ID A0A498K6G6_MALDO Unreviewed; 1963 AA.
AC A0A498K6G6;
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=Myb/SANT-like domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=DVH24_015223 {ECO:0000313|EMBL:RXI01874.1};
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:RXI01874.1, ECO:0000313|Proteomes:UP000290289};
RN [1] {ECO:0000313|EMBL:RXI01874.1, 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:RXI01874.1};
RA Hu J.;
RT "A high-quality apple genome assembly.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the Rab GDI family.
CC {ECO:0000256|ARBA:ARBA00005593}.
CC -!- SIMILARITY: Belongs to the SPCS3 family.
CC {ECO:0000256|ARBA:ARBA00009289}.
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:RXI01874.1}.
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DR EMBL; RDQH01000330; RXI01874.1; -; Genomic_DNA.
DR STRING; 3750.A0A498K6G6; -.
DR EnsemblPlants; mRNA:MD04G0169500; CDS:MD04G0169500.1; MD04G0169500.
DR EnsemblPlants; mRNA:MD04G0170000; mRNA:MD04G0170000; MD04G0170000.
DR Gramene; mRNA:MD04G0169500; CDS:MD04G0169500.1; MD04G0169500.
DR Gramene; mRNA:MD04G0170000; mRNA:MD04G0170000; MD04G0170000.
DR Proteomes; UP000290289; Chromosome 4.
DR GO; GO:0005787; C:signal peptidase complex; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; IEA:InterPro.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 1.10.405.10; Guanine Nucleotide Dissociation Inhibitor, domain 1; 1.
DR Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR Gene3D; 1.20.1420.30; NCX, central ion-binding region; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR018203; GDP_dissociation_inhibitor.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR024752; Myb/SANT-like_dom.
DR InterPro; IPR004837; NaCa_Exmemb.
DR InterPro; IPR044880; NCX_ion-bd_dom_sf.
DR InterPro; IPR007653; SPC3.
DR PANTHER; PTHR46929; EXPRESSED PROTEIN; 1.
DR PANTHER; PTHR46929:SF3; MYB_SANT-LIKE DNA-BINDING DOMAIN PROTEIN; 1.
DR Pfam; PF00996; GDI; 2.
DR Pfam; PF00125; Histone; 1.
DR Pfam; PF12776; Myb_DNA-bind_3; 4.
DR Pfam; PF01699; Na_Ca_ex; 2.
DR Pfam; PF04573; SPC22; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF47113; Histone-fold; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000290289};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1208..1226
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1279..1301
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1313..1332
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1338..1360
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1442..1458
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1478..1498
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1510..1536
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1575..1598
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1610..1637
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1644..1664
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 347..424
FT /note="Myb/SANT-like"
