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Database: UniProt
Entry: A0A5C7H969_9ROSI
LinkDB: A0A5C7H969_9ROSI
Original site: A0A5C7H969_9ROSI 
ID   A0A5C7H969_9ROSI        Unreviewed;      1455 AA.
AC   A0A5C7H969;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   08-NOV-2023, entry version 15.
DE   RecName: Full=HhH-GPD domain-containing protein {ECO:0000259|SMART:SM00478};
GN   ORFNames=EZV62_018939 {ECO:0000313|EMBL:TXG53683.1};
OS   Acer yangbiense.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Sapindales; Sapindaceae; Hippocastanoideae; Acereae; Acer.
OX   NCBI_TaxID=1000413 {ECO:0000313|EMBL:TXG53683.1, ECO:0000313|Proteomes:UP000323000};
RN   [1] {ECO:0000313|Proteomes:UP000323000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Malutang {ECO:0000313|Proteomes:UP000323000};
RX   PubMed=31307060; DOI=10.1093/gigascience/giz085;
RA   Yang J., Wariss H.M., Tao L., Zhang R., Yun Q., Hollingsworth P., Dao Z.,
RA   Luo G., Guo H., Ma Y., Sun W.;
RT   "De novo genome assembly of the endangered Acer yangbiense, a plant species
RT   with extremely small populations endemic to Yunnan Province, China.";
RL   Gigascience 8:0-0(2019).
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the DNA glycosylase family. DEMETER subfamily.
CC       {ECO:0000256|ARBA:ARBA00005646}.
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:TXG53683.1}.
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DR   EMBL; VAHF01000009; TXG53683.1; -; Genomic_DNA.
DR   Proteomes; UP000323000; Chromosome 9.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0035514; F:DNA demethylase activity; IEA:InterPro.
DR   GO; GO:0019104; F:DNA N-glycosylase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro.
DR   GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR   GO; GO:0080111; P:DNA demethylation; IEA:InterPro.
DR   CDD; cd00056; ENDO3c; 1.
DR   CDD; cd06222; RNase_H_like; 1.
DR   Gene3D; 1.10.1670.10; Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal); 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   InterPro; IPR044811; DME/ROS1.
DR   InterPro; IPR011257; DNA_glycosylase.
DR   InterPro; IPR003651; Endonuclease3_FeS-loop_motif.
DR   InterPro; IPR003265; HhH-GPD_domain.
DR   InterPro; IPR023170; HhH_base_excis_C.
DR   InterPro; IPR002885; Pentatricopeptide_rpt.
DR   InterPro; IPR028924; Perm-CXXC.
DR   InterPro; IPR044730; RNase_H-like_dom_plant.
DR   InterPro; IPR002156; RNaseH_domain.
DR   InterPro; IPR028925; RRM_DME.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   NCBIfam; TIGR00756; PPR; 1.
DR   PANTHER; PTHR46213:SF13; DEMETER-LIKE PROTEIN 2-RELATED; 1.
DR   PANTHER; PTHR46213; TRANSCRIPTIONAL ACTIVATOR DEMETER; 1.
DR   Pfam; PF15629; Perm-CXXC; 1.
DR   Pfam; PF13041; PPR_2; 1.
DR   Pfam; PF15628; RRM_DME; 1.
DR   Pfam; PF13456; RVT_3; 1.
DR   SMART; SM00478; ENDO3c; 1.
DR   SMART; SM00525; FES; 1.
DR   SUPFAM; SSF48150; DNA-glycosylase; 1.
DR   PROSITE; PS51375; PPR; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000323000};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   REPEAT          159..193
FT                   /note="PPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00708"
FT   DOMAIN          913..1055
FT                   /note="HhH-GPD"
FT                   /evidence="ECO:0000259|SMART:SM00478"
FT   REGION          29..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          473..582
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          641..662
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          805..898
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1431..1455
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        473..493
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        503..518
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        647..662
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        808..833
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        834..850
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        874..898
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1455 AA;  165878 MW;  1EDB1BECBE08041E CRC64;
     MVSKTSLVPS SSKTTFKARL LSSFTHSRNE VSSLSKHPNS KAKSMTEADP ARLRDSLHGK
     CKSGKIDLDE AHYLFDYMIH MQPTPHMSSF NILFTVLVKN NHYGDVISLQ NIMNSVGRGF
     NPNDVTFSRL IKGHTIVSLQ LHEQMVNGNS KYGGICKPGV VWYGIMIDGL CKDGFTDRAK
     ELFFEMKANG IPANAVTFTT LIHDTAEVLV GVSYRIEISR ISVLHVVLWQ VNTDAAVDLN
     DLRIGLGAVV RDNRGSVMAA CAQTSLVPVV VESDALQVVE FVSSQSPPSS EVGVVVLDIL
     QLIDSVPVTG VMFVLRLANV VVHSLAFVVV WEQGLEKKKL QRKMSKLKVY RRRKTRGRTD
     LEEKQLKREM SQLKVYQRRK TRSCIDLEEK QLQREMFPLK VYLRRKTRGR IDLKEKQFQR
     EMTPLKVYQR QRWKTRGRID LEEKQLQREC SWVPGTPAKL GNSEEENTNI FTTESSCSQN
     GQQTVQEDAV SEKQSENIQL KRKRQQKPKR KKHRPRVVVE GLKPKTPKPV TPKQTVPSKK
     RKYVRKSSRQ GNSVSEERRL PKRRKSSKKT SKNNPDVEVA EKTSCRKTLN FNLESGQFQP
     YVPSMFKKMR RRRLRRSDLA LLVAPPICNQ LPRLPAISRG VGRRSKMQGR NAQSSNSGDG
     TLVPYQEHYI RNRKRITGKV YLDPDTMRVW NQLMNLKDRD ANEEQTDPEK EDQWRREREI
     FQGRIESFTA RIHIILGDRR FKPWKGSVVD SVVGVYLTQN VSDCLSSSAY MSLAAKYPPK
     TTSNNTSSTG AAYDFEGNLL YFVTEPEPDR SPELKNREEP LDEEKDLKNV VEPHTFEDSS
     NVQLTPQRIN ESKAKHGFKS QDATIMRKIT SRGKGPKLKN DKAKKATPKE KKKDNKEKRD
     WDLFRKMYSS DEQSSSDQMD SVDWEAVRLA EPREVAMAIK DRGQQNVIAG RIQKFLTRLV
     EVHKSIDLEW LRHAPPDIVK EYLLEIPGLG LKSVECVRLL SLQHIAFPVD TNVGRIAVRL
     GWVPLEPLPE SLQIHLLEQY PLMNTIQKYL WPRLCNLDQR TLYELHYQLI TFGKVFCTKR
     NPNCGVCPLR GECKHFASAF ASARLALPRP SEKGIVYKRN PHVDVNPIPV TFLEAGMLPR
     PSEKGNPHVD VNPIPVTLLE ADLLSEAGIL NNCEPTIEEP ASPETQCTEM SSEPDLEDFC
     CGEPEEIPTI RLQDREFNIE QIQIFLETNK MMLQKSRDLV LLAAEATSMP APKLKSVNRL
     RTEHLVYVLP DNHLLLQGFG RRDTDDTCPY LLSIWTPGET PNSFEKPTKK CNSGESELCN
     EKTCYSCSTI QEQNADIVHG TILIPCRTAN IGRFPLNGTY FQVNEVFADH ETSHQPICVP
     RSMIAQLLTQ TAYFGTSATS IFRGLDLVEI QRCFWTGYIC VRGFERKNGA PRPLSRRLHT
     PPSKMGKAYD KWNDE
//
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