ID A0A5E4E2N8_PRUDU Unreviewed; 1459 AA.
AC A0A5E4E2N8;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE SubName: Full=PREDICTED: zinc finger {ECO:0000313|EMBL:VVA09845.1};
GN ORFNames=ALMOND_2B020385 {ECO:0000313|EMBL:VVA09845.1};
OS Prunus dulcis (Almond) (Amygdalus dulcis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=3755 {ECO:0000313|EMBL:VVA09845.1, ECO:0000313|Proteomes:UP000327085};
RN [1] {ECO:0000313|Proteomes:UP000327085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Texas {ECO:0000313|Proteomes:UP000327085};
RX PubMed=31529539; DOI=10.1111/tpj.14538;
RA Alioto T., Alexiou K.G., Bardil A., Barteri F., Castanera R., Cruz F.,
RA Dhingra A., Duval H., Fernandez I Marti A., Frias L., Galan B.,
RA Garcia J.L., Howad W., Gomez-Garrido J., Gut M., Julca I., Morata J.,
RA Puigdomenech P., Ribeca P., Rubio Cabetas M.J., Vlasova A., Wirthensohn M.,
RA Garcia-Mas J., Gabaldon T., Casacuberta J.M., Arus P.;
RT "Transposons played a major role in the diversification between the closely
RT related almond and peach genomes: results from the almond genome
RT sequence.";
RL Plant J. 101:455-472(2020).
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DR EMBL; CABIKO010000001; VVA09845.1; -; Genomic_DNA.
DR Gramene; VVA09845; VVA09845; Prudul26B020385.
DR Proteomes; UP000327085; Chromosome 7.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR CDD; cd00072; GYF; 1.
DR CDD; cd15568; PHD5_NSD; 1.
DR CDD; cd10567; SWIB-MDM2_like; 1.
DR FunFam; 3.30.40.10:FF:000303; Zinc finger CCCH domain-containing protein 19; 1.
DR FunFam; 3.90.70.200:FF:000002; Zinc finger CCCH domain-containing protein 19; 1.
DR Gene3D; 3.30.1490.40; -; 1.
DR Gene3D; 3.90.70.200; Plus-3 domain; 1.
DR Gene3D; 1.10.245.10; SWIB/MDM2 domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR003169; GYF.
DR InterPro; IPR035445; GYF-like_dom_sf.
DR InterPro; IPR058668; NERD_dom.
DR InterPro; IPR004343; Plus-3_dom.
DR InterPro; IPR036128; Plus3-like_sf.
DR InterPro; IPR019835; SWIB_domain.
DR InterPro; IPR036885; SWIB_MDM2_dom_sf.
DR InterPro; IPR003121; SWIB_MDM2_domain.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46695:SF4; ZINC FINGER CCCH DOMAIN-CONTAINING PROTEIN 44; 1.
DR PANTHER; PTHR46695; ZINC FINGER CCCH DOMAIN-CONTAINING PROTEIN 44-RELATED; 1.
DR Pfam; PF02213; GYF; 1.
DR Pfam; PF25980; NERD_plant; 1.
DR Pfam; PF03126; Plus-3; 1.
DR Pfam; PF02201; SWIB; 1.
DR SMART; SM00444; GYF; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00719; Plus3; 1.
DR SMART; SM00151; SWIB; 1.
DR SUPFAM; SSF90229; CCCH zinc finger; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF55277; GYF domain; 1.
DR SUPFAM; SSF159042; Plus3-like; 1.
DR SUPFAM; SSF47592; SWIB/MDM2 domain; 1.
DR PROSITE; PS50829; GYF; 1.
DR PROSITE; PS51360; PLUS3; 1.