FT /evidence="ECO:0000259|Pfam:PF12776"
FT DOMAIN 495..587
FT /note="Myb/SANT-like"
FT /evidence="ECO:0000259|Pfam:PF12776"
FT DOMAIN 677..770
FT /note="Myb/SANT-like"
FT /evidence="ECO:0000259|Pfam:PF12776"
FT DOMAIN 829..922
FT /note="Myb/SANT-like"
FT /evidence="ECO:0000259|Pfam:PF12776"
FT DOMAIN 1215..1357
FT /note="Sodium/calcium exchanger membrane region"
FT /evidence="ECO:0000259|Pfam:PF01699"
FT DOMAIN 1511..1661
FT /note="Sodium/calcium exchanger membrane region"
FT /evidence="ECO:0000259|Pfam:PF01699"
FT DOMAIN 1756..1867
FT /note="Histone H2A/H2B/H3"
FT /evidence="ECO:0000259|Pfam:PF00125"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1064..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1963 AA; 220965 MW; BE7A58D71B7552B7 CRC64;
MLHAMNDKKL GGGGGGGGGG GSAKKGGVID FPVQGGLAGV RVSDKAVRKA VATRKVRARA
MEAKRDMQQM GYMGQKGQMG QMGHVGNMGQ MGQRPQMSQM GRGAAEYGTP KNSLNQISLW
DGILPTKEHA KFWIHTSNKY RFIDQGTNLR GKEFNLTLHW HVMPKTGKMF ADKIVHKVPA
TDMEALKSPP MGLFEKRRAR KFILYVQDYS ETGPKTHEGM DLTRVTSRGF IVCLTSMSAK
DTISSMFFCI VRKVGKVAIV IAITSHPIPN TNESHSVKTY DRYEPINEPT LDNCFISTSY
DAITHFESIV LDVLNMYTLI TGKNSQTIEI SVIHRRGIGD GGWFFMVHRG NRLGHTFNKQ
AWNDMLMMFN GNFGTPYDMN TLKSHYTSLW RQFNDIKNLL DQNGFSWDNT RQMVIADKYA
WDAYVKVHPD AQVYRNKALM TFNDLCLIYA HTQADGRYSL SSHDIDFDDE IQGMIDGAGM
ISPTPASKVK RNADWKPAMD EFFLNLMLDQ LEKGRKMNNT FTKQAWKGMV TLFKKKFGSQ
YQTRFLKQLH KKLLKYYTDV RSILARNGFY WDENRQMIVA DDDVWGNCIQ ALPDARVYRK
KPLLNYQDLN SIYASEISNG LLNHLDQDEE EREGQFSFSG NGHLASFEDL DSEGLDFMTD
GEDIQSHGND IFSRKDWTPP MDRYLIDLLL EQLQKANKID YSLDDQAWVD VLVLFKERFG
LQYNKDLLRS RYKSLEKQYH DTKDLLDRRG FWWDETQQMV TAYDDVWDAY IKERPDTEAY
RTKSTPNYND LCLIYGNSNS GERYNQSGQA VGCNGDANYN HSYHRRTDWT PPMDRYFIDL
MLEQVRNGSM VNQKFSKLAW TDMVSKFRAQ FGSQHDKDVL KSRFVNLRKR FNDMKTLLDQ
SGFTWDEMQQ RITADGDLWD AHVKASSSHV LVQVRPDARS YRNRTLPNFN DLCLIYGNED
SLKREGSSNH SMDAEDDDPR VNVGDETQQT IFAEVDDVWD AYVKDHPYQP AYGNSILDYN
DSTMIYGNGV ADGRSSYLST EMGKTGFDMT FGGLQSRTMD YETSIQRKKR KPTASSTSAS
KRVQRTIKEE VQEALDEKPQ RVNGFVGNEE DKDCCSIERI VDALETVPDM NDELFLEASQ
ILEDESKAKM FVAMDVTARQ KWLFRKLRQS LIATAAKTPS CSSAAVTHSD GLFNYLYLHF
CLFRQNPFLS LSSLSLILLL LFYILIKTAQ DHFSLVTTKL VFALDLTPSM AAVTLLALGN
GAPDVFASVA AVRTGQYRTG FGAILSAGTF VSAFVVGFVA IYAAPFPLKP APFVRDVMFY
LTAALFLFYV YLSAEIYLWQ AVGFVGFYLF FVGLVFWMDL GMGGGGKESR VEAGSVGDIE
IQRGLVAPDS RIGHVLESSE DRKGSFGVGR ALGMISRAWE LPVSFLLKLT IPQASPSEWS
RFYMSANIAL CPLALLYACN SFMPFNHPVV FLLSNTHLPL WLVILLASSS LALLHYAVEK
DPPKTEQLPV LLIAFVMSVF WISTTAGELL NCLAALGTLL ELPPALLGLT VLAWGNSVGD
LVADVAVAKA GHPAMAMAGC FAGPMFNMLI GLGTALVIQT YDVYPEAYEL QFHVGIVIAF
VFLLLSLMGS LLVITWCRFR VPRFWGFCLV GLYVVFMAVS LVIAKFTGCS IISNPLQKQR
PPPTPFLSFV SIRAELQSST RMDPQGHNQP QSMGMVGSGA QLTYGSNPYQ HNQMVGSPNP
GSVAATVGAM QSASQSPGAQ LAQHQLAYQH IHQQQQQQLQ QQLQTFWANQ YQEIDKVTDF
KNHSLPLARI KKIMKADEDV RMISAEAPVI FARACEMFIL ELTLRSWNHT EENKRRTLQK
NDIAAAITRT DIFDFLVDIV PREDLKDEVL ASIPRGTVSV GGPADALPYC YMPPQHAPQV
GDPGMIMGKP MMDPSLYAQQ SHPYMTQPMW QQAPDQQQSP SDH
//