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Database: UniProt
Entry: A0A3Q2ZBU0_KRYMA
LinkDB: A0A3Q2ZBU0_KRYMA
Original site: A0A3Q2ZBU0_KRYMA 
ID   A0A3Q2ZBU0_KRYMA        Unreviewed;       332 AA.
AC   A0A3Q2ZBU0;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS   Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000000958.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000000958.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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}.
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DR   RefSeq; XP_017289054.1; XM_017433565.1.
DR   AlphaFoldDB; A0A3Q2ZBU0; -.
DR   STRING; 37003.ENSKMAP00000000958; -.
DR   Ensembl; ENSKMAT00000000989.1; ENSKMAP00000000958.1; ENSKMAG00000000740.1.
DR   GeneID; 108246159; -.
DR   KEGG; kmr:108246159; -.
DR   CTD; 441061; -.
DR   GeneTree; ENSGT00940000160025; -.
DR   OMA; QPWTCLC; -.
DR   OrthoDB; 1342875at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000264800; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR046356; MARCHF4/9/11.
DR   InterPro; IPR011016; Znf_RING-CH.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR46053; E3 UBIQUITIN-PROTEIN LIGASE MARCH4-LIKE; 1.
DR   PANTHER; PTHR46053:SF1; E3 UBIQUITIN-PROTEIN LIGASE MARCHF11; 1.
DR   Pfam; PF12906; RINGv; 1.
DR   SMART; SM00744; RINGv; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51292; ZF_RING_CH; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        173..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        214..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          92..152
FT                   /note="RING-CH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51292"
FT   REGION          1..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   332 AA;  36699 MW;  7F657332C4A43D48 CRC64;
     MSAEEGDAGP ACGEEKGGSA VTHSWEESEP LRSQGRPHPD GLDGAQRGEE EEEEEADAEK
     FNVEVNGGNS SSEEGAVGGR SCKVMHSNCS SETCIPTPSC RICFQGAEQG DLLNPCRCDG
     SVRYTHQQCL LKWISERGCW TCELCCYRFQ VIAINLKRPW QWQSITITLV EKVQIIAVFL
     GSLFLVASIS WLLWSALSPQ AIWQRRDVLF QICYGMYGFM DLVCVGLIVH EGVAVYNVFM
     RWRAVNLHWD VQSYDKAKDM EETSTGHSSL GPRTLWLPLT TFGPSGPLHP TQLGSQPWTC
     LCLAPFCPGL VSRNNLSQDA DSGEVVIRVT SV
//
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