ID   A0A384AYU7_BALAS        Unreviewed;       413 AA.
AC   A0A384AYU7;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, 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   Name=RAD18 {ECO:0000313|RefSeq:XP_007192560.1};
OS   Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS   (Balaenoptera davidsoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC   Balaenopteridae; Balaenoptera.
OX   NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007192560.1};
RN   [1] {ECO:0000313|RefSeq:XP_007192560.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_007192560.1};
RG   RefSeq;
RL   Submitted (JAN-2023) to UniProtKB.
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   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   RefSeq; XP_007192560.1; XM_007192498.2.
DR   AlphaFoldDB; A0A384AYU7; -.
DR   CTD; 56852; -.
DR   OrthoDB; 6177at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000261681; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0006301; P:postreplication repair; IEA:InterPro.
DR   GO; GO:0006513; P:protein monoubiquitination; IEA:InterPro.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 1.10.720.30; SAP domain; 1.
DR   InterPro; IPR039577; Rad18.
DR   InterPro; IPR006642; Rad18_UBZ4.
DR   InterPro; IPR003034; SAP_dom.
DR   InterPro; IPR036361; SAP_dom_sf.
DR   PANTHER; PTHR14134; E3 UBIQUITIN-PROTEIN LIGASE RAD18; 1.
DR   PANTHER; PTHR14134:SF2; E3 UBIQUITIN-PROTEIN LIGASE RAD18; 1.
DR   Pfam; PF02037; SAP; 1.
DR   SMART; SM00513; SAP; 1.
DR   SMART; SM00734; ZnF_Rad18; 1.
DR   PROSITE; PS50800; SAP; 1.
DR   PROSITE; PS51908; ZF_UBZ4; 1.
PE   4: Predicted;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|PROSITE-
KW   ProRule:PRU01256};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|PROSITE-
KW   ProRule:PRU01256}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261681};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU01256}.
FT   DOMAIN          114..141
FT                   /note="UBZ4-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51908"
FT   DOMAIN          161..195
FT                   /note="SAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50800"
FT   REGION          69..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          302..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          375..413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..86
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        309..323
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   413 AA;  46662 MW;  2A1FE691F7D0508A CRC64;
     MNWNHLLQFA LESPPISSSS SSKNLAAKVH TSVAFRHSLK QGSRLMENFL IREAGGSVSE
     LLIKENESEF SPQKELSSSA KTRGTPSVEK SAPGFSEAGV PETPSTSALK QVTKVDCPVC
     GVHIPENHIN KHLDSCLSRE EKIESLRSSV HKRKPLPKTV YNLLSDRDLK KKLKQHGLSV
     RGNKQQLIKR HQEFVHMYNA QCDALHPKSA AEIVQEIENM EKTRMRLEAS KLNESIMVFT
     KDQTEKEIDE IHSKYRIKHQ NEFQRLVDQA RKGYKKTVGM SKKKVTEEDE STEKLLSVCG
     GQEDNKMKFS DMPSVTNHFP QSKLDSPGKL EPDRPDDSSS CTDIQEVALS SPESDSCNSS
     SSDIIRDLLE EEEAWEASHK CDLQDTEISP RQNRRTRSAE SAELEPRNKR NRN
//