ID A0A5D2ZB66_GOSMU Unreviewed; 1104 AA.
AC A0A5D2ZB66;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=5'-3' exoribonuclease {ECO:0000256|PIRNR:PIRNR037239};
DE EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR037239};
GN ORFNames=E1A91_A05G273700v1 {ECO:0000313|EMBL:TYJ35948.1};
OS Gossypium mustelinum (Cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=34275 {ECO:0000313|EMBL:TYJ35948.1, ECO:0000313|Proteomes:UP000323597};
RN [1] {ECO:0000313|EMBL:TYJ35948.1, ECO:0000313|Proteomes:UP000323597}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1408120.09 {ECO:0000313|EMBL:TYJ35948.1};
RA Chen Z.J., Sreedasyam A., Ando A., Song Q., De L., Hulse-Kemp A., Ding M.,
RA Ye W., Kirkbride R., Jenkins J., Plott C., Lovell J., Lin Y.-M., Vaughn R.,
RA Liu B., Li W., Simpson S., Scheffler B., Saski C., Grover C., Hu G.,
RA Conover J., Carlson J., Shu S., Boston L., Williams M., Peterson D.,
RA Mcgee K., Jones D., Wendel J., Stelly D., Grimwood J., Schmutz J.;
RT "WGS assembly of Gossypium mustelinum.";
RL Submitted (JUL-2019) 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 -!- 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; CM017640; TYJ35948.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5D2ZB66; -.
DR Proteomes; UP000323597; Chromosome a05.
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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000323597};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 262..276
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 416..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 826..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 908..938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 981..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1040..1104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 499..526
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 455..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..861
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1026
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1064
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1065..1090
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1104 AA; 126419 MW; 5D980447D1BFB229 CRC64;
MGVPAFYRWL AEKYPLIVVD VIEEEPVVIE GVSIPVDTSK PNPNKLEYDN LYLDMNGIIH
PCFHPEDRPS PTTFDEVFQC IFDYIDRLFV MVRPRKLLYM AIDGVAPRAK MNQQRSRRFR
AAKDAAEAAA EEARLREEFE REGRRLPPKE ESQLVDSNVI TPGTPFMAVL SIALQYYIHL
RLNYDPGWKN IKVILSDANV PGEGEHKIMS YIRLQRNLPG FDPNTRHCLY GLDADLIMLA
LATHEVHFSI LREIVFTPGQ DKCFICGQMG HIAANCEGKA KRKEGEFDEK ADGKAVARKP
YQFLNIWTLR EYLEYEMRIP NPPFEIDLER VVDDFIFICF FVGNDFLPHM PTLEIREGAI
NLLMAVYKKE FRSFGGYLTD GSKPNLSRVE HFIQAVGSYE DKIFNKRARL HQRQAERIKR
EKAQARRGDD AQPQVQPDSL VPVARFHGSR LASGPTPVPF QQTVESNGNG SSSRPHKVRH
LSSGANIGAA IVEAEDSIET DVHENKEELK AKLKELIRDK SDVFNSSNHE EDKIKLGEPG
WKERYYQEKF SAKTPEEMEE IRKDVVLKFT EGLCWVMHYY YEGVCSWRWF YPYHYAPFAS
DLKDLGQLDI QFELGSPFKP FNQLLGVFPA ASSHALPEQY RKLMTDPNSP IIDFYPTDFE
VDMNGKRYSW QGIAKLPFID EERLLAEVAK IEHTLTEEEA QRNSTMCDML FVAASHRLSE
QIFSLDSRCK QLPERQRIEV KEEVKPDLRY ECSDGMNGYI SPCAGDTQPP VFRSPIKDME
DILANEVICC IYRLPRAHKH ITRPPPGVAF PPKMVQFSDL KPAPALWHED SGRRPWENGR
QPAGGHQMDR HNSSGSVSGQ DASHRLITNS LQLKMDRNGF GNNIHASSYA IAPYNPSVNS
HANYGYHNQG QPRIVPPRQD YPGAGYPYSQ NPPSRHPNSQ GYHHYQINNE EAANNMHYPP
RHYQDGRARH IPMAQMSAEA DLYPSHPGGY DRSRRYQAPE NSSYQQWGGR MAPQANQNVS
GGYGLYQQGG VNQGVYRGRD QQQQRGNQSY HHHQRGDYEE RGSQPHRGSQ QYFGSNQQHG
GSQQQRGNPY SALDRRGHRR PPNH
//
