ID   MKRN1_SERQU             Reviewed;         435 AA.
AC   Q8JFF3; Q76L86; Q76L91;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 75.
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 {ECO:0000250|UniProtKB:Q9UHC7};
OS   Seriola quinqueradiata (Five-ray yellowtail).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=8161;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAB91214.2}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Testis {ECO:0000312|EMBL:BAB91214.2};
RA   Chamnan C., Abe S., Doi M., Chiba S., Gray T.A.;
RT   "The genomic organization of MKRN1, and expression profiles of MKRN1,
RT   MKRN2, and RAF1 in yellowtail fish (Seriola quinqueradiata).";
RL   J. Egypt. Ger. Soc. Zool. C Histol. Histochem. 43C:57-75(2003).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:BAC99018.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 18-435.
RC   TISSUE=Testis {ECO:0000312|EMBL:BAC99018.1};
RA   Chamnan C., Abe S.;
RT   "Genomic structure of the gene coding protein featuring ring-finger,
RT   Makorin1, found in Yellowtail Tuna.";
RL   Submitted (APR-2002) 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.
CC   -!- TISSUE SPECIFICITY: Weakly expressed in adult brain, heart and kidney.
CC       {ECO:0000269|Ref.1}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC99018.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AB073984; BAB91214.2; -; mRNA.
DR   EMBL; AB073985; BAB91215.2; -; Genomic_DNA.
DR   EMBL; AB083365; BAC98837.1; -; mRNA.
DR   EMBL; AB083692; BAC99018.1; ALT_FRAME; Genomic_DNA.
DR   AlphaFoldDB; Q8JFF3; -.
DR   UniPathway; UPA00143; -.
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; IPR031644; MKRN1_C.
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; PF15815; MKRN1_C; 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; 2.
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; Repeat; Transferase; Ubl conjugation pathway; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..435
FT                   /note="Probable E3 ubiquitin-protein ligase makorin-1"
FT                   /id="PRO_0000361758"
FT   ZN_FING         18..45
FT                   /note="C3H1-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         48..75
FT                   /note="C3H1-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         155..182
FT                   /note="C3H1-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         228..282
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         311..340
FT                   /note="C3H1-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          81..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          183..210
FT                   /note="Makorin-type Cys-His"
FT                   /evidence="ECO:0000255"
FT   REGION          345..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        349..365
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   435 AA;  48929 MW;  0A2B04D0DE02D811 CRC64;
     MAEAAAASTA ASGVIGGWTK HVTCRYFMHG LCKEGDNCRY SHDLTNSKPA AMICKFFQKG
     NCVFGDRCRF EHCKPAKNEE LPAPQMLPLP SASLAGPSDP EPSGPTPVPG AQDWVNAAEF
     VPGQPYCGRA EQAKVESSVP LIEEFDSYPA PDNKQLRKQL CPYAAVGECR YGINCAYLHG
     DVCYMCGLQV LHPTDNNQRS EHTKACIEAH EKDMEISFAI QRSKDMMCGV CMEVVFEKAN
     PSERRFGILS NCSHCYCLKC IRKWRSAKQF ESKIIKSCPE CRITSNFVIP SEYWVEDKDD
     KQKLIQKYKD GMGSKPCRYF DEGRGTCPFG SNCFYKHAFP DGRLEEAQPQ RRQTGSNSRN
     RNSRRTPLWD IYDERESTDS FDNEDEEMVT FELSEMLLML LAAGTDDEEV IIRPPSCATS
     SGRLDPTVTR YRKAC