位置:首页 > 蛋白库 > SDN1_ARATH
SDN1_ARATH
ID   SDN1_ARATH              Reviewed;         409 AA.
AC   A3KPE8; Q9SN08;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Small RNA degrading nuclease 1;
DE            EC=3.1.-.-;
GN   Name=SDN1; OrderedLocusNames=At3g50100; ORFNames=F3A4.180;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=18787168; DOI=10.1126/science.1163728;
RA   Ramachandran V., Chen X.;
RT   "Degradation of microRNAs by a family of exoribonucleases in Arabidopsis.";
RL   Science 321:1490-1492(2008).
CC   -!- FUNCTION: 3'-5' exonuclease degrading single-stranded small RNAs.
CC       {ECO:0000269|PubMed:18787168}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype; due to the redundancy with
CC       other SDN ribonucleases. Simultaneous knockdown of SDN1, SDN2 and SDN3
CC       results in elevated miRNA levels and pleiotropic developmental defects.
CC       {ECO:0000269|PubMed:18787168}.
CC   -!- MISCELLANEOUS: Presence of 2'-O-methyl or 3'poly-U in the small RNA
CC       deters the activity of SDN1.
CC   -!- SIMILARITY: Belongs to the REXO1/REXO3 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB62118.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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   EMBL; AL132978; CAB62118.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE78626.1; -; Genomic_DNA.
DR   EMBL; BT030315; ABO09879.1; -; mRNA.
DR   PIR; T45863; T45863.
DR   RefSeq; NP_190579.2; NM_114870.4.
DR   PDB; 5Z9X; X-ray; 2.80 A; A=1-409.
DR   PDB; 5Z9Z; X-ray; 2.05 A; A=309-409.
DR   PDBsum; 5Z9X; -.
DR   PDBsum; 5Z9Z; -.
DR   AlphaFoldDB; A3KPE8; -.
DR   SMR; A3KPE8; -.
DR   STRING; 3702.AT3G50100.1; -.
DR   iPTMnet; A3KPE8; -.
DR   PaxDb; A3KPE8; -.
DR   PRIDE; A3KPE8; -.
DR   ProteomicsDB; 232666; -.
DR   EnsemblPlants; AT3G50100.1; AT3G50100.1; AT3G50100.
DR   GeneID; 824172; -.
DR   Gramene; AT3G50100.1; AT3G50100.1; AT3G50100.
DR   KEGG; ath:AT3G50100; -.
DR   Araport; AT3G50100; -.
DR   TAIR; locus:2083163; AT3G50100.
DR   eggNOG; KOG2248; Eukaryota.
DR   HOGENOM; CLU_030142_0_0_1; -.
DR   InParanoid; A3KPE8; -.
DR   OMA; CAFVIFR; -.
DR   OrthoDB; 774159at2759; -.
DR   PhylomeDB; A3KPE8; -.
DR   PRO; PR:A3KPE8; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; A3KPE8; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IDA:TAIR.
DR   GO; GO:0000175; F:3'-5'-exoribonuclease activity; IDA:CACAO.
DR   GO; GO:0044748; F:3'-5'-exoribonuclease activity involved in mature miRNA 3'-end processing; IDA:TAIR.
DR   GO; GO:0004527; F:exonuclease activity; IBA:GO_Central.
DR   GO; GO:0035198; F:miRNA binding; IPI:TAIR.
DR   GO; GO:0010587; P:miRNA catabolic process; IDA:TAIR.
DR   CDD; cd06145; REX1_like; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR034922; REX1-like_exo.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   Pfam; PF00929; RNase_T; 1.
