ID A0A9Q1LQN1_9SOLA Unreviewed; 1887 AA.
AC A0A9Q1LQN1;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 08-OCT-2025, entry version 10.
DE RecName: Full=C3H1-type domain-containing protein {ECO:0000259|PROSITE:PS50103};
GN ORFNames=K7X08_002420 {ECO:0000313|EMBL:KAJ8541604.1};
OS Anisodus acutangulus.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Hyoscyameae;
OC Anisodus.
OX NCBI_TaxID=402998 {ECO:0000313|EMBL:KAJ8541604.1, ECO:0000313|Proteomes:UP001152561};
RN [1] {ECO:0000313|Proteomes:UP001152561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. KIB-2019 {ECO:0000313|Proteomes:UP001152561};
RX DOI=10.1073/pnas.2302448120;
RA Wanga Y.-J., Taina T., Yua J.-Y., Lia J., Xua B., Chenc J., D'Auriad J.C.,
RA Huanga J.-P., Huanga S.-X.;
RT "Genomic and structural basis for evolution of tropane alkaloid
RT biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 120:e2302448120-e2302448120(2023).
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:KAJ8541604.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JAJAGQ010000015; KAJ8541604.1; -; Genomic_DNA.
DR OrthoDB; 3247158at2759; -.
DR Proteomes; UP001152561; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR FunFam; 4.10.1000.10:FF:000008; zinc finger CCCH domain-containing protein 3; 1.
DR FunFam; 4.10.1000.10:FF:000022; Zinc finger CCCH domain-containing protein 7; 1.
DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 2.
DR InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR46156; CCCH ZINGC FINGER; 1.
DR PANTHER; PTHR46156:SF1; ZINC FINGER CCCH DOMAIN-CONTAINING PROTEIN 3; 1.
DR SMART; SM00356; ZnF_C3H1; 5.
DR PROSITE; PS50103; ZF_C3H1; 3.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP001152561};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 1623..1652
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 1678..1704
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 1705..1732
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 1623..1652
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 1678..1704
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 1705..1732
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1061..1080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1089..1121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1187..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1227..1257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1300..1332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1753..1777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1821..1887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..14
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..26
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..56
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..105
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1753..1763
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1764..1774
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1859..1871
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1872..1887
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1887 AA; 209140 MW; 66B2EADC538E2ECA CRC64;
MDLPPYHHHH HRYVQRPPNF SHNPNFFHHH HLPPPPPPPQ RPPPQPIPNL PPPPPLPHHH
ISHQFSFPSE NPRFYDFPQI NRSSPPRVST LDQPPYHPPR YHNPPPPPFP RFIVDDFNRS
STVNDNQEPV VWVRRENVEF NYDDNDERYR LERRRMDIDV NPSRDFRSSP GNYDDRYEVE
TWEHGGNVVN GNDRFSNRLR VDKEEIHRSL QKKQVQKKSA FLRIQCGKAN YRSRNQDNEL
GSGGVRRKQK DVFERLERRV EGREEKQMEL NVSFKSNALV AKAIMTPSSL AIDSDRSETP
PRSKKIRKVN SGSPMKRIGD DLGKGDGSAN DSGRRSSSNK ESKCLADKIT VSAGGSSSNS
TLESKKDSRH LADKITDSSG GGRASNGTLN PNKKSKILPF FIVRKKKEVT KKKITFPIKV
GVDPVNSIDS RKQDENFVEL VERITFDDMT TLEDVNVKLP SDEVVSKLDK PSELAAVSKN
ESVEQSNSDG KKASPAKVLV SSSVDSEIND IADYTSRSVQ SGPSMLNSET CMTEVQNKPT
SFDSDNTGNV GGHSEDELRV SEDGPIKESS EAMACVERNG DVVLSLLDER KIQKDEVSSS
TKDTYISAAS DLGFSDAKKN TDAAIGSFEA GSVETSSDPN IVPLLTNIEE GLRESFLDEN
DSSFNSDETG RIAVVNDLQT VECLSNSDSS STSGGSFESY VDIVSLSPEM RHTNGSDTTA
VSVGDDVRVI VDDDCLPKVT RKRKITDDES GLPTTKMSET EENEVSSLLG QGKRFSCLGE
DHASREEDVT VSGNGTDSLK EDRSHGGPSE VELSLQDCFK DGSNSCSTKS PKKREVSSPA
KVKSVPCFTT YEEPSSRPIT VPLINDVSAT ELESRNALSI VGDGPPACPS VIMLENSTAK
DVGQAEPFED DLMDHFSDVQ QVIAHNSQLG AVGQETTTSA VSVETLGMTD IVSEDEGSSL
GIDQNLAPEG RESDNYLLEK DDMPLLANNL SLFADKVSVI SIESVPVMSL LESFHEELPN
NSVSREPDYK SSLSSEIVIE KTQNVNENSV AAYDRVSSSV KTSSDTSEFG RSSDHKIGGN
PLVIVNTAPV SSQNTVKSTN NLSSQSWKPN LRANQQNPAG PKVFSVRTSG FITSRNVPIS
KKPLTWHRTG NSSPSVVGRG YQMNSLPPQS HLPKDIAKVS SYIRKGNSLV RNPSPVGSLS
KGYHAPSSSV YQLNSSGVND LKRISENRAE ITDSPSCRGT PEVNAPSERP KTPPQSEPFS
CITLKSSSLP VVDHPGNGSI ATNSDHLEVT DYILALKPSE HPSTSSALPE CQIGLGGNSE
SRNTLDEGSS RKNLVYVKQR SNQLVAASDK TQTSSDGYYK RRKNQLIRAS SNNHMKQRVA
AAKNIVPFQR GLAKTSKFSK FSLVWKLGDT QSSRKYGGTV EYEKLWPYLF PWKRASYRRS
FLSSSPSNSS SIIRRKLLLS KKRETIYTRS IHGLSLRRSK VLSVSGSSLK WSKSIEQRSK
KDAEEAALAI ASVDKRKRGQ DGSNSDSMNG NNVSREKIFR IGCERYKMDR SGKTLQRISD
EEPSVSVPEA KKSYIPKILL IGNDEYVRVG NGNKLVRNPK RRVRILANEK VRWSLHTARI
RLARKKQYCQ FFTRFGKCNK DNGKCPYIHE PSKIAVCTKF LNGSCSDTNC KLTHEVIPER
MQDCSYFLQG ICSNENCPYR HVNVNPNASI CDGFLRGYCA DGNECQKKHS YVCLVFEATG
NCPQGSKCKL HHPKNKRKGV KRKASSEMKN DRGRYFGSPH IDISERITAG KQKPSVKGNN
DIFFQEGKFV DFISLDCSDE EEQTIDQRSE ETPLSESGPG EMQLDDLIKP MRLINRNRSV
SSSPHIDSPS DMTTSYVSEE SQTRYCK
//
