ID A0A328DZ44_9ASTE Unreviewed; 1041 AA.
AC A0A328DZ44;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 03-MAY-2023, entry version 16.
DE RecName: Full=5'-3' exoribonuclease {ECO:0000256|PIRNR:PIRNR037239};
DE EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR037239};
GN ORFNames=DM860_016967 {ECO:0000313|EMBL:RAL50500.1};
OS Cuscuta australis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Convolvulaceae; Cuscuteae; Cuscuta;
OC Cuscuta subgen. Grammica; Cuscuta sect. Cleistogrammica.
OX NCBI_TaxID=267555 {ECO:0000313|EMBL:RAL50500.1, ECO:0000313|Proteomes:UP000249390};
RN [1] {ECO:0000313|EMBL:RAL50500.1, ECO:0000313|Proteomes:UP000249390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Yunnan {ECO:0000313|Proteomes:UP000249390};
RC TISSUE=Vines {ECO:0000313|EMBL:RAL50500.1};
RA Liu H.;
RT "The Genome of Cuscuta australis (Dodder) Provides Insight into the
RT Evolution of Plant Parasitism.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Possesses 5'->3' exoribonuclease activity. Acts as an
CC endogenous post-transcriptional gene silencing (PTGS) suppressor.
CC {ECO:0000256|PIRNR:PIRNR037239}.
CC -!- SIMILARITY: Belongs to the 5'-3' exonuclease family. XRN2/RAT1
CC subfamily. {ECO:0000256|ARBA:ARBA00006994,
CC ECO:0000256|PIRNR:PIRNR037239}.
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:RAL50500.1}.
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DR EMBL; NQVE01000060; RAL50500.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A328DZ44; -.
DR Proteomes; UP000249390; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0004534; F:5'-3' RNA exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-UniRule.
DR CDD; cd18673; PIN_XRN1-2-like; 1.
DR Gene3D; 1.25.40.1050; -; 1.
DR Gene3D; 3.40.50.12390; -; 2.
DR InterPro; IPR027073; 5_3_exoribonuclease.
DR InterPro; IPR041412; Xrn1_helical.
DR InterPro; IPR004859; Xrn1_N.
DR InterPro; IPR017151; Xrn2/3/4.
DR InterPro; IPR001878; Znf_CCHC.
DR PANTHER; PTHR12341:SF74; 5'-3' EXORIBONUCLEASE 4; 1.
DR PANTHER; PTHR12341; 5'->3' EXORIBONUCLEASE; 1.
DR Pfam; PF17846; XRN_M; 2.
DR Pfam; PF03159; XRN_N; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR PIRSF; PIRSF037239; Exonuclease_Xrn2; 2.
DR SMART; SM00343; ZnF_C2HC; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 3: Inferred from homology;
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|PIRNR:PIRNR037239};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR037239};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW ECO:0000256|PIRNR:PIRNR037239};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|PIRNR:PIRNR037239};
KW Reference proteome {ECO:0000313|Proteomes:UP000249390};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 259..273
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 410..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..1041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..971
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..997
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1022
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1041 AA; 117022 MW; 27E6BCF54E6DD639 CRC64;
MGVPAFYRWL ADRYPLSIAD VAEEEPRDGM PFPVDVSGPN PNGMEFDNLY LDMNGIIHPC
FHPEGMPAPA TYNDVFKSIF EYIDHLFSLI RPRKLLYLAI DGVAPRAKMN QQRTRRFKAA
KDAAETEAEE RLRKEFEIEG AKLSVEKTET SDSNVITPGT PFMAVLSVAL QYYIQSRLNS
NAGWRFTKVI LSDANVPGEG EHKIMSYIRL QRDLPGFDPN TSHCLYGLDA DLIMLSLATH
EVHFSILREV IPPPGQQNKC YACGQSGHLA ADCNGIGFSQ TADANGKASN AIPIHKKKYQ
LINMWVLREY LQHDLAISHP PFKIDFERVL DDFVFLCFFV GNDFLPHMPT LEIREGAINL
LMAVYRTEFT AMGGYLTDAG EVSLDRAEHF IQAVARHEDQ IFRKRARISQ ARNDSNDEPS
PPDVDKVRLG EPGYKDRYYL EKFGLSSPAE IEMTRQDVVQ KYVEGLCWVC RYYFQGVCSW
QWFYPYHYAP FASDLKGLAD LEITFFRGEP FRPFDQLMGV LPAASSSALP ERYRTLMTDP
SSPIIEFYPT DFELDMNGKR FAWQAVVKLP FIDENKLLAE TKRLEDTLTP EEQLRNSVMF
DLLYIHPLHP LAPYILTYYR HNVSVPRKEQ IPWPIDASTS GGMNGFIWLS ERNGLKNVVP
PPIPELDAIT NNQILNITFL NPPPHKHIPK PPAGVIMPSK AVRQFDVKPL PALWHEEYGS
RRQLGKDRPP VAGAIAGPSL GEAAHRLLKS TLNIGYGGNC GGASNQANFR NSPGSNNMIT
KPRAFGGSWG RDEGFYDQTN SNQSSAGNHV GYRARGAVQS GRFCDDPSSY GNHYNNAPRG
VMGIPGPRYG PPSPYEFQGN RQHFRGQDRV FHQDQYHGNR GGMPLSVPNE FHGTRQNYRG
QDRHFHPEQY HGIRGGPSLP APNEFQGNRQ NFRGPGRLLH QDPTHGIRGG MSALTIEGSG
RTRQQTAPSP RLPHLQPIPP FANNNVGPLP SPPPRWITRP SSSGGRGMSS KQQITSNDGR
EKQVKMVYQV KTRPAHPGSL Q
//
