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Database: UniProt
Entry: A0A3B3UDU8_9TELE
LinkDB: A0A3B3UDU8_9TELE
Original site: A0A3B3UDU8_9TELE 
ID   A0A3B3UDU8_9TELE        Unreviewed;       398 AA.
AC   A0A3B3UDU8;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=E3 ubiquitin-protein ligase makorin-2 {ECO:0000256|ARBA:ARBA00029530};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE   AltName: Full=RING-type E3 ubiquitin transferase makorin-2 {ECO:0000256|ARBA:ARBA00030863};
OS   Poecilia latipinna (sailfin molly).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000010772.1, ECO:0000313|Proteomes:UP000261500};
RN   [1] {ECO:0000313|Ensembl:ENSPLAP00000010772.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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_014873845.1; XM_015018359.1.
DR   AlphaFoldDB; A0A3B3UDU8; -.
DR   STRING; 48699.ENSPLAP00000010772; -.
DR   Ensembl; ENSPLAT00000028937.1; ENSPLAP00000010772.1; ENSPLAG00000013770.1.
DR   GeneID; 106937049; -.
DR   KEGG; plai:106937049; -.
DR   CTD; 23609; -.
DR   GeneTree; ENSGT00950000183077; -.
DR   OrthoDB; 2906101at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000261500; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0000209; P:protein polyubiquitination; IEA:InterPro.
DR   Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR045072; MKRN-like.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR036855; Znf_CCCH_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR11224:SF17; E3 UBIQUITIN-PROTEIN LIGASE MAKORIN-2; 1.
DR   PANTHER; PTHR11224; MAKORIN-RELATED; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   Pfam; PF00642; zf-CCCH; 1.
DR   Pfam; PF14608; zf-CCCH_2; 3.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00356; ZnF_C3H1; 4.
DR   SUPFAM; SSF90229; CCCH zinc finger; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50103; ZF_C3H1; 4.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}.
FT   DOMAIN          2..29
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          31..58
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          145..167
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          213..267
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          296..325
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   ZN_FING         2..29
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         31..58
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         145..167
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         296..325
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
SQ   SEQUENCE   398 AA;  44089 MW;  BC023D50BFC15A0F CRC64;
     MSTRQVTCRY FLHGVCREGS NCLFSHDLNN SKPSTICKYY QRGTCAYGER CRYDHVKHSM
     RGGGGASADP AGAGRGVRGE GKKPLVLKDR ALCGDRTFGS LSDGPIPAVP EAAATPQSYV
     EAIRTGLDGS APEPEPHAVG GAYQLCPYAA AGHCFYGDSC PYLHGDLCEV CRLQVLHPHD
     PEQRRAHEKV CLLAFEADME KAFAAQLSQN KVCSICMEVV VQKAAPSERR FGILSSCCHT
     FCLSCIRQWR GTTNFCNKII KSCPECRIIS EFVIPSVYWV EDQEEKDQLI ELFKSGVSKK
     ACKYFDQGRG SCPFGGNCLY LHAYPDGTRP EPDRPRKQLS SEGNVRFMNR VRLWDFIEER
     EQHAAPPLDD DITELRQLFM QMSGPSAEEA EGPPNPGV
//
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