ID A0A3P9QGU3_POERE Unreviewed; 352 AA.
AC A0A3P9QGU3;
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=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
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:ENSPREP00000033410.1, 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:ENSPREP00000033410.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000033410.1};
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};
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DR RefSeq; XP_008411767.1; XM_008413545.2.
DR AlphaFoldDB; A0A3P9QGU3; -.
DR STRING; 8081.ENSPREP00000033410; -.
DR Ensembl; ENSPRET00000033789.1; ENSPREP00000033410.1; ENSPREG00000022638.1.
DR GeneID; 103467296; -.
DR KEGG; pret:103467296; -.
DR CTD; 559882; -.
DR GeneTree; ENSGT00950000183077; -.
DR OMA; CLQCIMT; -.
DR OrthoDB; 2906101at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000022638; Expressed in caudal fin and 1 other cell type or tissue.
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: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; IPR041367; Znf-CCCH_4.
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; MAKORIN-RELATED; 1.
DR PANTHER; PTHR11224:SF39; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF18044; zf-CCCH_4; 2.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00356; ZnF_C3H1; 3.
DR SUPFAM; SSF90229; CCCH zinc finger; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50103; ZF_C3H1; 3.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; 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 5..31
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 33..60
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 193..247
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 275..303
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 5..31
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 33..60
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 275..303
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
SQ SEQUENCE 352 AA; 40423 MW; 6B04A0162C3F6C9E CRC64;
MDSVRSGNIC RRFINGSCRF GRRCKYRHEF TPIPASQICR YFQKGGCWYG ERCRFFHVLL
PQVGPVFPGR RGSVPVASPS SMPHYSERRG SEPTLWRVNV PSRQRCSGSQ SAMYPFNLQQ
ESGHLPEYVL EELSQENYLE SAPSYSGIAQ ASAWEGRYER TSKSETYEDG AAAAYNEKSE
ETLAFLQSKN VVCGICMDKV YEKENQRDRV FGILPNCNHP FCLDCIATWR KTKDIGLDVV
RACPQCRVRS AFYVPNKYWV EGQEKENVIS AFKKKFGKKR CCFYDRYGCC PFKKECLYRH
VADSNSPVFS YLSEEEDDSF TDLLGFFISM SLLGGEEADE ELLFCLTEDY GF
//
