ID A0A0R0JZ47_SOYBN Unreviewed; 871 AA.
AC A0A0R0JZ47;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=CCHC-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=GLYMA_05G072900 {ECO:0000313|EMBL:KRH57619.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH57619.1};
RN [1] {ECO:0000313|EMBL:KRH57619.1, ECO:0000313|EnsemblPlants:KRH57619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH57619};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH57619.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH57619}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH57619};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH57619.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH57619.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CM000838; KRH57619.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R0JZ47; -.
DR PaxDb; 3847-GLYMA06G31572-1; -.
DR EnsemblPlants; KRH57619; KRH57619; GLYMA_05G072900.
DR Gramene; KRH57619; KRH57619; GLYMA_05G072900.
DR InParanoid; A0A0R0JZ47; -.
DR OMA; PSNTHYQ; -.
DR Proteomes; UP000008827; Chromosome 5.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00303; retropepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 1.
DR Gene3D; 3.10.10.10; HIV Type 1 Reverse Transcriptase, subunit A, domain 1; 1.
DR Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR InterPro; IPR001995; Peptidase_A2_cat.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR018061; Retropepsins.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR46249; CCHC-TYPE DOMAIN-CONTAINING PROTEIN-RELATED; 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; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Reference proteome {ECO:0000313|Proteomes:UP000008827};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 417..431
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 643..742
FT /note="Peptidase A2"
FT /evidence="ECO:0000259|PROSITE:PS50175"
FT REGION 368..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 871 AA; 100623 MW; EBB023E2B1567CC1 CRC64;
MAIPFKTKDV NEEITSKDIK SLMEQANYTN KYLQALGETI KTKVVPKQKP IEETSPKIPI
EKPLFKPFKV SEKAKRKIRE LRKTKSLIEG VGDNHSELLN KIGSLLKVIP DTPQASENTS
KMVTRSISKL INVINEDSDQ NSDNTTEIGS VSEKNINPIN SKHWKTPSKL YYQRPTAPDL
LLEERGENNF KSFSANNIYE WNIDAQTEYN IMNTLQHMTM VATAYQTSHE SQHFIGDPSL
WKDRSAELLS NLKCRTLADF RWYRDTFLTR VYTREDSQRP FWKEKFLAGL PRSLGDKVRD
KIRSQSANGD IPYESLSYGQ LISYVQKVAL KICQDDKIQR QLAKEKAQTK RDLGSFCEQF
GLPACPKQKK KQSSKKEIHE NKPINTKRFP RRRYSHKPST SRGMENPKQK TKSKITCYNC
GKQGHISKYC RLKRKLRNLN LEPAIEEQIN NLLIETSEEE TETSSSVLSD ENLNLIQQDD
QLSSTDDDDG QINTLTREQD LLFEAINSIP DPQEKKVFLE KLKKTLEVKP RQKDFITNNK
FDVSNILKRL ENSSTKPTTI QDLQTEINNL KREVKELRQQ QEIHQIILSQ LEEDSDSEST
NNSEENQPEN LEDDMFMGLI NKIKIQKFYI NIKIIINDFV LETMALFDTG ADSNCILEGL
IPTKFFEKTS EKLSTANGSK LKINFKLSNA IIENQGLKIN TNFLLVKNLK NEVILGTPFI
RALFPIQISN EGITTNYLGR KIIFNFSTKP ISRNINLIEN KINQINFLKE EVSFNNIQIQ
LGKPQVKERI QSLLNHIEST VCSELPHAFW DRKKHIVDLP YEKDFREKQI PTKARPIQMN
EELLQYCQKE IKDLLDKGLI RKSKSPCITM D
//
