ID A0A067HCC4_CITSI Unreviewed; 379 AA.
AC A0A067HCC4;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=CISIN_1g037216mg {ECO:0000313|EMBL:KDO85421.1};
OS Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO85421.1, ECO:0000313|Proteomes:UP000027120};
RN [1] {ECO:0000313|EMBL:KDO85421.1, ECO:0000313|Proteomes:UP000027120}
RP NUCLEOTIDE SEQUENCE.
RG International Citrus Genome Consortium;
RA Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
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 -!- SIMILARITY: Belongs to the RING-type zinc finger family. ATL subfamily.
CC {ECO:0000256|ARBA:ARBA00024209}.
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 EMBL; KK784873; KDO85421.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067HCC4; -.
DR PaxDb; 2711-XP_006464383-1; -.
DR eggNOG; KOG0800; Eukaryota.
DR Proteomes; UP000027120; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR CDD; cd16461; RING-H2_EL5-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45768:SF16; E3 UBIQUITIN-PROTEIN LIGASE ATL4; 1.
DR PANTHER; PTHR45768; E3 UBIQUITIN-PROTEIN LIGASE RNF13-LIKE; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000027120};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT TRANSMEM 95..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 177..219
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 379 AA; 42282 MW; CB0606C9D9FB60C0 CRC64;
MTPFSRDRHV ISILARSQSQ HQCMMIYYLS PMIIHLSVYK RNSPAPDYSS LFHSFSPLSS
SSSLTPPPYD LFTYNNTQHS HHRSLSSMEN LKPSLIIIIL ILAITVFLSI SLCLLLRHLN
RRCLRHLSTV TTVSSADSRR VSSRRVSPDN PAFSVMDSLP LFAFSSVSRR SSSGGDCAIC
LFKFEPHDQL RLLPLCCHAF HARCIDTWLE SNLTCPLCRS PIIATETDVM KAIHASSGGG
SDSFRLEIGS ISRRQAGNEP PGEPQRRSYS LGSFDYVVDE ESDITTSQIH RGSMSDKEEV
GAQAASEANL ASEVAAGRSW LKDYVDRLSF SVSSRAMSFR SSGRFFTGSS RQSDVGDYDM
ETNRVGEEIS EFFRWFSGV
//
