ID A0A2C9W574_MANES Unreviewed; 661 AA.
AC A0A2C9W574;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 22-FEB-2023, entry version 16.
DE RecName: Full=CCHC-type domain-containing protein {ECO:0000259|PROSITE:PS50158};
DE Flags: Fragment;
GN ORFNames=MANES_03G066000 {ECO:0000313|EMBL:OAY54325.1};
OS Manihot esculenta (Cassava) (Jatropha manihot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC Manihot.
OX NCBI_TaxID=3983 {ECO:0000313|EMBL:OAY54325.1, ECO:0000313|Proteomes:UP000091857};
RN [1] {ECO:0000313|EMBL:OAY54325.1, ECO:0000313|Proteomes:UP000091857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AM560-2 {ECO:0000313|Proteomes:UP000091857};
RC TISSUE=Leaf {ECO:0000313|EMBL:OAY54325.1};
RA Bredeson J.V., Prochnik S.E., Lyons J.B., Schmutz J., Grimwood J.,
RA Vrebalov J., Bart R.S., Amuge T., Ferguson M.E., Green R., Putnam N.,
RA Stites J., Rounsley S., Rokhsar D.S.;
RT "WGS assembly of Manihot esculenta.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CM004389; OAY54325.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C9W574; -.
DR EnsemblPlants; OAY54325; OAY54325; MANES_03G066000.
DR Gramene; OAY54325; OAY54325; MANES_03G066000.
DR Proteomes; UP000091857; Chromosome lg3.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd00303; retropepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 1.
DR Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR018061; Retropepsins.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR33054; CCHC-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR33054:SF9; CCHC-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00077; RVP; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Reference proteome {ECO:0000313|Proteomes:UP000091857};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 190..204
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 132..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 357..391
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 132..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 661
FT /evidence="ECO:0000313|EMBL:OAY54325.1"
SQ SEQUENCE 661 AA; 76900 MW; 6C489BDDBA4C3B32 CRC64;
MFTDRAQEQL INLRCPDLSH FKWYRDTFFS LVFTREDSQN HVWKEKFLAG LPALFAERVR
DQIRSKHNGN IPYHDYTYGE LASKVVTTGI HLCNELKIHK QMQKERFYGK QILGNFCEQY
GLPPIKFPST KFKGGRREAE NVRQHRRKHF FANKRPYKEQ HRRFSKPESS RKSKERKKPN
PGKAEKTIVC YKCGKVGHYA NKCRVKQQIQ ALTIEEDLKE ALAKILLNET DSEQETLEIN
AVDYTTEEEE SSTEEEEDQK EDCEGNCDYY KSLCAMNGLL VLTKEDNLIL DLIDNIEDPE
KKREKLETYI GLYKDKETNT TAQDLTDKKI ESRQPSYDLK DILERVKNSK RQKEPTVAEL
RSELNSVKTE IKEMKERINI LELLNEQQQQ LAMEEPEEDQ GGKDLNNLHY INMADRVITH
KWHTRVTIVV HKNYVFETNA LIDSGADLNC INEGLVPSKY FSKTLEELHT ADGSKMSVKY
KLNNTVICNQ GTCFEIPFLM VKGLSHPVIL GNPFLHMLYP IQITKEGIST EINGKVITFY
FSSQPRLKEI DVLKNTVENK TKFVNSLKQE VIYKGIDDRL KEPKIQQRIK IIQEELLSSI
CAESPDAFWT RKRHVVTLPY DPEFSEKAIP TKARPIAMGP RHLELCKKEI AELEAKGLIR
K
//