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Database: UniProt
Entry: A0A1L8EVG0_XENLA
LinkDB: A0A1L8EVG0_XENLA
Original site: A0A1L8EVG0_XENLA 
ID   A0A1L8EVG0_XENLA        Unreviewed;       388 AA.
AC   A0A1L8EVG0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=marchf4.L {ECO:0000313|RefSeq:XP_018092334.2};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018092334.2};
RN   [1] {ECO:0000313|RefSeq:XP_018092334.2}
RP   IDENTIFICATION.
RC   STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018092334.2};
RC   TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018092334.2};
RG   RefSeq;
RL   Submitted (NOV-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}.
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DR   RefSeq; XP_018092334.2; XM_018236845.2.
DR   AlphaFoldDB; A0A1L8EVG0; -.
DR   STRING; 8355.A0A1L8EVG0; -.
DR   PaxDb; 8355-A0A1L8EVG0; -.
DR   KEGG; xla:108701829; -.
DR   OMA; PNMFKYR; -.
DR   OrthoDB; 1342875at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd16824; RING_CH-C4HC3_MARCH4; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR046356; MARCHF4/9/11.
DR   InterPro; IPR047905; MARCHF4_RING_CH-C4HC3.
DR   InterPro; IPR011016; Znf_RING-CH.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR46053; E3 UBIQUITIN-PROTEIN LIGASE MARCH4-LIKE; 1.
DR   PANTHER; PTHR46053:SF3; E3 UBIQUITIN-PROTEIN LIGASE MARCHF4; 1.
DR   Pfam; PF12906; RINGv; 1.
DR   SMART; SM00744; RINGv; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS51292; ZF_RING_CH; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000186698}.
SQ   SEQUENCE   388 AA;  43655 MW;  B8AE57B1F17DCF20 CRC64;
     MFLRTILLLW CCGVLSCRQM LRHQGLLKCR CRMFFNDLKV FLLRRPPPIP SLPMNSSECD
     FGAGGALASN NNTLTALGRA WRTAAGGTTP EEDWIYPGNG LQHQQMSMVS TTSSDDFCKG
     KTEDRYSLGS SLDSGMRTPL CRICFQGPEQ GELLSPCRCD GSVRCSHQPC LIKWIGERGS
     WSCELCYYKY HVIAISTKNP LQVKWQAISL TVIEKVQIAA AILGSLFLIA SISWLIWSTF
     SPSAKWQRQD LLFQICYGMY GFMDIVCIGL IIHEGPSVYR IFKRWQAVNQ QWKVMNYDKS
     KDLEDQKLGT SQRTNQQTIS NNNNSSVGNP GSNTTPADSG NHVNGHSGTL SDHHCAYTIF
     HILSHLRPHE HRSQSNANRE FVMRVTTV
//
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