ID A0A2R6WDJ0_MARPO Unreviewed; 1015 AA.
AC A0A2R6WDJ0;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=5'-3' exoribonuclease {ECO:0000256|PIRNR:PIRNR037239};
DE EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR037239};
GN ORFNames=MARPO_0105s0035 {ECO:0000313|EMBL:PTQ31923.1};
OS Marchantia polymorpha (Common liverwort) (Marchantia aquatica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=3197 {ECO:0000313|EMBL:PTQ31923.1, ECO:0000313|Proteomes:UP000244005};
RN [1] {ECO:0000313|Proteomes:UP000244005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 {ECO:0000313|Proteomes:UP000244005};
RX PubMed=28985561; DOI=10.1016/j.cell.2017.09.030;
RA Bowman J.L., Kohchi T., Yamato K.T., Jenkins J., Shu S., Ishizaki K.,
RA Yamaoka S., Nishihama R., Nakamura Y., Berger F., Adam C., Aki S.S.,
RA Althoff F., Araki T., Arteaga-Vazquez M.A., Balasubrmanian S., Barry K.,
RA Bauer D., Boehm C.R., Briginshaw L., Caballero-Perez J., Catarino B.,
RA Chen F., Chiyoda S., Chovatia M., Davies K.M., Delmans M., Demura T.,
RA Dierschke T., Dolan L., Dorantes-Acosta A.E., Eklund D.M., Florent S.N.,
RA Flores-Sandoval E., Fujiyama A., Fukuzawa H., Galik B., Grimanelli D.,
RA Grimwood J., Grossniklaus U., Hamada T., Haseloff J., Hetherington A.J.,
RA Higo A., Hirakawa Y., Hundley H.N., Ikeda Y., Inoue K., Inoue S.I.,
RA Ishida S., Jia Q., Kakita M., Kanazawa T., Kawai Y., Kawashima T.,
RA Kennedy M., Kinose K., Kinoshita T., Kohara Y., Koide E., Komatsu K.,
RA Kopischke S., Kubo M., Kyozuka J., Lagercrantz U., Lin S.S., Lindquist E.,
RA Lipzen A.M., Lu C.W., De Luna E., Martienssen R.A., Minamino N.,
RA Mizutani M., Mizutani M., Mochizuki N., Monte I., Mosher R., Nagasaki H.,
RA Nakagami H., Naramoto S., Nishitani K., Ohtani M., Okamoto T., Okumura M.,
RA Phillips J., Pollak B., Reinders A., Rovekamp M., Sano R., Sawa S.,
RA Schmid M.W., Shirakawa M., Solano R., Spunde A., Suetsugu N., Sugano S.,
RA Sugiyama A., Sun R., Suzuki Y., Takenaka M., Takezawa D., Tomogane H.,
RA Tsuzuki M., Ueda T., Umeda M., Ward J.M., Watanabe Y., Yazaki K.,
RA Yokoyama R., Yoshitake Y., Yotsui I., Zachgo S., Schmutz J.;
RT "Insights into land plant evolution garnered from the Marchantia polymorpha
RT genome.";
RL Cell 171:287-304.e15(2017).
CC -!- FUNCTION: Possesses 5'->3' exoribonuclease activity. Acts as an
CC endogenous post-transcriptional gene silencing (PTGS) suppressor.
CC {ECO:0000256|PIRNR:PIRNR037239}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the 5'-3' exonuclease family. XRN2/RAT1
CC subfamily. {ECO:0000256|ARBA:ARBA00006994,
CC ECO:0000256|PIRNR:PIRNR037239}.
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DR EMBL; KZ772777; PTQ31923.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R6WDJ0; -.
DR EnsemblPlants; PTQ31923; PTQ31923; MARPO_0105s0035.
DR Gramene; PTQ31923; PTQ31923; MARPO_0105s0035.
DR Proteomes; UP000244005; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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 GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
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 InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR12341:SF41; 5'-3' EXORIBONUCLEASE 1; 1.
DR PANTHER; PTHR12341; 5'->3' EXORIBONUCLEASE; 1.
DR Pfam; PF17846; XRN_M; 1.
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 SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000244005};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 263..277
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 411..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 820..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..1015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..868
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..929
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..1015
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1015 AA; 114688 MW; DA37426823A7EC64 CRC64;
MGVPAFYRWL ADKYPLIVVD CIEEEVQVIE NVRVPIDTTK PNPNGLEYDN LYLDMNGIIH
PCFHPEDRPA PTTFSEVYEC MFDYIDRLFA IVRPRKVLYM AIDGVAPRAK MNQQRSRRFR
AAKDAQDAAE EEERLRKEFL AEGRNIPPKE KSEAYDSNVI TPGTPFMGSL SIALQYYIHL
RLNHDPGWRY IKVILSDANV PGEGEHKIMS YIRLQRNLPG FDPNTRHCLY GLDADLIMLA
LATHEVHFSI LREVVFMPGQ QDKCFLCGQV GHLAADCEGK PKRKRGEHDE KGEAEIVPKK
PFQFLHIWTL REYLEFDMSI PNPPFEVDFE RLVDDFVFMC FFVGNDFLPH MPTLEIREGA
INLLMLVYKR EFKQMGGYLT EDGEVNLKRV EYFIQIIGAQ EETIFQKRAR IHQRQADRRR
REKGQLKRGD DAEPTVPPEQ LFPAEDQQDE ADNVEELKLK LKNVLREKSD MTSGGKEIED
AVRLGEPGWK ERYYVEKFET RTAEEMEEIR RDVVLKFTEG LCWVMRYYYQ GVCSWNWYYP
YHYAPFASDL TGLDELEITF FLGRPFKPFD QLMGVLPAAS SNALPKMYRP LMSDPNSPII
DFYPTDFDVD MNGKRFSWQG VAKLPFIEED RLLAEISKVE GTLTPEERKR NSTLSEMLYV
SCSHSLAPYI FSFYDRCGHL VGQARAEAKE EIDPIASGGM NGYLYLCDGE ACPAMFRSPV
EGMSSITNNQ VLSVIYKLPP HHRHIAKPPE GVVMPKKEVT EQDVKTQPLW HEDNGRRQQI
QDRPPVAGAL AGQVLGEAAR RLLVNSLPNR HNSSGGAMQM LQRQAQQASG SGGILGAPAP
YQHPSAQGIP PGGRPRPAGP PGYEQGFGPP SPPYGGVYGA GQTYAQAAYP SAPQHQYPVP
GGYAPPSNGG SYYPPTSRQS HQLHQSHQPH HTVPRAPPAV GGPGFMGRGG PYQQPPPHHS
QQSGPQAPNA WNGGRGASGT QNFSRVQQQV VTTNSFTALQ GRGRGGRQQN NNNRY
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