ID A0A0D2RWL2_GOSRA Unreviewed; 410 AA.
AC A0A0D2RWL2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=U-box domain-containing protein {ECO:0000256|RuleBase:RU369093};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU369093};
DE AltName: Full=RING-type E3 ubiquitin transferase PUB {ECO:0000256|RuleBase:RU369093};
GN ORFNames=B456_006G149000 {ECO:0000313|EMBL:KJB36259.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB36259.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB36259.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
CC -!- FUNCTION: Functions as an E3 ubiquitin ligase.
CC {ECO:0000256|RuleBase:RU369093}.
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 ECO:0000256|RuleBase:RU369093};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU369093}.
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DR EMBL; CM001745; KJB36259.1; -; Genomic_DNA.
DR RefSeq; XP_012485723.1; XM_012630269.1.
DR AlphaFoldDB; A0A0D2RWL2; -.
DR EnsemblPlants; KJB36259; KJB36259; B456_006G149000.
DR Gramene; KJB36259; KJB36259; B456_006G149000.
DR eggNOG; ENOG502QR5G; Eukaryota.
DR OMA; CATYLKD; -.
DR OrthoDB; 5489991at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000032304; Chromosome 6.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR CDD; cd16664; RING-Ubox_PUB; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR045185; PUB22/23/24-like.
DR InterPro; IPR045210; RING-Ubox_PUB.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22849:SF24; E3 UBIQUITIN-PROTEIN LIGASE PUB24; 1.
DR PANTHER; PTHR22849; WDSAM1 PROTEIN; 1.
DR Pfam; PF04564; U-box; 1.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000032304};
KW Transferase {ECO:0000256|RuleBase:RU369093};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU369093}.
FT DOMAIN 7..83
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
SQ SEQUENCE 410 AA; 46066 MW; A2FD99E42E47C5A8 CRC64;
MEDIDVEVPK YFICPISLQI MRDPVTAITG ITYDRESIEQ WLLKGKSTNC PVTQQPLPTV
SDLTPNHTLR RLIQAWCNEN ASLGVDRIPT PKPSIDKLHF LKLIKQLQHP DSKMKALKEL
DLLAAKNERN RKYMVEAGVP KAMLSFIVNC FKEDCVSGLE EALSVLFLIR IPSAEAKLLP
KQNDQIIKSL IWVLGCEFNT QVMVKSHAVS ALKSIIETAS SVVLERLEPK FFEMIVGVLK
QCTTRITQQG INSALHVLLD ACPWGRNRLM MVESGAVSAL IELELGSPEK RTTELILGIL
FHLCSCADGR AEFLRHKGGI AVVTKRIMRV SPAADDRAVL ILSLISKFSA TSWVVHEMLE
VGTVTKLCML LQLDCATYLK EKTMEILRSH SDDWLKFPCI DKTVLTRYIK
//
