ID A0A091M9E3_CARIC Unreviewed; 1002 AA.
AC A0A091M9E3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=N322_11876 {ECO:0000313|EMBL:KFP68121.1};
OS Cariama cristata (Red-legged seriema).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cariamiformes; Cariamidae; Cariama.
OX NCBI_TaxID=54380 {ECO:0000313|EMBL:KFP68121.1, ECO:0000313|Proteomes:UP000054116};
RN [1] {ECO:0000313|EMBL:KFP68121.1, ECO:0000313|Proteomes:UP000054116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N322 {ECO:0000313|EMBL:KFP68121.1};
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};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus, PML body {ECO:0000256|ARBA:ARBA00004322}.
CC -!- SIMILARITY: Belongs to the Arkadia family.
CC {ECO:0000256|ARBA:ARBA00007622}.
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DR EMBL; KK525946; KFP68121.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091M9E3; -.
DR Proteomes; UP000054116; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16681; RING-H2_RNF111; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR029306; RNF111_N.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR16200:SF1; E3 UBIQUITIN-PROTEIN LIGASE PLR-1-RELATED; 1.
DR PANTHER; PTHR16200; RING ZINC FINGER; 1.
DR Pfam; PF15303; RNF111_N; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000054116};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 950..991
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 66..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..523
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..690
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..723
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1002 AA; 109479 MW; FE5E9C45A6399ED8 CRC64;
MSKWTPECNI VYTLKADMKS EVPSDAPKRQ ESLKGILLNP EPIGAAKSFT AEVEMIASKV
GNEFSHLCGD SEKQKDMNGN RTDQDKSIVV RKKRKSQQAG PSYSQNCPDK ENQGILGLRQ
HLETQSEDND SSFSDCISSP SSSLHFGDSD TVTSDEEKDA PVRHPQAVLN TTSRTHSARS
QKWPRTEADS VPGLLMKRPC FHSSSLRRLP YRKRFVKTSS SQRTQNQKER ILMQRKKREV
LARRKYALLP SSSSSSENDL SSESSSSSST EGEEDLFVSP GENHQNSTAV PSGSIDEDVV
VIEASSTPQV TANEEINVTS TDSEVEIVTV GESYRSRSTL GHTRPHWGQS SSSHAARPQE
QRNRSRISTV IQPLRQNAAE VVDLTVDEDE PTVVPTTSAR VEPQVVSSAS SNSSSTSTSE
QASDAVPNVS NSQPSAAPEM TSSLPSGGTA GTSTGDDTRR TASNTTLETG PPAMPRLPSC
CPQHSPCGGP SQTHHALGHP HTSCFQQHGH HFQHHHHHHH NPHPAVPLSP SFSDSSCPVE
RPPPVPAPCG TSSSSGTGYH DQAYGLFTQQ ALPVDLSSSG IRSHGSGAFH GTSAFDPCCP
GSSSRTAIYG HQAGAGPSQS ITIDGYGSSM VAQPQPQPPP QASLSSCRHY MHSPYASLTR
PLHHQASACP HSHGNPPPQP QPPPQVDYVI PHPVHPFHPS ISSHSSSHPV PPPPPPPTHP
LANAAAPIPQ HLPATHQPIS HHIPATAPPA QRLHPHEVIQ RMEVQRRRMM QHPTRAHERP
PPHPHRMHPN YGHGHHIHVP QTMSSHPRQA PERSAWELGI EAGVTAATYP PGPLHPHLAH
YHAPPRLHHL QIGALPLMVP DMAGYPHIRY ISSGLDGTSF RGPFRGNFEE LIHLEERLGN
VNRGATQGTI ERCTYPHKYK KVTTDWFSQR KLHCKQDGEE GTEEDTEEKC TICLSILEEG
EDVRRLPCMH LFHQVCVDQW LITNKKCPIC RVDIEAQLPS ES
//
