ID   MKRN1_XENLA             Reviewed;         408 AA.
AC   Q6GLT5;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Probable E3 ubiquitin-protein ligase makorin-1;
DE            EC=2.3.2.27;
DE   AltName: Full=RING-type E3 ubiquitin transferase makorin-1 {ECO:0000305};
GN   Name=mkrn1;
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;
RN   [1] {ECO:0000312|EMBL:AAH74368.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain {ECO:0000312|EMBL:AAH74368.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E3 ubiquitin ligase catalyzing the covalent attachment of
CC       ubiquitin moieties onto substrate proteins. {ECO:0000250}.
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;
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
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DR   EMBL; BC074368; AAH74368.1; -; mRNA.
DR   RefSeq; NP_001086242.1; NM_001092773.1.
DR   AlphaFoldDB; Q6GLT5; -.
DR   DNASU; 444671; -.
DR   GeneID; 444671; -.
DR   KEGG; xla:444671; -.
DR   CTD; 444671; -.
DR   Xenbase; XB-GENE-959147; mkrn1.S.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000186698; Chromosome 3S.
DR   Bgee; 444671; Expressed in blastula and 19 other tissues.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR045072; MKRN-like.
DR   InterPro; IPR041367; Znf-CCCH_4.
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; PTHR11224; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   Pfam; PF18044; zf-CCCH_4; 3.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00356; ZnF_C3H1; 4.
DR   SUPFAM; SSF90229; SSF90229; 3.
DR   PROSITE; PS50103; ZF_C3H1; 4.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding; Reference proteome; Repeat; Transferase;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..408
FT                   /note="Probable E3 ubiquitin-protein ligase makorin-1"
FT                   /id="PRO_0000361047"
FT   ZN_FING         34..61
FT                   /note="C3H1-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         63..90
FT                   /note="C3H1-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         174..201
FT                   /note="C3H1-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         247..301
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         330..359
FT                   /note="C3H1-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          90..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          154..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          202..229
FT                   /note="Makorin-type Cys-His"
FT                   /evidence="ECO:0000255"
FT   REGION          363..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..113
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   408 AA;  45635 MW;  31CA35DEB3DEAF9A CRC64;
     MAEAAAAPAL LTSAASAGKA PLPAFPENPP VGVWTRHVTC RYFIHGVCKE GINCRYSHDL
     ATSRSAMICR YFQRGCCAYG DRCRYEHNKP LQEDPTGDTC TAPSESLPEP SGNINSKAAE
     LAASELASGG PRAQDWVNAV EFVPGQLYSG RAPEAYTQGT VKPDEGREEP ADPELKKQLC
     PYAAMGECRY GENCVYLHGD PCDMCGLQVL HPVDTCQRSQ HIKSCIEAHE KDMELSFAVQ
     RSKDIVCGIC MEVVYEKTNP SERRFGILSN CSHSYCLKCI RKWRSAKQFE SKIIKSCPEC
     RITSNFIIPS EYWVEEKEEK HKLIHKYKEA MSSKSCRYFD EGRGTCPFGG NCFYRHAYPD
     GRIEEPQPRQ KSGMSSRYRI PSPSAGIDFG SLTSERAETR LRTRKTKL