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Database: UniProt
Entry: A0A1Y1MUX8_PHOPY
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ID   A0A1Y1MUX8_PHOPY        Unreviewed;       518 AA.
AC   A0A1Y1MUX8;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   08-NOV-2023, entry version 23.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=PPYR_12467 {ECO:0000313|EMBL:KAB0795628.1};
OS   Photinus pyralis (Common eastern firefly) (Lampyris pyralis).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Elateriformia; Elateroidea;
OC   Lampyridae; Lampyrinae; Photinus.
OX   NCBI_TaxID=7054 {ECO:0000313|EMBL:JAV89461.1};
RN   [1] {ECO:0000313|EMBL:JAV89461.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=28004739; DOI=10.1038/srep38556;
RA   Al-Wathiqui N., Fallon T.R., South A., Weng J.K., Lewis S.M.;
RT   "Molecular characterization of firefly nuptial gifts: a multi-omics
RT   approach sheds light on postcopulatory sexual selection.";
RL   Sci. Rep. 6:38556-38556(2016).
RN   [2] {ECO:0000313|EMBL:KAB0795628.1, ECO:0000313|Proteomes:UP000327044}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1611_PpyrPB1 {ECO:0000313|EMBL:KAB0795628.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KAB0795628.1};
RX   PubMed=30324905;
RA   Fallon T.R., Lower S.E., Chang C.H., Bessho-Uehara M., Martin G.J.,
RA   Bewick A.J., Behringer M., Debat H.J., Wong I., Day J.C., Suvorov A.,
RA   Silva C.J., Stanger-Hall K.F., Hall D.W., Schmitz R.J., Nelson D.R.,
RA   Lewis S.M., Shigenobu S., Bybee S.M., Larracuente A.M., Oba Y., Weng J.K.;
RT   "Firefly genomes illuminate parallel origins of bioluminescence in
RT   beetles.";
RL   Elife 7:e36495-e36495(2018).
RN   [3] {ECO:0000313|EMBL:KAB0795628.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=1611_PpyrPB1 {ECO:0000313|EMBL:KAB0795628.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KAB0795628.1};
RG   Photinus pyralis genome working group;
RA   Fallon T.R., Sander Lower S.E., Weng J.-K.;
RL   Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL2
CC       subfamily. {ECO:0000256|ARBA:ARBA00007930}.
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DR   EMBL; GEZM01020010; JAV89461.1; -; Transcribed_RNA.
DR   EMBL; VVIM01000008; KAB0795628.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1MUX8; -.
DR   InParanoid; A0A1Y1MUX8; -.
DR   OrthoDB; 7846at2759; -.
DR   Proteomes; UP000327044; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR   CDD; cd01923; cyclophilin_RING; 1.
DR   CDD; cd16663; RING-Ubox_PPIL2; 1.
DR   Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   InterPro; IPR044666; Cyclophilin_A-like.
DR   InterPro; IPR026951; PPIL2_U-box_dom.
DR   InterPro; IPR003613; Ubox_domain.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45625; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-RELATED; 1.
DR   PANTHER; PTHR45625:SF1; RING-TYPE E3 UBIQUITIN-PROTEIN LIGASE PPIL2; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   Pfam; PF04641; Rtf2; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SMART; SM00504; Ubox; 1.
DR   SUPFAM; SSF50891; Cyclophilin-like; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
DR   PROSITE; PS51698; U_BOX; 1.
PE   3: Inferred from homology;
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000327044}.
FT   DOMAIN          37..110
FT                   /note="U-box"
FT                   /evidence="ECO:0000259|PROSITE:PS51698"
FT   DOMAIN          287..433
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50072"
SQ   SEQUENCE   518 AA;  59358 MW;  5CF1B5F2C0863B6C CRC64;
     MGKRQHQKDK MYLTYTEWTT LYGGKRAGPV IDDLAFKRLP FDHCCLSLQP FEDPYCDDNG
     NIFDLQALLP FLKKFKVNPV TGSPMDVKAL FKLNLHKNAE GEFHCPVLFR TLTNSSHFAA
     IRTTGNVYSM EAIEQLNIKN KNWKDLITDA PFERKDVIVL QDPRDLTKFN ISLFHHVKNN
     LRMETEEEVA ERGDPQARIK KMNPETKHTL EELERDYKEP TIKIQGTPKS TEKADKFNAA
     HYSTGAVAAS FTSTVMAVEL THEPAIMHED LVRYSRVKKK GYVRLVTNIG PLNLELHCDI
     VPKTCENFLR HCDNGYYDGT KFHRSIRHFM IQGGDPTDSG QGGKSIWGKP FEDEFRPNLT
     HTGRGVLSMA NSGKNTNGSQ FFITFRSCKH LDNKHTIFGR LVGGMDTLTI MERIEVDNQD
     RPIEDIIIVK AQIFVDPYTE ADETLKKDRE DELKRQAEEE LAQKRKVEAK KPLTVYKSGV
     GKYINPQVTK SNTKNDDEGA LTVRKKKNVA YNFNFNNW
//
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