ID M7BQ33_CHEMY Unreviewed; 685 AA.
AC M7BQ33;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=UY3_08663 {ECO:0000313|EMBL:EMP34158.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP34158.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; KB533688; EMP34158.1; -; Genomic_DNA.
DR RefSeq; XP_007061571.1; XM_007061509.1.
DR AlphaFoldDB; M7BQ33; -.
DR STRING; 8469.M7BQ33; -.
DR eggNOG; KOG2177; Eukaryota.
DR OrthoDB; 207577at2759; -.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR047153; TRIM45/56/19.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR25462; BONUS, ISOFORM C-RELATED; 1.
DR PANTHER; PTHR25462:SF304; E3 UBIQUITIN-PROTEIN LIGASE TRIM56; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF101898; NHL repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50119; ZF_BBOX; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 19..58
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 88..138
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 153..194
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT REGION 366..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..405
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 685 AA; 76875 MW; 804824528D3AF0EA CRC64;
MALTFMSLQE LIREDFLTCK ICYDLYTVPK ILPCLHSYCQ HCLEPLVRDG ALQCPECRLQ
TDVPGGASNL KTNFFINSLL ELFQIKHNRD LACTVCSDAQ KILTATARCL DCKDFLCQSC
TQGHCCSRLT LHHKVVKLEE FLAGEYDAEM RLLQELCCQD HQQEALRFFC DTCSAPICRD
CRMLDHFQHK VVSMANAVQR ERPSVEQLID SLAGTITCIS EQEKAVEETI DKLKTSGENI
KERITKYVDD IISYLLAQKE AVLGELSAFL TQQMEGCRLV KEELQSQKDK AISTREFSQR
VLYVGKDYEI LHLEGMIRNR IQELQTYIPR KLESQIPELA IAWDQPEMLS EAALFSLVFP
REQPEGDMET VFEPDSEASA SPSEESEDDP DLPLDSEDQE DSCPSSEESA PDTPDKNPSC
CSRRSKRPKR VCTFEVDQCW SQAKPNITGI AVLPHAGGIL LLDQENDEIK QYSASGHFQQ
SIPLPDSDGV FCGISLCGDV LACSSDSFLF FLTLEGKFLR KLLLRGSESS YAITSYEDSY
IAVSEGTLCS ISLYSPSGHC VGRVAPTDYH GGKFLFIAVN DWEEFIVSDF IKKQIVIIEK
SGLILNVLKT SHSLLTKPFS VCVDVSSNIF VVDQLKVIKF SPDGETGEVV LSNQSRLKRP
RVLAVDDGGR LVLVQEDGYV HIYCF
//
