GenomeNet

Database: UniProt
Entry: A0A493T235_ANAPP
LinkDB: A0A493T235_ANAPP
Original site: A0A493T235_ANAPP 
ID   A0A493T235_ANAPP        Unreviewed;       491 AA.
AC   A0A493T235;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE   AltName: Full=RING-type E3 ubiquitin transferase makorin-1 {ECO:0000256|ARBA:ARBA00042581};
OS   Anas platyrhynchos platyrhynchos (Northern mallard).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anatinae; Anas.
OX   NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000019999.1, ECO:0000313|Proteomes:UP000016666};
RN   [1] {ECO:0000313|Ensembl:ENSAPLP00000019999.1, ECO:0000313|Proteomes:UP000016666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT   "A new Pekin duck reference genome.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSAPLP00000019999.1}
RP   IDENTIFICATION.
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};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; A0A493T235; -.
DR   Ensembl; ENSAPLT00000047163.1; ENSAPLP00000019999.1; ENSAPLG00000016256.2.
DR   GeneTree; ENSGT00950000183077; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000016666; Chromosome 1.
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   CDD; cd16730; RING-HC_MKRN1_3; 1.
DR   Gene3D; 2.30.30.1190; -; 2.
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; 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:SF37; E3 UBIQUITIN-PROTEIN LIGASE MAKORIN-1; 1.
DR   PANTHER; PTHR11224; MAKORIN-RELATED; 1.
DR   Pfam; PF15815; MKRN1_C; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   Pfam; PF14608; zf-CCCH_2; 1.
DR   Pfam; PF18044; zf-CCCH_4; 3.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00356; ZnF_C3H1; 4.
DR   SUPFAM; SSF90229; CCCH zinc finger; 3.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50103; ZF_C3H1; 4.
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:UP000016666};
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          55..82
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          84..111
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          236..263
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          309..363
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          392..421
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   ZN_FING         55..82
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         84..111
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         236..263
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         392..421
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
SQ   SEQUENCE   491 AA;  54816 MW;  68E9E0ACED07E0DD CRC64;
     MAEAVALGTA AGAAAAAAAL GPSAAAAAAA AEEAGTLFGP AAVPPPLALG PGGGWTKQVT
     CRYFMHGVCK EGDNCRYSHD LSTSQSAMVC RYYQRGCCAY GDHCRYEHTK PLIQEEEEED
     VTTVNPDEKI YPSVSSDLAS FPDETIEEEL VELEAEDLDM AAAGVGVEDW VNAVEFVPGQ
     PYCGRAATSC TELPLDGTLD GTLDGTLDGT LDGTLDGTLD GMVIEEEYEK QEENEEMKKQ
     LCPYAAVGEC RYGENCVYIH GDVCDMCGLQ VLHPIDAAQR SQHIKSCIEA HEKDMELSFA
     VQRSKDMVCG ICMEVVYEKA NPSERRFGIL SNCNHTYCLK CIRKWRSAKQ FESKIIKSCP
     ECRITSNFVI PSEYWVEEKE EKQKLIQKYK EAMSNKPCRY FDEGRGSCPF GGNCFYKHAY
     PDGRQEEPQR PKAQRRNRFW EFIEERENGD PFETDEDEVV TFELGDDELT DSEDEWDLFH
     DELEDYYDLD L
//
DBGET integrated database retrieval system