ID   A0A498IHJ2_MALDO        Unreviewed;      1328 AA.
AC   A0A498IHJ2;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=RanBP2-type domain-containing protein {ECO:0000259|PROSITE:PS50199};
GN   ORFNames=DVH24_035036 {ECO:0000313|EMBL:RXH81615.1};
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:RXH81615.1, ECO:0000313|Proteomes:UP000290289};
RN   [1] {ECO:0000313|EMBL:RXH81615.1, 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:RXH81615.1};
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:RXH81615.1}.
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DR   EMBL; RDQH01000338; RXH81615.1; -; Genomic_DNA.
DR   STRING; 3750.A0A498IHJ2; -.
DR   Proteomes; UP000290289; Chromosome 12.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 2.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR001876; Znf_RanBP2.
DR   InterPro; IPR036443; Znf_RanBP2_sf.
DR   PANTHER; PTHR43689; HYDROLASE; 1.
DR   PANTHER; PTHR43689:SF14; LYSOPHOSPHOLIPASE BODYGUARD 4-RELATED; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   Pfam; PF00641; zf-RanBP; 2.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   SMART; SM00547; ZnF_RBZ; 2.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR   PROSITE; PS01358; ZF_RANBP2_1; 2.
DR   PROSITE; PS50199; ZF_RANBP2_2; 2.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000290289};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00322};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322}.
FT   DOMAIN          283..312
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   DOMAIN          315..345
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   REGION          62..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          437..560
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          594..768
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1282..1309
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        437..512
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        545..560
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        594..611
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        612..626
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        642..752
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1328 AA;  149609 MW;  0CF713ED301508A1 CRC64;
     MLLHVQMGGA SNRFFTILST TTTSHPFHRF PSLLRLSRQY KPPLFPSSLS FLSHRHSLTS
     RPSSSASSFP PGSSHHFHSH SPVSSAYPSS SADSATFPAS HPWPEWSHLL NSLSAAGYNG
     VNGQDEFTAA VRDLPEDFMR AASVCLALAR QRAGLLRLLS RRDLEVVVEN GTPFLFQNGD
     DSARRMRLFL GQGSTNALGI DKAQTIDLMR FILSYASNPV FSSERNNLYN REIVESSVRT
     LLSELAKLCY SVPDSNSIGS MQSRSSDNFG ESARPFEKTI EMKRGDWICQ RCNFMNFARN
     MKCLECEEAQ PKRELTGKEW ECPQCDFFNY GRNMVCLRCD CKRPGEVSRG STNDGLDMGY
     VNMGDKSQAN IDSRLAANEE KAQRWFSKIS QLDSTSDMSS AVSDEDFPEI MPLRKGVNRF
     VVSTRKTPLE RRLANAQYQR NVDNEGSYQG KDLQSGSVNR SLGRTPNRTL DEILGHVNTS
     TNPRQNVGTD TPSSISSSVS SEYGQPRGGN SNYPQFVPLP ADSFAKKPEN SSVEESMQLS
     EKPPEQAGSK DEERDQAEKS ERWFKRVAEL HDVTNLASAI SDEDFPEIMP MRKGENRFVV
     SKKKDRSLTT PASKRHTATE QPNNGNYVPF VPFPPDYFAK KKNQQTDLTN KIADESTSTT
     MPDNSSDSLV DARSHVQQVK NQQSNVPSWY SENSGQNQFG DSAPSFANSS SYGMDGLNIG
     SSGKEKSNQT ASSTGNSPQQ SNDQNIRQGW SGKSLEGSAV KEPDPLDMSE EAKAERWFKR
     VAQIKDISEL SQIPDEDFPS IMPMRKGVNR FVVSKRKTPL ERRLTSPQHR KNLPVVSSDP
     AKERDTKWRN PTTTLVSALN FIVFLVFDFL DTFLCVVYRY IDELFEGQEA SSCYCTDKEE
     QEARRNGDGE EGEELSLSET LYERKNVFRK MGFLGYAKKW RKSKSENPGK VKNQKNRWSD
     CGCQSCVSWT NDAAQKLHFV IGEPEPSSQA LTDEDCRGKP PENVIFLHGF LCSSSFWTET
     VFPNLSEHGK RNYRLFAVDL LGFGRSPKPR DCFYTLKDHL EMIEKSVICP FQLSSFHLVA
     HSMGCLIAIA LAAKHPELVK SVTLVAPPYF PSKDGDSLRV LEKLAARKLW PPFVFGTSFM
     SWYEHLGRCV CFLVCRHHRT WETIAKLLTR RRDLHFMAVD FTRHTHHSAW HTMHNVICGG
     AKLMEGYLQV LSKAGVKICV IHGDRDNVVP MECSNNIQMA APDAEVNIVK NTNHNSVIFG
     RERDFTRHME IGSDPPKSKE RLACTRDHAR ALREDLHALD NEIVTLSQSS LVGYIQKAIF
     GRFYWFFR
//