ID A0A0D9WSF1_9ORYZ Unreviewed; 2063 AA.
AC A0A0D9WSF1;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 28-JAN-2026, entry version 37.
DE RecName: Full=C3H1-type domain-containing protein {ECO:0000259|PROSITE:PS50103};
OS Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR06G18390.1, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR06G18390.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR06G18390.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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 STRING; 77586.A0A0D9WSF1; -.
DR EnsemblPlants; LPERR06G18390.1; LPERR06G18390.1; LPERR06G18390.
DR Gramene; LPERR06G18390.1; LPERR06G18390.1; LPERR06G18390.
DR eggNOG; KOG1492; Eukaryota.
DR HOGENOM; CLU_003156_0_0_1; -.
DR Proteomes; UP000032180; Chromosome 6.
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:UP000032180};
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 1823..1852
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 1878..1904
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 1905..1932
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 1823..1852
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 1878..1904
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 1905..1932
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 1..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1126..1157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1357..1420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1438..1511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1737..1781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..49
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..77
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..103
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..170
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..575
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..768
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..783
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..853
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1397..1409
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1455..1471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1477..1492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1747..1758
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1759..1775
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2063 AA; 226808 MW; AB59C12A0D4D14B4 CRC64;
MDPPPPFDHT HHRRGGYHHP YDHHFPGGSG SGGGAAAASR SRYEYGAAYD PHPHQYHHLS
DHHSHHPPRV HHHHHHYQPP SAPSPPPPPP PLPPPPPPPP PLPQHRHEPP PHYGFPPRGL
PDAYSPPAYR EPSPHHHYLG HPRHGGEDFL PADEIRRVVG GHHQHHHHHP QLQQRLPWEE
AEEERRRYGA AQPLWLSPPA GPRKRQRCAV HDSDLESSSS SGAPPRRQRQ QSHPDDSFVD
RNAAHPGYMG HEGFSIHSDN KVSRKIQMPA QMTLPGSPRG TGTGYTRRAP QKVAPMRVSV
WHRIEENPAM YEPSSPKHVP KEVHISPCKS NNVAPTSKEL ASVVSVDCRG KSADGDDGDS
NAGKKKTPVK KNEKVLASVL VKPSVEPKEK EVAGKKMLKK LDKIQKNAAD SNIRGLVRTP
CPGAGAKKVK KIVIKKIVRK INGKGNLISS PVISEKKDKI DANACEKEEG EITTSFEKDA
ISAHDPIAVS DTAGFVNDVN AQKEESNIFT DPSGRHAASA IESTATCGSG SAHPGNEDSR
IPMNPDDGIN GAVVVEPTEV LDKSGTEHPR KEHDMGSIGK GVSDAFADKT NYTQEEVKTP
QDEMNVAVAS KSVRVSDAWK LPVCDDSSME ESKVPKDVGG TNAVCVDGVD SDRGTTELNE
IEGARRECGI LIGRNEENTS LGNSCAGSPN SADICMTAEQ ATWKKEDIIL TGLSEKSIGL
LGDSVGTHRT TELGVSKNAP NEGDNMLSHP SEKDFLSLNS RGSLNNTEVS EKEDLQEKED
RTPMEAVIAC TSSGNEDMQL NEGRKPMELS GTNAFSGSEN ICGNIIPMGS SEINTSLGNH
VNTSNTKDAS VNEDTQKKES HMPIESCKSN TLEIMHYKEA PSTEEVIMGM SFRTLAEVSS
NERCSGATGN SANALGFHLA CAAKDNQMKD LLNNRTVLNE INTPLDAEDS SAFDLPSSRN
VESTYALSLY DPMEDSTSDC ILNIGLGMNV TSKAVELMDV HRVHMRSEDD SFIHSRDSLS
VSGNCEQSVP TALTLGSNIY FSRVETDDQP EESHELVEGQ RGLNVATARI LDSPGKKEVL
TGEGLISKGI QNWLSLPPSV NDMEMSGQVL NYDFIVSKGR LGLDQSMDDT TSMSQDHDTT
QDMDQCGSED ASFSQDHGIS LSGSDLLAPK ESNMDVEDQS EIALTGLHPT SSVNVLVHYG
YQTVDIPIDN LNKPISSALE SSGVMDTDQV SSQVCVDPDH ANDSNVENPG VKSNAKQDLL
SSWIEAIVSE AKKEHRPCNS TPLSVGLPDK LLEPKDGNRK TVLETVVPSA VKSQISFTSS
TLPKVAPKQV TLPSSSRELT RANQIVRHRT WHRGNIASST SSFHASQPLG LPPKLPPKKS
DKAQNSYIRK GNALIRNPSN GNHPHSSSSQ DTQNKLNKPV VRRSMNFVRK ADTKDLVANV
PVERPKTPPL PLHTKSISCP TSLLEPLSQN SQKHHGHETE KEDPTGHQKL DVDNPGIKST
QKSEPSDGSK VVYVRPKSNQ LVAAQRQHPV DLVNSSMDKV LALQAPIASD LYLKKRKNQI
VLSSCSPSDS QNTKEMLPAE NTNSNEKKDL MITCSINGIP GGKDRPQKAA LQTTNSVGHF
SHVWTLNGQQ PQRKGFIGNS HMNTFPRILP WKRKIFCKNF RSSHTTLSNV SSIRIVRKLL
QTRKRDMIYT VSTDGFSLRK SGVLSVGGSS LKWSRSLEKC SQKVNKEAIS ALAEVERKKR
EKRKRQSLHD KGRNDHQYTE TVSGNQLRNN HQASSDLKKP STCNEYVRVS KGNQLVRNPK
NVIRMLASDK VRWSLHTVRS RQAKKQQYCQ FFTRFGECKK PRGKCPYIHD QAKVTICTKF
LKGLCSNTSC KLTHKVLPER MPDCSYFLRG LCTNIACPYR HVKVNFNAPV CEDFLKGYCA
DGDECHKKHS FVCPIFEATG ECPQRSRCKL HHPKNKVKSK KSRPDFLQNS SWGRYFDTSI
GHESETRKVS LDENESEKPQ RVFSDEDLID FIGLADDADE DVAASDTSDD IPLMELDSGG
LSEQTDNLDA LIKPLRIMRT ARV
//
