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Database: UniProt
Entry: A0A834TXK0_9FABA
LinkDB: A0A834TXK0_9FABA
Original site: A0A834TXK0_9FABA 
ID   A0A834TXK0_9FABA        Unreviewed;      1751 AA.
AC   A0A834TXK0;
DT   29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 1.
DT   28-JAN-2026, entry version 12.
DE   SubName: Full=Zinc finger CCCH domain-containing protein 7 {ECO:0000313|EMBL:KAF7829794.1};
GN   ORFNames=G2W53_012127 {ECO:0000313|EMBL:KAF7829794.1};
OS   Senna tora.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Caesalpinioideae; Cassia clade; Senna.
OX   NCBI_TaxID=362788 {ECO:0000313|EMBL:KAF7829794.1, ECO:0000313|Proteomes:UP000634136};
RN   [1] {ECO:0000313|EMBL:KAF7829794.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF7829794.1};
RA   Kang S.-H., Pandey R.P., Lee C.-M., Sim J.-S., Jeong J.-T., Choi B.-S.,
RA   Jung M., Ginzburg D., Zhao K., Won S.Y., Oh T.-J., Yu Y., Kim N.-H.,
RA   Lee O.R., Lee T.-H., Bashyal P., Kim T.-S., Lee W.-H., Kawkins C.,
RA   Kim C.-K., Kim J.S., Ahn B.O., Rhee S.Y., Sohng J.K.;
RT   "Genome-Enabled Discovery of Anthraquinone Biosynthesis in Senna tora.";
RL   Submitted (SEP-2020) 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:KAF7829794.1}.
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DR   EMBL; JAAIUW010000005; KAF7829794.1; -; Genomic_DNA.
DR   OrthoDB; 3247158at2759; -.
DR   Proteomes; UP000634136; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-ARBA.
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:UP000634136};
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          1508..1537
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          1563..1589
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          1590..1617
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   ZN_FING         1508..1537
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         1563..1589
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         1590..1617
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          262..282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          977..1031
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1080..1115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1638..1664
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1703..1728
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        266..275
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1017..1031
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1080..1089
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1103..1115
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1638..1649
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1709..1719
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1751 AA;  191391 MW;  BBEF3CBD81B67EFE CRC64;
     MVKPNHRNRE TEQLHYTSYA DDSGSNSFRG KDQFEYSGYG MKTEEREGSP VELDISFKSN
     SLVAKAIVAP SSSAIVSDAD VTSVSDTDLT SAEKKKNGLV SDYDFSDLKP AKPSTVTANL
     SSSPCKSNGV PCSGKDLQEN VSDSQPYPSA IHNFHCKNEG AQTPKGIVPG DITKSCSGKT
     SPRVTKKKKI VKKVVKKVVS NPNLHVSSAI SSSMLDKTVQ ADSVTFSPSF TSGSDKSETF
     LKEKITAVGK FSMPGCLQSS PSKVHLLPDN RKEDTPPLSM GTDTMLQVYK TDDNSEIGEV
     ARVEKSENIS SSPLGAGSIK DEKSDSDCLD ADNFVHGLHS MKNTDKVANE VSLSPGQYSD
     VQCLENRYRV EDDTNCRLSS SAESVINTDV INTSDSANVR VSGLSFTGNS QEKVAVCDIR
     NDGKADCERK AIALTDNAIL GENQETSIPV PICGMVDHFS SGETTIQDGQ DCLKHSRVPM
     HGYGNWPTNS EDNITVPHGV IVRDSGKQAS SLDFTMSPGN CATEQFPNAK FSERFGEEDT
     RNSKKRKVGT HLEFSSSNIG GIFPDPIQTV SIANVDTTFS PLKDPSPSEV SDAVVQSSEF
     SLHANKSGFT VLDEQGKITE AGVYFGNNGD NSADRASPMP KRNEVTTSHP NFSLCQAELC
     DAIVVATSCA EVPISISDNQ TRQKEVAFSS ITKCPTSPTL PYPEDSAKLY GNSLVGASIE
     SMDTNRGTMT SECSETQHPG LEFNSLHEEL ASPNNQFPEL EGEQNENGTA VVPINNTQED
     IRVVGNTERE KIDIQAVEKC ESIDIEQRSP SVVKSSDLQR KDDLPLEQDC LSCPADTDGV
     TISYSNALSD MFSPGTTSDI PDRRISDCPA IHNESIPVDE ENVVSSFMVE HGSDLTDSTL
     PSEHTIENRK LDHATKCNNL IMEKIMPQSL QVYSKVMTKG LNSSCSEGGK NQPGSAIPTT
     IQGRFVFPKS KTSALSTHGS KLRTWHRTGN NSASLPGSKP SAGFAPSKRP ISEKKGNFQN
     TSYIRKGNNS IVRKHTPVSA LPQGSVNRSS SLGFDDFHFR KSTGSESKVD ITDQTNLLKS
     GITHTSPEGQ RTPPPPTDTK LPNQTTTSSE ENRSSSLIEL LSNADCDSAS EPRKFMESYD
     ALNSAEDALK SYVPVETQMG PSNNGEILVD ANDVSVSSLN SKKIVYVKRK SNQLVASSNS
     CDLSVTADDT QAASSDGYYK RRKNQLVRTA FESHINQAVG MPIVAVNSEG KGTHKAVCNR
     RFSKKRSHKV VGTARKPLRA SLVWTLCGAN SSKNGSGAVH HQKVLPHLFP WKRATYLRNF
     IHNPALSSNA SSLSAISKKL VLLRKRDTVY TRSSHGFSLR KSKVLGVGGS SLKWSKSIEK
     CSKKANEEAT RAVAAVERKK REQKDVACIS SRAKRQRIFR IGSVRYRMDP SGRTLHRISD
     DESPSSASIP SGLHAKRSYI PRRLVIGNDE YVRIGNGHQL IRDPKKRTRI LANEKIRWSL
     HTARQRLARK QKYCQFFTRF GKCNKDDKKC PYIHDPSKVA VCTKFLNGLC SSPNCKLTHK
     VIPERMPDCS YFLQGLCTNR NCPYRHVNVN PKASVCEGFL RGYCADGNEC PKKHSYVCPS
     FEATGICTQG TKCKLHHPQK QSKGKKRKRY GDQKNSRGRY FGSVPIDVSE SGATVAPRQE
     EQNDDDLEGE LADYISLDID DEEVAESIGQ PSEQATFSDS EPLDTQMDDV DELIKPVLIM
     KMDSRVQESS V
//
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