ID A0A194RCD2_PAPMA Unreviewed; 695 AA.
AC A0A194RCD2;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=E3 ubiquitin-protein ligase UHRF1 {ECO:0000313|EMBL:KPJ15503.1};
GN ORFNames=RR48_09432 {ECO:0000313|EMBL:KPJ15503.1};
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:KPJ15503.1, ECO:0000313|Proteomes:UP000053240};
RN [1] {ECO:0000313|EMBL:KPJ15503.1, ECO:0000313|Proteomes:UP000053240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ya'a_city_454_Pm {ECO:0000313|EMBL:KPJ15503.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KPJ15503.1};
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00358}.
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DR EMBL; KQ460367; KPJ15503.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194RCD2; -.
DR STRING; 76193.A0A194RCD2; -.
DR InParanoid; A0A194RCD2; -.
DR Proteomes; UP000053240; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR CDD; cd01797; Ubl_UHRF; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 2.30.280.10; SRA-YDG; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR014722; Rib_uL2_dom2.
DR InterPro; IPR036987; SRA-YDG_sf.
DR InterPro; IPR003105; SRA_YDG.
DR InterPro; IPR021991; TTD_dom.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR019956; Ubiquitin_dom.
DR InterPro; IPR045134; UHRF1/2-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR14140; E3 UBIQUITIN-PROTEIN LIGASE UHRF-RELATED; 1.
DR PANTHER; PTHR14140:SF45; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF02182; SAD_SRA; 1.
DR Pfam; PF12148; TTD; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00184; RING; 1.
DR SMART; SM00466; SRA; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
DR PROSITE; PS51015; YDG; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00358}; Reference proteome {ECO:0000313|Proteomes:UP000053240};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 1..73
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 306..471
FT /note="YDG"
FT /evidence="ECO:0000259|PROSITE:PS51015"
FT DOMAIN 624..663
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 144..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 695 AA; 78935 MW; 76483DCD3E97F533 CRC64;
MHVRIRTFGK PDSVVVVESK LTKIEKFRRI ISEKFDIEPK SQRLFYGGKL LEDGYTFHDY
NIKLNDVIQL MIKVQPVDST ETETQKVNHE QNNKTKSNSK VYQDTESDLY LIGDLVDVKD
KEQGTWLEGK IVKIVYDPET LSTNVNHETR TNGDTEGNSV KEDDHNEASQ IQNDKNTKVT
KTSITKFFSP RSKTKKQNGH KSSEPNELKS DRSILYKIQL DDDEEDSDLY CTEKEIRPRA
RTVLEIKDLK IGQKVMVNYN TDEPLEKGYW YDFKQRKQAR SNRDWGRGMA CVGKTKTCAM
PPNHFGPIPG IEVGMCWRFR IQLSETGVHR PPVSGIHGRD VEGAYSIVLS GGYEDDVDNG
NEFTYTGSGG RDLSGNKRTA EQSCDQTLTR ENKALARNCA AGEVSEKGGD AGEAWKNGKP
VRVVRSYKML RHFPKYAPSE GIRYDGIYKV VKYYPEKGLS GFRVWKYLLR RDDPSPAPWE
PNAKQYSIIY PDGYLEAEAE KKKLKEKKSK GNRGSKKRET HNSSDSDCKV SPPKKKRKVS
NEKLKTEKSD DPKKSPKKKM ANIFNVKNPN TKNTKINSNL LTPEEQEAIE SDTLNSKLWK
ECLSVCHESG KKEFIEQVTQ AFLCIICQDV AVNPITTPCC HNFCLACLKL AFKSNAKCCP
CCRRGLQEPP SSENVNEHLR AALRAVMPGY DAGKK
//
