ID A0A498HYC3_MALDO Unreviewed; 982 AA.
AC A0A498HYC3;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=DVH24_039519 {ECO:0000313|EMBL:RXH75820.1};
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750 {ECO:0000313|EMBL:RXH75820.1, ECO:0000313|Proteomes:UP000290289};
RN [1] {ECO:0000313|EMBL:RXH75820.1, ECO:0000313|Proteomes:UP000290289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC TISSUE=Young leaf {ECO:0000313|EMBL:RXH75820.1};
RA Hu J.;
RT "A high-quality apple genome assembly.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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:RXH75820.1}.
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DR EMBL; RDQH01000341; RXH75820.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498HYC3; -.
DR STRING; 3750.A0A498HYC3; -.
DR Proteomes; UP000290289; Chromosome 15.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd16587; RING-HC_TRIM32_C-VII; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR44489; -; 1.
DR PANTHER; PTHR44489:SF11; F-BOX_WD REPEAT-CONTAINING PROTEIN A; 1.
DR Pfam; PF00400; WD40; 2.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00184; RING; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000290289};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT TRANSMEM 886..909
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 20..65
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 148..477
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 559..598
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 689..728
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 913..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..982
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 982 AA; 107686 MW; 7DFA2164E6E92A6A CRC64;
MSLACGGDME SMESPELPEC PVCLQNYDSE STIPRVLACG HSACEACLVR LPERYPETIR
CPACTQLVKY PPQGPTALPK NIDLLSFSLS LHPNPNSGIS QTPHKQSADG VGSFLPCIWS
DEFYIKWKDW VLPSDAVSVE TEVDDGTRDE LCTVLKGRTG SGFGSGRVWF REDESVSLFR
VGSLPGSDSS GFEFSYTARV LKCLSGMREE ERNEMGLLLR VSLSHCRRVC KVYGFWGNLE
DGFLYLGCER RNRSFSGKLG AGEDGFTKDG LPAFAMIAME VCEVVSGLNS EGFVAGCFGF
SCFSFDDFGH VEVDLNEVLV TGRKVWRSVV DSVSGGIGTE STDAEVLKLA FWNLFKDGDF
VSPEVLIELL QKQGFAVECD SSRYPVGCGS DVWSLACVFL RLLLGKEFDE ELVKNCGISF
FDHVTYASWI ERVRALIEGR LGQEYASLRE NLCKCLNYDP ASRPLVMDLM KCIRELIIKP
QCDIMASLEG VIKEDSRSFC LILGQLCGTS KEILETAKEN GLQGSEISGG SDFDQVGDER
ADSDFVDGLA GGKVKFKILQ GHRDAITALA VGGDFLFSSS FDKTIHVWSL QDFSHVHTFK
GHEHTIKALI YVDEEQPLCI SGDSGGGIFV WGTCTPLRQE PLKTFHEDKD WRFSGIHALA
CRNGYVYTGS GDRTVKAWSV RDGTLSCTMS GHRSVVSTLA VCDGVLYSGS WDGTIRLWSL
SDHSPLTVLG EDTSGTVASV LSLAVDRHML IATHDNGCVK VWRNDVFMKS IKMHNGAVFA
SGIEGKWLFT GGLDKTVNVQ YFYVMKLVCY VIKLLNSCKF ICVSQELSGD EFQIDSRLIG
SIPCDSVITT LLGWQGKIFV GCANRNIVVS YYETSSDCVI KIFRCFVGFL VLHLAWLGVA
SGFLHLGMVG GRGQGGRRPI GGATDELGLS GGESDDGAHE FSEFLMSSPI EIRIEGWGRG
EGENASREES RGREQRAIEG IS
//