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Database: UniProt
Entry: A0A3P9DBW0_9CICH
LinkDB: A0A3P9DBW0_9CICH
Original site: A0A3P9DBW0_9CICH 
ID   A0A3P9DBW0_9CICH        Unreviewed;       415 AA.
AC   A0A3P9DBW0;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
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   Maylandia zebra (zebra mbuna).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX   NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005032185.1, ECO:0000313|Proteomes:UP000265160};
RN   [1] {ECO:0000313|Ensembl:ENSMZEP00005032185.1}
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_004559018.1; XM_004558961.2.
DR   AlphaFoldDB; A0A3P9DBW0; -.
DR   STRING; 106582.ENSMZEP00005032185; -.
DR   Ensembl; ENSMZET00005033226.1; ENSMZEP00005032185.1; ENSMZEG00005023975.1.
DR   GeneID; 101464427; -.
DR   KEGG; mze:101464427; -.
DR   CTD; 23609; -.
DR   GeneTree; ENSGT00950000183077; -.
DR   OrthoDB; 2906101at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000265160; 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; IPR041686; Znf-CCCH_3.
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; PF14608; zf-CCCH_2; 2.
DR   Pfam; PF15663; zf-CCCH_3; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000265160};
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          153..180
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          226..280
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          309..338
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         153..180
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         309..338
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          58..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   415 AA;  45915 MW;  A4871174CD070373 CRC64;
     MSTKQVTCRY FLHGVCREGN RCLFSHDPST SKPSTICKFY QRGACAYGER CRYDHIRLSS
     RGGGSGTSED LTGGGRGGGG ASRSGRGGAK KTLVLRDRVL GVEDVFRGPS DNSGSEVTAA
     ATASPHSYVD AIRAGLDTSA QERAPPPVGG AYPDLPQLCP YAAGGRCFYE DSCTYLHGDL
     CEVCGLQVLH PQDPEQRRAH EKMCLLAFEA DMEKAFAAQL SNDKVCSICM DVVVQKANPS
     ERRFGILSSC NHIFCLSCIR KWRCTRNFHN KIIKSCPQCR VISEFVIPSM YWVEDQDEKD
     HLIDLFKSGV GKKACKYFDQ GRGSCPFGGK CLYLHAFPDG SRAEAERPRK QLSSEGSVRF
     MNSVRLWDFI EEREQRSVPP LPSLTDDITE LRELFMQMSG PSHEDEPETS PANDL
//
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