DR   SMART; SM00479; EXOIII; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Exonuclease; Hydrolase; Nuclease; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..409
FT                   /note="Small RNA degrading nuclease 1"
FT                   /id="PRO_0000355084"
FT   DOMAIN          140..291
FT                   /note="Exonuclease"
FT   HELIX           10..23
FT                   /evidence="ECO:0007829|PDB:5Z9X"
FT   HELIX           32..38
FT                   /evidence="ECO:0007829|PDB:5Z9X"
FT   HELIX           54..61
FT                   /evidence="ECO:0007829|PDB:5Z9X"
FT   HELIX           67..86
FT                   /evidence="ECO:0007829|PDB:5Z9X"
FT   HELIX           90..92
FT                   /evidence="ECO:0007829|PDB:5Z9X"
FT   HELIX           95..105
FT                   /evidence="ECO:0007829|PDB:5Z9X"
FT   HELIX           109..112
FT                   /evidence="ECO:0007829|PDB:5Z9X"
FT   HELIX           127..129
FT                   /evidence="ECO:0007829|PDB:5Z9X"
FT   HELIX           132..135
FT                   /evidence="ECO:0007829|PDB:5Z9X"
FT   STRAND          140..150
FT                   /evidence="ECO:0007829|PDB:5Z9X"
FT   STRAND          155..164
FT                   /evidence="ECO:0007829|PDB:5Z9X"
FT   STRAND          169..175
FT                   /evidence="ECO:0007829|PDB:5Z9X"
FT   HELIX           192..197
FT                   /evidence="ECO:0007829|PDB:5Z9X"
FT   HELIX           203..215
FT                   /evidence="ECO:0007829|PDB:5Z9X"
FT   STRAND          219..224
FT                   /evidence="ECO:0007829|PDB:5Z9X"
FT   HELIX           225..232
FT                   /evidence="ECO:0007829|PDB:5Z9X"
FT   STRAND          239..241
FT                   /evidence="ECO:0007829|PDB:5Z9X"
FT   HELIX           242..245
FT                   /evidence="ECO:0007829|PDB:5Z9X"
FT   HELIX           259..266
FT                   /evidence="ECO:0007829|PDB:5Z9X"
FT   HELIX           280..296
FT                   /evidence="ECO:0007829|PDB:5Z9X"
FT   HELIX           309..313
FT                   /evidence="ECO:0007829|PDB:5Z9Z"
FT   STRAND          316..323
FT                   /evidence="ECO:0007829|PDB:5Z9Z"
FT   HELIX           328..334
FT                   /evidence="ECO:0007829|PDB:5Z9Z"
FT   STRAND          337..343
FT                   /evidence="ECO:0007829|PDB:5Z9Z"
FT   STRAND          351..361
FT                   /evidence="ECO:0007829|PDB:5Z9Z"
FT   HELIX           362..371
FT                   /evidence="ECO:0007829|PDB:5Z9Z"
FT   STRAND          374..378
FT                   /evidence="ECO:0007829|PDB:5Z9Z"
FT   STRAND          384..391
FT                   /evidence="ECO:0007829|PDB:5Z9Z"
FT   STRAND          397..405
FT                   /evidence="ECO:0007829|PDB:5Z9Z"
SQ   SEQUENCE   409 AA;  46364 MW;  E7750B8B1411415D CRC64;
     MELKLATAEK QVLDELVKLL QSRDLRGENG NWKEFLHVYD KNADSPSDPS RRSHEDLVQF
     LTTFKKKEDL QLLKCHANHL LIENLKQESQ DEDTPEQMLV RLTVEHPSYS LDYSFKPYSE
     DWFVSDVGMK MKKVMESTNM VAVDCEMVLC EDGTEGLVRV GVVDRDLKVI LDEFVKPNKP
     VVDYRTDITG ITAEDIENAS LSVVDIQETL QPFLSTGTIL VGHSLNRDLE VLKIDHPKVI
     DTALVFKYPN TRKLRRPSLN NLCKSILGYE VRKTGVPHDC VHDASAAMKL ALAVVEKRVD
     TTIKPSKEML EVEKAKLFLH KIPNNVPSEE LEQVLSGKFT LDVKQAKTQG RYYCAFALFH
     SSEDADQAFE HIDGIEMTDS LGLPQKVVII KLSSGSRASI YVRKMVQDE
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024