DR PROSITE; PS51925; SWIB_MDM2; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 330..413
FT /note="DM2"
FT /evidence="ECO:0000259|PROSITE:PS51925"
FT DOMAIN 473..606
FT /note="Plus3"
FT /evidence="ECO:0000259|PROSITE:PS51360"
FT DOMAIN 787..841
FT /note="GYF"
FT /evidence="ECO:0000259|PROSITE:PS50829"
FT DOMAIN 1434..1459
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 1434..1459
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 925..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1223..1250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..13
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..908
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..954
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..984
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1002
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1036
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1077..1100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1459 AA; 159869 MW; 3CD23E6B29F06B34 CRC64;
MELQKAQLSS TFYRPSLEED GGGGREEQPQ AFDRSLPTAE DRMSVDQCEA IGDLDDSRLV
GVPQTVAGGG MVAGRVGQMM ADVAVKVAAE KSLGKRRRGR PPSGHVRATP VRKQNEEEDV
CFICFDGGSL VLCDRRGCPK AYHPSCIKRD ESFFRSKAKW NCGWHICSSC QKASHYWCYT
CTYSLCKGCT KDADYQCVRG NKGFCGTCMR TIMLIENVQG NKEVAQVDFD DKSSWEYLFK
VYWSLLKGKL SLTLDELINA KNPWKGGAVV VCKRDSSGEL YNGDKTTDSI SLNSFADLEA
THSKRSNKKP RISNKDLTVE KSLGGRGMPF SEGTVWASKE LLAFVAHMKN GDISVLSQFD
VQALLLEYIK KNSLRDPRRK CQIVCDSRLI NLFGRECVGH FEMLKLLESH FLIKESSRAD
NISSAAVVTS VSSQMEFDGI HDNQMMMGND KRRKTRKRVD EKGPQTNPAA YAAIDVHNIN
LIYLSRNWME ILIEDIDKFH EKVVGSVVRI RISSGDQKQE IYRLVQVIGT SKVAEPYKIG
TRTTDVKLEI LNLDKKEVIS IDEISNQEFT QDECKRLRQS IRCGLTKRLT VGEIQEKAMA
LQAVRVNDLL EAEVLRLNHL RDRASEKGHR KELRECVEKL QLLNSPEERQ RRLHETQEVH
PDPSMDPSYE SEDSAGDFNK RQDDKVKPRK SVFSRKGREP FPQPWEGDIS NNIGGMAQKN
RGRETFGING CSTIKNQVNP TGLTAFDWNN QSVVESNTST ELASEISSLP LSAVMKTDLS
VDNFETDKIW HYHDPTGKIQ GPFAMIQLRK WSTTGHFPLD HRIWRINEKP DDSILLADAV
NGQYYKELLL PHDSHLLSQG FTVAMDERNN GQDAGSNKSM NATEIDGKKV EESWNTKQDG
QSLHNNGNVE PVRCTTAVDV VNSNEEQTGN HLQGQDPLKG NSSSPNKAQE SGSLPSPVVP
VKPYETLEGE SRGAENNSDQ NNGNLDPPKT AQGQIMNGQC TENRSDSEGH SGQSSGQNWR
PPPVSSPSNG CDSNSDLIPL SKSCETSEQD QRELSFPDIP SPTPKPSNGD LLGQAAENKQ
SVSSNFPVQD SGPSWSTASS LGGGGAQLPE VGGEWGGYSP TPAKPTSLEE WESSLVSASS
LKPSEMAGDC VATAVSVSGQ LTHSSPSHPT SNASGWQDIL TGSTEFCTLA GESVSDLLAE
VEAMESLSGL ATPTSIMNCG GEFTEGSKNE SISSVEGFSP PDPGKGDALS SSGDLRVPMV
TDEPLGECQG NAIDLQKGCG VHSSTSAEVE GDRKPSDVSV NQWEAGTEIQ NTAPPKENWD
IASTDNHWKA RSESTETSWE AAQGNANMGW GGSEQGGANT GWGGGQGIAQ GNTSIHPGTP
AGAMLESQSR YGGDRFIGPR DRGFQNRDVG FGRGRFQWNR QTYGNGGGSF RPPPKGQRVC
KYYESGYCKK GASCGYLHP
//
