IETAPSPITK
QKDRDEIARE SSRNEKKYKQ SYNNEHDSKT NKRKLQENEI NSSNKKSRRE QPKTPSPLCK
REHERKEQKK TKTKHINKSK DRKNRKLNKK RKPSTSSDSS SESSTSSSST SSSSESDRKK
KKLRRKRKES TSSSSSSYSS DSSSSSSSSS TSYSSSSSSN SDHKKRKHKK KVKKNVKKPR
NKL
//
