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Database: UniProt
Entry: A0A1U8NWT5_GOSHI
LinkDB: A0A1U8NWT5_GOSHI
Original site: A0A1U8NWT5_GOSHI 
ID   A0A1U8NWT5_GOSHI        Unreviewed;       893 AA.
AC   A0A1U8NWT5;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   08-OCT-2025, sequence version 2.
DT   28-JAN-2026, entry version 32.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=LOC107952768 {ECO:0000313|RefSeq:XP_016743427.2};
OS   Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=3635 {ECO:0000313|Proteomes:UP000818029, ECO:0000313|RefSeq:XP_016743427.2};
RN   [1] {ECO:0000313|Proteomes:UP000818029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. TM-1 {ECO:0000313|Proteomes:UP000818029};
RX   PubMed=32313247; DOI=10.1038/s41588-020-0614-5;
RA   Chen Z.J., Sreedasyam A., Ando A., Song Q., De Santiago L.M.,
RA   Hulse-Kemp A.M., Ding M., Ye W., Kirkbride R.C., Jenkins J., Plott C.,
RA   Lovell J., Lin Y.M., Vaughn R., Liu B., Simpson S., Scheffler B.E., Wen L.,
RA   Saski C.A., Grover C.E., Hu G., Conover J.L., Carlson J.W., Shu S.,
RA   Boston L.B., Williams M., Peterson D.G., McGee K., Jones D.C., Wendel J.F.,
RA   Stelly D.M., Grimwood J., Schmutz J.;
RT   "Genomic diversifications of five Gossypium allopolyploid species and their
RT   impact on cotton improvement.";
RL   Nat. Genet. 52:525-533(2020).
RN   [2] {ECO:0000313|RefSeq:XP_016743427.2}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (AUG-2025) to UniProtKB.
CC   -!- FUNCTION: Functions as an E3 ubiquitin ligase.
CC       {ECO:0000256|ARBA:ARBA00003861}.
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}.
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DR   RefSeq; XP_016743427.2; XM_016887938.2.
DR   AlphaFoldDB; A0A1U8NWT5; -.
DR   GeneID; 107952768; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000818029; Chromosome D07.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd16655; RING-Ubox_WDSUB1-like; 1.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   CDD; cd01989; USP_STK_Ubox_N; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR051348; U-box_ubiquitin_ligases.
DR   InterPro; IPR003613; Ubox_domain.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45647; OS02G0152300 PROTEIN; 1.
DR   PANTHER; PTHR45647:SF100; U-BOX DOMAIN-CONTAINING PROTEIN 33; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF04564; U-box; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00504; Ubox; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS51698; U_BOX; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000818029};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          541..804
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          822..893
FT                   /note="U-box"
FT                   /evidence="ECO:0000259|PROSITE:PS51698"
FT   REGION          219..320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          371..513
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        219..257
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..302
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        307..320
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         568
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   893 AA;  99928 MW;  F2588869DC896116 CRC64;
     MALVSVVPAI TEGMNSMRFC DVRAPGILSS GREIVEETVA RIIEEKIYVA VGKNVDKYKS
     VLFWALQHSG GKKICIIHVH QPAKMIPVSE MGTKFPASKL EEQEVKAYWE IERKNMEKML
     NDYLLLCLQR GVQAEKLYIE RDSIEQGILE MISENRIRML VMGGAADKHY SKKVVDLKSK
     KAIFVRENAP NTCHTIWFLC KGLLIYTRKL SSDVTDTKVA SSSLPASPNL ESSENHFRSQ
     SVILRQTSRV KPSTSAPDSL RRVRSENVYG HVGSTLGFPS PDGNEGLSTP WNRSDVEGSS
     NEWDGLSRSP QNSVLSSSSS NGMADAALVP YMGTEVNGNG LQSSLIPHAE GNFNLSSLPN
     IQDVTTDNTL YDQLQKVMAE ATNSRREAFE EAMKRSEAEK DALVSIRRVK ASEILYAQEL
     KQRKEIEEAL AKEKDELGKM KNQRDEVRIE LQAALGQKSS LENQIAESEK EVKELQEKIF
     SAVELLQNYK KERDELQMER DNALKEAEEL RKSRAEPSGA HMHQFFTEFS FTEIEEATLN
     FDPSLKIGEG GYGSIYKGNL RHTTVAIKRL HSNSLQGPSE FQQEVDVLSK MRHPNLVTLI
     GACPDAWTLI YEYLPNGSLE DRLSCRGNSP PLSWQTRIRL ATELCSVLIF LHSSKPHGIV
     HGDLKPANIL LDANFVTKLS DFGICRLLSD NTTICCRTDP KGTFAYMDPE FLSTGELTQK
     ADVYSFGVIL LRLLTGRQAL GIIKEVQYAL DNGSLKNLLD PLAGDWPFVQ AEQLANLALR
     CCEMNRRCRP DLSTDVWRVL EPMRASCGGS SSFQLGSEEQ CHPPSYFICP IFQEVMQDPH
     VAADGFTYEA EALRGWLDSG HDTSPMTNIK LAHSNLVPNL ALRSAIQEWL QQH
//
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