ID A0A2P5ARY3_PARAD Unreviewed; 442 AA.
AC A0A2P5ARY3;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Zinc finger, CCCH-type {ECO:0000313|EMBL:PON39295.1};
GN ORFNames=PanWU01x14_306200 {ECO:0000313|EMBL:PON39295.1};
OS Parasponia andersonii (Sponia andersonii).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Parasponia.
OX NCBI_TaxID=3476 {ECO:0000313|EMBL:PON39295.1, ECO:0000313|Proteomes:UP000237105};
RN [1] {ECO:0000313|Proteomes:UP000237105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. WU1-14 {ECO:0000313|Proteomes:UP000237105};
RA Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA Smit S., Geurts R.;
RT "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT legume Parasponia.";
RL Submitted (JUN-2016) 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:PON39295.1}.
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DR EMBL; JXTB01000470; PON39295.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5ARY3; -.
DR STRING; 3476.A0A2P5ARY3; -.
DR OrthoDB; 1206973at2759; -.
DR Proteomes; UP000237105; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.30.30.1190; -; 1.
DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 2.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR12506; PROTEIN PHOSPHATASE RELATED; 1.
DR PANTHER; PTHR12506:SF50; ZINC FINGER CCCH DOMAIN-CONTAINING PROTEIN 26; 1.
DR Pfam; PF00642; zf-CCCH; 5.
DR SMART; SM00356; ZnF_C3H1; 5.
DR SUPFAM; SSF90229; CCCH zinc finger; 5.
DR PROSITE; PS50103; ZF_C3H1; 5.
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:UP000237105};
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 47..75
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 89..117
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 134..162
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 283..311
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 328..356
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 47..75
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 89..117
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 134..162
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 283..311
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 328..356
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 442 AA; 47690 MW; 3DCAC0EE61876D1A CRC64;
MPDTRQPVKN AGPNQSDGNI EEAIWRLKIN DNQEGGGVAQ TNPFPDRPGE PDCIFYLRTG
LCGYGTNCRF NHPAYAPQVA QYNGELPERV GQPDCGYFLK TGTCKYGSTC KFHHPRDRRG
AGPVSFNVLG LPMRQEEKSC PYYVRTGACK FGPACKFHHP QPASFGTGFL GGPPPAFGSA
GSAVLPSSNL PYAGGLQAWS LPRVPYPLSG PQPQPQPYMP VIVSPSQGII PAGVWNTYVG
NISPVSPAGI LGSSLVYNPR NPGESCSAGQ VNLSNSTPNL PDRPDQPECR YFMNTGTCKY
GTECKYHHPK ERMAQAAPIA NQIGLPSRPG LAVCSYYSMY GLCKYGPTCK FDHPPMQNLY
NYGLSLPAML DSPYLYYTKG SSTPHVPETS HSLASKSFDV VPKPLSNKNH NSDSRLSDDS
VKQASSLAHS SPSSEASEDQ SG
//
