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Database: UniProt
Entry: A0A1S3GJ66_DIPOR
LinkDB: A0A1S3GJ66_DIPOR
Original site: A0A1S3GJ66_DIPOR 
ID   A0A1S3GJ66_DIPOR        Unreviewed;       708 AA.
AC   A0A1S3GJ66;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=G2/M phase-specific E3 ubiquitin-protein ligase isoform X1 {ECO:0000313|RefSeq:XP_012888923.1, ECO:0000313|RefSeq:XP_012888924.1};
GN   Name=G2e3 {ECO:0000313|RefSeq:XP_012888923.1,
GN   ECO:0000313|RefSeq:XP_012888924.1};
OS   Dipodomys ordii (Ord's kangaroo rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC   Dipodomyinae; Dipodomys.
OX   NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012888923.1};
RN   [1] {ECO:0000313|RefSeq:XP_012888923.1, ECO:0000313|RefSeq:XP_012888924.1}
RP   IDENTIFICATION.
RC   TISSUE=Kidney {ECO:0000313|RefSeq:XP_012888923.1,
RC   ECO:0000313|RefSeq:XP_012888924.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_012888923.1; XM_013033469.1.
DR   RefSeq; XP_012888924.1; XM_013033470.1.
DR   GeneID; 105998670; -.
DR   KEGG; dord:105998670; -.
DR   CTD; 55632; -.
DR   OrthoDB; 2899995at2759; -.
DR   Proteomes; UP000081671; Unplaced.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   CDD; cd15669; ePHD_PHF7_G2E3_like; 1.
DR   CDD; cd15496; PHD_PHF7_G2E3_like; 1.
DR   Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR   Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR034732; EPHD.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   InterPro; IPR042013; PHF7/G2E3_ePHD.
DR   InterPro; IPR042012; PHF7/G2E3_PHD.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR12420:SF37; G2_M PHASE-SPECIFIC E3 UBIQUITIN-PROTEIN LIGASE; 1.
DR   PANTHER; PTHR12420; PHD FINGER PROTEIN; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF13771; zf-HC5HC2H; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00249; PHD; 2.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR   PROSITE; PS51805; EPHD; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          11..128
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51805"
FT   DOMAIN          534..705
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   ACT_SITE        668
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   708 AA;  81012 MW;  F9AD910A314021D5 CRC64;
     MNENKPGDSQ NLACVFCRKT DDCPYKYGEK KTNEKWNLTV HYHCLLMSSG IWQRGKEEEG
     LYGFLIEDIK KEVHRASKLK CSVCKKSGAS IGCVAPRCKR SYHLPCGLER ECIFQFTGNF
     ASFCWSHRPI QITTSNNYRD SLPCTICLEY IEPIPTYSVL QSPCCKNAWF HRDCLQVQAI
     NAGIFFFRCT ICNNSEIFQK EMLKMGIHIP EKDASWELEE NAYQDLLQHH ERCDVRRCRC
     KEGREYNEPD SKWEIKRCQC CGSSGTHLAC SSLRSWEQNW ECLECRSIIY NSGFKSVGFQ
     KAKKHAAPKS NKVAITDCLL EESSPKLQKL SSGPQHEELL RQGSKFRRDI STILIELGFQ
     IKKKTEKLYI NKANIWNSAI DEFKNFNPSY TIEVSYVNEN DGFGKECLGS KQEFLSLLMH
     HLANSSLFEG SLSKNLSLNS QALEENLYYE AGKILAISLV HGGPSPGFFS KTLFNCLVYG
     PENTEPVLED VSDFDVAQII IRINTAADIT DLNSVINECY NYLDVIGCLR HVTTLNDKYM
     LAKDVLVYQV IKRVQIPFES FKQGLKTLGV LEKIQTYPEA FYDILCHKPE TLSAKVLSDL
     FEMHTLPDVQ TSGYWKNYLQ NIEEGKSATT MEDILIFATG CNSVPPSGFK PTPSIEYLHT
     DFPVGNKCNN CLVLPITKTY KEFEESMDFT IRNTIKLEKE EYSHYVEH
//
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