ID A0A0B0MDF1_GOSAR Unreviewed; 366 AA.
AC A0A0B0MDF1;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-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=F383_36711 {ECO:0000313|EMBL:KHF97433.1};
OS Gossypium arboreum (Tree cotton) (Gossypium nanking).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29729 {ECO:0000313|EMBL:KHF97433.1, ECO:0000313|Proteomes:UP000032142};
RN [1] {ECO:0000313|Proteomes:UP000032142}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. AKA8401 {ECO:0000313|Proteomes:UP000032142};
RA Mudge J., Ramaraj T., Lindquist I.E., Bharti A.K., Sundararajan A.,
RA Cameron C.T., Woodward J.E., May G.D., Brubaker C., Broadhvest J.,
RA Wilkins T.A.;
RL Submitted (SEP-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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KHF97433.1}.
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DR EMBL; JRRC01006813; KHF97433.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B0MDF1; -.
DR SMR; A0A0B0MDF1; -.
DR Proteomes; UP000032142; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
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; PTHR23328:SF0; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR23328; UNCHARACTERIZED; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000032142};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 141..180
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 366 AA; 41334 MW; 66F7566FC5DD4EC7 CRC64;
MVREEAKPAP EDSQQPNKAE TSQNVDNLFS PRFKSVAAMA GWDEEALIIA SFVVEDTPDR
QQSKQKKRSD SIFNTPPCTS SRRKRRAQRT PFNLDEEQEV PREESEKESM EQRIVVEDEK
NPKANEPALH CMNKLREELS CAICLDICFE PSTTPCGHSF CKKCLRSAAD KCGKRCPKCR
QLIGNGRSCT VNTVLWNTIQ LLFPKEVETR KAVAADALNS KEAFECQSPQ SGTRSTRTTR
TRTRTRVENQ ALAARLQRED ISRLVNSDTN MTRRRGDPNQ DNNAASARLQ RDNDLSRLVR
TGRRRGTPSQ DEDAALALRL QREEFMEAFR GSSGHEGNEQ TRIPLALARA NLRAMASRAI
NRGRAL
//