ID A0A0B0PVW6_GOSAR Unreviewed; 462 AA.
AC A0A0B0PVW6;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 03-MAY-2023, entry version 26.
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_14063 {ECO:0000313|EMBL:KHG27556.1};
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:KHG27556.1, 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};
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DR EMBL; KN441535; KHG27556.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B0PVW6; -.
DR Proteomes; UP000032142; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR CDD; cd16469; RING-H2_RNF24-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045191; MBR1/2-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22937; E3 UBIQUITIN-PROTEIN LIGASE RNF165; 1.
DR PANTHER; PTHR22937:SF174; RING/U-BOX SUPERFAMILY PROTEIN; 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 4: Predicted;
KW Ligase {ECO:0000313|EMBL:KHG27556.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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 411..453
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 72..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 462 AA; 50569 MW; A060FE230214E556 CRC64;
MPVDAVHFSS HWNSMPRSSG FATSSHNVEA PCYQPDTSGP SHDLFLHSSA PRTFGSAPEN
YMHHASSSNY DRQTFQGIDG GLVDLPMSSG RGPHKRKSPG VPSVCERGGS SRYAGAGSSS
DIPLSSDFWQ EKPNVDPQHM YWDHISMPPS CRGNGLSIRG ECSMRNVRSR PALDLESNLV
RTHLSSNTSY LTSHPVEHSS SVDITGQSSN AMSRDWSHLR MSPSHGRIPA ADSNVFNHET
NRFLGGSSAT NASVEVGGLQ HNFISGRNPV LPQGFHGNSA QSLRGPRTNY FQRSSPNFRA
SSSSVHIGHA ASYEEGMQVV SESYSTRYPR PLSAVTWRNN ERSGRSRISN DRYQSLADDA
AFHGRFSSEE LLALGERIGS VNTGLSEDLI SKCLAETIYS SSDQFQDESS CVICLEEYKD
MDEVGALKTC GHKYHIPCIK KWLSMKNTCP ICKASAVADD IK
//