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Database: UniProt
Entry: A0A091GPD3_9AVES
LinkDB: A0A091GPD3_9AVES
Original site: A0A091GPD3_9AVES 
ID   A0A091GPD3_9AVES        Unreviewed;      1319 AA.
AC   A0A091GPD3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=N303_15582 {ECO:0000313|EMBL:KFO75972.1};
OS   Cuculus canorus (common cuckoo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX   NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO75972.1, ECO:0000313|Proteomes:UP000053760};
RN   [1] {ECO:0000313|EMBL:KFO75972.1, ECO:0000313|Proteomes:UP000053760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO75972.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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};
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DR   EMBL; KL447656; KFO75972.1; -; Genomic_DNA.
DR   STRING; 55661.A0A091GPD3; -.
DR   Proteomes; UP000053760; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   CDD; cd16541; RING-HC_RNF123; 1.
DR   CDD; cd12882; SPRY_RNF123; 1.
DR   Gene3D; 2.60.120.920; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR045129; RNF123/RSPRY1-like.
DR   InterPro; IPR003877; SPRY_dom.
DR   InterPro; IPR035773; SPRY_RNF123.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR13363:SF5; E3 UBIQUITIN-PROTEIN LIGASE RNF123; 1.
DR   PANTHER; PTHR13363; RING FINGER AND SRY DOMAIN-CONTAINING; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   Pfam; PF13920; zf-C3HC4_3; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053760};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          84..264
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000259|PROSITE:PS50188"
FT   DOMAIN          1266..1304
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          83..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          727..749
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1319 AA;  149000 MW;  C7D32B2AA64625F4 CRC64;
     MTSRGAGTAF SRKNYRLSTE LEKSKVTGLF PFCFSQGIVN SRLLNDYLHR IFTNADGNQS
     AAAYRKHLTF QNLQEHLDRL LAEEDDSDDS RDQGAEGRLG PSTVVLDHTS GFEGLLLVDD
     DLLGVIGHSN FGSIRATTCV YKGKWIYEVL ISSQGLMQIG WCTLNCRFNQ EEGVGDTPDS
     YAYDGNRVRK WNVTTTNYGK SWAAGDIVSC LIDLDEGTIA FCLNGISLGT AFDNITRGAG
     MAYFPAISLS FKESVAFNFG SRPLRYPLVE GYRPLQDPPV ADLVKTRKLL GYLKNVIHIG
     IDVTEGKLVE RDMSMWQLQG EPTVLITLAH IFNYFSPLMC KVYLVEDVLM TFLLSILEQG
     GAVESHPLIQ QLLDLMWLLM EEYEVHECLK QLLMSLLRAY RFSPIIPDLG LQIHYLRLTI
     AVLKHEKSRK YLLSNVLFDV LRSVVFFYIK SPLRVEEAGL QELIPTTWWP NRFTKEGKEG
     KEVKEESAEE RLRRRAYERG CQRLKKRIEV VEGLQVEILK LLLNNKDRGG GEASRYIFLN
     KFRKFLQENA SNRGNLTVLC PPEYMVCFLH RLIAALRFFW DGHKAKTPAA LSSEEAYIPP
     QLFYNGKVDY FDLQRLGGLL SHLKKTLKDD LAAKANVLID PAELHAVTMD DLDEDEESAT
     SAAQSQRPSA ALAIGGALAR PGWLSSPTLG RANRFLSTAA VSLMNPRRPL GALEKIKVRT
     LSVEQRTEED IEGSHGNEGL LLGRPPEEPD QPITENSLLE ILDGIVMMYN LSVHQQLGKM
     VGVSDDVNEY AMALKDTEGK ISRCPRRRRD IHDELLKSQK VFSEKLNHLS RRLAWINVTI
     YSKEKMQDIY WLLRVCIRTI EHGDRTGSLF AFMPEFYLSV AINSYSALKN YFSPVNSMED
     LPGYDETLMR LAAILAKHFA DSRIVGTDIR DSLMQALASY VCYPHSLRAV ERIPEEQRIS
     MMKNLLAPYE QRPWAQTNWI LVRLWRGCGF GYRYTRLPHL LKTKPEDASL PSLQKPCPST
     LLQRHMADLL CSDRDLAPSF LNSVLNQLNW AFSEFIGMIQ EIQQAAERLE RNFVDSRQLK
     VCATCFDLSV SLLRVLEMTV TLAPEIFLDW NRPSSELLLR RLAQLLSVLI PCFRAAERNL
     FDRVVNLRLP GLESVDHYPI LVAVTGILVR LLVDTDVQGA ERATAVLLAD PCFQLRSIQY
     LLGHAEPSAL AAAAPATDKH HFSLHTYTEY ISAEELAKVD RMLNHLSEES KQAAATTLPT
     SEEDLCPICY AHPISAIFRP CSHKSCKACI NQHLMNNKDC FFCKATITGV DDFTKPASS
//
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