ID A0A1S3ATK7_CUCME Unreviewed; 808 AA.
AC A0A1S3ATK7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=LOC103482570 {ECO:0000313|RefSeq:XP_008437017.1};
OS Cucumis melo (Muskmelon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3656 {ECO:0000313|Proteomes:UP000089565, ECO:0000313|RefSeq:XP_008437017.1};
RN [1] {ECO:0000313|Proteomes:UP000089565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DHL92 {ECO:0000313|Proteomes:UP000089565};
RX PubMed=22753475; DOI=10.1073/pnas.1205415109;
RA Garcia-Mas J., Benjak A., Sanseverino W., Bourgeois M., Mir G.,
RA Gonzalez V.M., Henaff E., Camara F., Cozzuto L., Lowy E., Alioto T.,
RA Capella-Gutierrez S., Blanca J., Canizares J., Ziarsolo P.,
RA Gonzalez-Ibeas D., Rodriguez-Moreno L., Droege M., Du L.,
RA Alvarez-Tejado M., Lorente-Galdos B., Mele M., Yang L., Weng Y.,
RA Navarro A., Marques-Bonet T., Aranda M.A., Nuez F., Pico B., Gabaldon T.,
RA Roma G., Guigo R., Casacuberta J.M., Arus P., Puigdomenech P.;
RT "The genome of melon (Cucumis melo L.).";
RL Proc. Natl. Acad. Sci. U.S.A. 109:11872-11877(2012).
RN [2] {ECO:0000313|RefSeq:XP_008437017.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Functions as an E3 ubiquitin ligase.
CC {ECO:0000256|ARBA:ARBA00003861}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR RefSeq; XP_008437017.1; XM_008438795.2.
DR AlphaFoldDB; A0A1S3ATK7; -.
DR GeneID; 103482570; -.
DR OrthoDB; 1118232at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000089565; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd16655; RING-Ubox_WDSUB1-like; 1.
DR CDD; cd01989; STK_N; 1.
DR Gene3D; 3.40.50.620; HUPs; 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; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45647; OS02G0152300 PROTEIN; 1.
DR PANTHER; PTHR45647:SF15; U-BOX DOMAIN-CONTAINING PROTEIN 35; 1.
DR Pfam; PF00069; Pkinase; 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:UP000089565};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 455..717
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 737..808
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REGION 181..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 328..387
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 194..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 482
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 808 AA; 90539 MW; 5D1443AE02ABE798 CRC64;
MEVTADQAKK NHMLLPSSSP VVAVAISGKK NSKYIIRWSL EKFLPEGIID FKLLHFFPRI
TSVPTPMGNA IPVSQVREDV AVAYRKEIWW QTSEKLLPFK KMFAQRKVHV DVVTLEADDV
VDAIIEEVTK CSINKLVIGV SSQGLFSRKL SGLSSRISAL APRYCTVYAI SKGKLASIRP
PDMDTDVSIR DDASEESSAS SYSSYTSSSL TDGSSSLTTS YSHFPSPSPS LPLQRFQALS
TINQPLLTKK PSLIKADHSR CQSIDIEVVD GVRSSSHVSD CTQTLSRASS SKSSPTENQS
WISDEASSSG AFNDYSSCES QADVSFELEK LRIELRHARG MYAIAQRETI DASRELNHLN
KQRSEEARKL EEINNKVVAA KEFAREERVK HEALRREAKY VKERAEREGI YRKEAETKAL
QDAKEKGKHE NALQGPLQQY QHFQWEDIVS ATLSFSEDLK IGMGAHGTVY KCSLHHTTVA
VKVLHSRDSH KQMQLLQELE VLSRIHHPHL LLLLGACPDK NCLVYEYMEN GSLEDRLYRR
GNTPAIPWYE RFRIAWEIAS ALVFLHSSKP KSIIHRDLKP ANILLDQNLV SKIGDVGLST
VFNSDPSMST AFMNSGPVGT LCYIDPEYQR TGLISPKSDV YAFGMVILQL LTAKPAVALT
HVVETAIDNS NLIKVLDIEA GHWPLEETYE LARLGLRCAE MQRKDRPDLK DQVLPLLMTL
KKVADEARNF ASKVPAAIPN HFICPILQDV MNDPCVAADG YTYDRQAIEK WLQKNDNSPM
TKLPLPDKNL IPNYSLLSAI VEWNSKRS
//
