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
//