ID A0A3P9QB84_POERE Unreviewed; 399 AA.
AC A0A3P9QB84;
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 Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000031284.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000031284.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000031284.1};
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_008406440.1; XM_008408218.2.
DR AlphaFoldDB; A0A3P9QB84; -.
DR STRING; 8081.ENSPREP00000031284; -.
DR Ensembl; ENSPRET00000031642.1; ENSPREP00000031284.1; ENSPREG00000021199.1.
DR GeneID; 103464240; -.
DR KEGG; pret:103464240; -.
DR CTD; 23609; -.
DR GeneTree; ENSGT00950000183077; -.
DR OMA; MQGVCRE; -.
DR OrthoDB; 2906101at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000021199; Expressed in caudal fin and 1 other cell type or tissue.
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; 1.20.120.1350; Pneumovirus matrix protein 2 (M2), zinc-binding domain; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000242638};
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 146..168
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 214..268
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 297..326
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 146..168
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 297..326
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 380..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 399 AA; 44193 MW; 5D69BAA589BD7CAD CRC64;
MSTRQVTCRY FLHGVCREGS NCLFSHDLNN SKPSTICKYY QRGTCAYGER CRYDHVKHSV
RGGGGGASAD PACAGRGVRG EGKKPLVLKD RALCGDRTFG GLSDGPIPAV PEAAAAPQSY
VEAIRTGLDG SVPEPEPHAV GGAYQLCPYA AAGHCFYGDS CPYLHGDLCE VCRLQVLHPH
DPEQRRAHEK VCLLAFEADM EKAFAAQLSQ NKVCSICMEV VVQKAAPSER RFGILSSCCH
TFCLSCIRQW RGTTNFCNKI IKSCPECRII SEFVIPSVYW VEDQDEKDHL IELFKSGVSK
KACKYFDQGR GSCPFGGNCL YLHAYPDGTR PEPDRPRKQL SSEGNVRFMN RVRLWDFIEE
REQHAAPHLD DDITELRQLF MQMSGPSAEE AEGPPNPGE
//
