ID D7L3Z4_ARALL Unreviewed; 1134 AA.
AC D7L3Z4;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE RecName: Full=Exonuclease domain-containing protein {ECO:0000259|SMART:SM00479};
GN ORFNames=ARALYDRAFT_318289 {ECO:0000313|EMBL:EFH61331.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
CC -!- SIMILARITY: Belongs to the PPR family. PCMP-H subfamily.
CC {ECO:0000256|ARBA:ARBA00006643}.
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DR EMBL; GL348715; EFH61331.1; -; Genomic_DNA.
DR RefSeq; XP_002885072.1; XM_002885026.1.
DR AlphaFoldDB; D7L3Z4; -.
DR STRING; 81972.D7L3Z4; -.
DR EnsemblPlants; fgenesh1_pm.C_scaffold_3001305; fgenesh1_pm.C_scaffold_3001305; fgenesh1_pm.C_scaffold_3001305.
DR Gramene; fgenesh1_pm.C_scaffold_3001305; fgenesh1_pm.C_scaffold_3001305; fgenesh1_pm.C_scaffold_3001305.
DR eggNOG; KOG0542; Eukaryota.
DR eggNOG; KOG4197; Eukaryota.
DR HOGENOM; CLU_278666_0_0_1; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009451; P:RNA modification; IEA:InterPro.
DR CDD; cd06133; ERI-1_3'hExo_like; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 4.
DR InterPro; IPR032867; DYW_dom.
DR InterPro; IPR046848; E_motif.
DR InterPro; IPR047201; ERI-1_3'hExo-like.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR006527; F-box-assoc_dom_typ1.
DR InterPro; IPR002885; Pentatricopeptide_rpt.
DR InterPro; IPR046960; PPR_At4g14850-like_plant.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR NCBIfam; TIGR00756; PPR; 5.
DR PANTHER; PTHR47926; PENTATRICOPEPTIDE REPEAT-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR47926:SF339; UMP-CMP KINASE; 1.
DR Pfam; PF14432; DYW_deaminase; 1.
DR Pfam; PF20431; E_motif; 1.
DR Pfam; PF07734; FBA_1; 1.
DR Pfam; PF01535; PPR; 4.
DR Pfam; PF13041; PPR_2; 2.
DR Pfam; PF00929; RNase_T; 1.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS51375; PPR; 5.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 125..310
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
FT REPEAT 434..468
FT /note="PPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00708"
FT REPEAT 535..569
FT /note="PPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00708"
FT REPEAT 640..674
FT /note="PPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00708"
FT REPEAT 741..775
FT /note="PPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00708"
FT REPEAT 776..811
FT /note="PPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00708"
FT REGION 43..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1134 AA; 127138 MW; 134DFDDCBD68B2A0 CRC64;
MASAFSAFRV SLSRISPFRD TRFSYPATFA LAHTKRIMCS STHSVSSSPS PSDISSSSSS
SPSTFSLMGA SENARWRPMC LYYTHGKCTK MDDPAHLEIF NHDCSKELPV AATDLGRKKS
QEFNFFLVID LEGKVEILEF PVLIVDAKTM EVVDLFHRFV RPTKMSEQAI NKYIEGKYGE
VGVDRVWHDT AIPFKQVVEE FEAWLAEHDL WTKDTDGALN DAAFITCGNW DIKTKIPEQC
VVSNINLPPY FTEWINLKDI YLNFYGREAR GMVSMMRQCG IKLMGSHHLG IDDTKNITRV
VQRMLSEGAV LKITARRSKS NTRNVEFLFK NRIKPMNWPN LGCNRLCAGS SESQTATLCL
CSFCQHLLHS PTEEDSHVLE NCYVLEFIIF TNSNFRLSGS GLNLITSNYL IDMYCKCREQ
LIAYKVFDSM PERNVVSWTA LMSGHVLNGD LNGSLSLFTE MGRQGIYPNE FTFSTNLKAC
GLLNALEKGL QIHGFCLKIG FEMMVEVGNS LVDMYSKCGR INEAEKVFRW MVGRSLISWN
AMIAGYVHAG YGSRALATFG MMQEAKIKER PDEFTLTSLL KACSSTGMIY AGKQIHGFLV
RSGFHCPSSA TITGSLVDLY VKCGNLFSAR KAFDQIKEKT MISWSSLILG YAQEGDFVEA
MGLFKRLQEL SSQIDSFVLS SIIGVFADFA LLQQGKQMQA LVVKLPSGLE TSVSNSLVDM
YLKCGLVDEA EKCFAEMQLK DVISWTVMIT GYGKHGLGKK AVSIFNKMLR HNIEPDEVCY
LAVLSACSHS GMIKEGEELF SKLLETQGIK PRVEHYACVV DLLGRAGRLK EAKHLVDTMP
IKPNVGIWQT LLSLCRVHGD IELGKEVGKI LLRIDGKNPA NYVMMSNLYG QAGYWNEQGN
ARELGSIKGL QKEAGMSWVE IEREVHFFRS GEDSHPLTLV IQETLKEVER RLREELGYVY
GLKHELHDID DESKEENLRA HSEKLAIGLA LATGGLNQKG KTIRVFKNLR VCVDCHEFIK
GLSKITKIAY VVRDAVRFHS FEDGCCSCGD YCFFIDEQEK VAVVFDVDGY RDTETARYHT
AFIIGDDGYF KSVSLGEAPN VYDGKPGHLG YTPQFYCPPL VCSSSYLPSF VSHS
//