ID A0A444Z408_ARAHY Unreviewed; 1175 AA.
AC A0A444Z408;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 11.
DE RecName: Full=CCHC-type domain-containing protein {ECO:0000259|PROSITE:PS50158};
GN ORFNames=Ahy_B05g076767 {ECO:0000313|EMBL:RYR08900.1};
OS Arachis hypogaea (Peanut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX NCBI_TaxID=3818 {ECO:0000313|EMBL:RYR08900.1, ECO:0000313|Proteomes:UP000289738};
RN [1] {ECO:0000313|EMBL:RYR08900.1, ECO:0000313|Proteomes:UP000289738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC TISSUE=Leaves {ECO:0000313|EMBL:RYR08900.1};
RA Chen X.;
RT "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT genome evolution and oil improvement.";
RL Submitted (JAN-2019) 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:RYR08900.1}.
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DR EMBL; SDMP01000015; RYR08900.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A444Z408; -.
DR STRING; 3818.A0A444Z408; -.
DR Proteomes; UP000289738; Chromosome b05.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd06222; RNase_H_like; 1.
DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR025558; DUF4283.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR044730; RNase_H-like_dom_plant.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR002156; RNaseH_domain.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR026960; RVT-Znf.
DR InterPro; IPR025836; Zn_knuckle_CX2CX4HX4C.
DR InterPro; IPR001878; Znf_CCHC.
DR PANTHER; PTHR33710; BNAC02G09200D PROTEIN; 1.
DR PANTHER; PTHR33710:SF78; DUF4283 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF14111; DUF4283; 1.
DR Pfam; PF13456; RVT_3; 1.
DR Pfam; PF14392; zf-CCHC_4; 1.
DR Pfam; PF13966; zf-RVT; 1.
DR SUPFAM; SSF56219; DNase I-like; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Reference proteome {ECO:0000313|Proteomes:UP000289738};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 149..164
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 179..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1131..1175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1131..1157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1175 AA; 136207 MW; DDD0F44AA335ACE0 CRC64;
MWKNPQGVAV TDIGWKKMLF SFKDSKKGLH IIQNGPWNVK RNMVNLRLWR EGKSVFEIDH
DFMEFWIQVH GIPHDLMDKE TCILIGEMLG VLAEVEDPKV DGILRRPYLR IRVSINITKP
LPTGFWLDRE EMPPLWVFFK YERLPDSYCF NCGILGHEKK TCKNPTVMAC WDPTKNKYSP
GLGVSQRRPG PTMRGGFSKQ QGWREEGEEQ AREQLDPDRE SGDKQSSEES RIRAEQVLQQ
KISEKSVWKN QMMRDEEMAD IEEHVEEVPK IPDFQEERDT QRDLGAAYKL SNNKKAQKRE
KRYEVQKSSG NGPIRDIGPN TGALHLQSWN VEGSGLNHYI TEEREVNNYK MEDWKLGPEK
EKEKETIGQE LKRLMLARTR DKQVCKARTE GKEHQELLKS GTEENELKKL SKKAQNREHE
SLGQHAKPGE NIYYVDLASD EDEDKEIEAE ADWKMRLAKK LELNLNLKKK RENKQNSGAC
PVDYVCYGNL ILISMVFLCM VTQFFQSEGN YGRSLRSKEE PQAYLGDFND ILIQDEKVGI
HPQPRNYLYT FRRFVDNNGL MDVDFKGSKY TWFSNPRNNF ITRKILDRVF VNWKWLHIYQ
NVILKAAPAM SSDHCALILE TQLQVRIKKE FRFEAFWTEH EECKEVIRRT ELITRTPISL
INKKDHFVWP YRNDGQYSVR IGYHVAKEEK DTKEETKLSK ASTSQNLREV WETIWRVSVP
GKVRMFLWKA VHRILPVNTN LYQRKSAITP RCSICQEEDE TIEHALLLCP WTRAVWFGSS
LQIVPTAYNV RSFEKWMMNT IEKIKNETGK EHDKFLCNLG CVCWCIWKAR NEHIFQQTKV
NPEKVIIYSE HLATEYHNAT KGLNIDNKPK VGKNGESKRI TWRPPPHNKV KVNTDAVFHR
ETGMAALAAV VRDWQGKIIT ETTSTFRTTS ALAVKAQAYR ETFILIKNLQ IANCIIETDC
LPLVQAIKAR TPLAESDAII RDILQLLDEA PDVGATWTPQ EGNKFAHQLA AMVVWNQLQR
QWTINPPVQV RNTIKTEAGF VILQHNQHNQ NQANKVSVST SLQGYQREEG LPGRVETETC
DRHDAEGEER FRPTTLQRPI NDTSNDAINI GRRDSRGDAE GLIAWREVTR QRSSSGHRMT
VTPGTSGRTQ AHHQELQRGT SLVRCGRGRN QVEKL
//
