ID W7TMF7_9STRA Unreviewed; 1198 AA.
AC W7TMF7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=5'-3' exoribonuclease {ECO:0000256|PIRNR:PIRNR037239};
DE EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR037239};
GN ORFNames=Naga_100010g30 {ECO:0000313|EMBL:EWM27232.1};
OS Nannochloropsis gaditana.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Eustigmatophyceae;
OC Eustigmatales; Monodopsidaceae; Nannochloropsis.
OX NCBI_TaxID=72520 {ECO:0000313|EMBL:EWM27232.1, ECO:0000313|Proteomes:UP000019335};
RN [1] {ECO:0000313|EMBL:EWM27232.1, ECO:0000313|Proteomes:UP000019335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-31 {ECO:0000313|EMBL:EWM27232.1,
RC ECO:0000313|Proteomes:UP000019335};
RX PubMed=23966634; DOI=10.1093/mp/sst120;
RA Corteggiani Carpinelli E., Telatin A., Vitulo N., Forcato C., D'Angelo M.,
RA Schiavon R., Vezzi A., Giacometti G.M., Morosinotto T., Valle G.;
RT "Chromosome Scale Genome Assembly and Transcriptome Profiling of
RT Nannochloropsis gaditana in Nitrogen Depletion.";
RL Mol. Plant 7:323-335(2014).
CC -!- FUNCTION: Possesses 5'->3' exoribonuclease activity. May promote
CC termination of transcription by RNA polymerase II.
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}.
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:EWM27232.1}.
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DR EMBL; AZIL01000517; EWM27232.1; -; Genomic_DNA.
DR AlphaFoldDB; W7TMF7; -.
DR EnsemblProtists; EWM27232; EWM27232; Naga_100010g30.
DR OrthoDB; 167745at2759; -.
DR Proteomes; UP000019335; Chromosome 7.
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: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 PANTHER; PTHR12341:SF41; 5'-3' EXORIBONUCLEASE 1; 1.
DR PANTHER; PTHR12341; 5'->3' EXORIBONUCLEASE; 1.
DR Pfam; PF17846; XRN_M; 2.
DR Pfam; PF03159; XRN_N; 1.
DR PIRSF; PIRSF037239; Exonuclease_Xrn2; 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 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:UP000019335};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552}.
FT DOMAIN 1..254
FT /note="Xrn1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03159"
FT DOMAIN 326..430
FT /note="Xrn1 helical"
FT /evidence="ECO:0000259|Pfam:PF17846"
FT DOMAIN 595..955
FT /note="Xrn1 helical"
FT /evidence="ECO:0000259|Pfam:PF17846"
FT REGION 448..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1018..1053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1073..1136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 647..674
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 450..477
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..622
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1018..1039
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1074..1103
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1109..1136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1166..1181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1198 AA; 134017 MW; C2E66266B7C3D8D6 CRC64;
MGVPAFFRWL SEKYPRTVLD MVEQRPQVVD GVPLPMDLRA PNPNNMEFDN LYIDMNGIIH
PCSHPEDRPT PKTEAEMFVN VMVYVDRIFA AVRPRRLVFL AIDGVAPRAK MNQQRTRRFR
SAGDARERHE IKLATRQEMV AMGLPVPPEE LDKEWDSNVI TPGTEFMVTL ASYLRFYVAH
RVNTCKAWQQ VKVLFSDGSE PGEGEHKIMD FIRKERAQPG YDPNTRHILH GLDADLIMLA
LATHEPHFTI LREQVFFGRR GRDGPQVSAA QSAFDAMQGQ KADDGLARGE GSRFPYLKPF
QMLHIPTLRE YLEEEFRSLR GLPFGYNFER VVDDFVFLCF FVGNDFLPHL PSLDIRDGAI
DFLLNVYKRV LPAMGDYLTA PGGTVNLEQV DIILAEVGRV EDEVFRRRRA GEEQHQARLN
RRVREVERRH GGTVQELSAR IVPADVQPLG RPKLPHPVPR LSPVASPFLP APPGPSPEEK
NMKNKSVAQQ LREKLKKPKK ELENGVAGVE GGPEASDAPI GDDCEAGMKH ELDHTTKMET
PVIEASDSAK PVKRVKTEDS NIMDDKADLV TLKEPGSVTA LGMSVEMCLE TTASAQDSQE
GTKELEEDDE DVGDDAMGEE EGKEEFEDPH IVVPPELEGT ELAAAQKELA ERVKSKQEAR
LDRLKEEIED TIRYHEAGWK DRYYQDKLKK QNLEKGGGRE HMYRTYIEGL CWVFQYYYRG
CQAWGWFYPF HYAPFASDLV NIERYHVAFE AGKPLRPLEQ LMAVLPPESA DALPVPLARL
MTSQDSPIKD FYPRDVEVDP NGKAMPWLWV TLLPFIDEAR LLESIAAVES QLSEAEKKRN
VVGGSLLCLH EYHPTFRAIA RVLEVEGAQD RAGVEVEAAS AQGFSGTLLP PPPDAALRLT
AQVVAPKMPP SVLQDVEDNR VLVAGFTLPS QTTPHASALL PGLTHPPRRL TDRDLQPRRP
PRLGRGINIA ELGTQFGFNE VHATAAHRLI VQNMPRGAGS GSMLIYQQNQ QQRMSCGGYI
GSGQTGTRSW GSFEPQNQGK QRPPPRLPAP SLYPGLGGGL ACGAYSATPN LPHPAHMGPR
PPLLFPEPPM MSGGPPFPPG PYSHQVAPHY SGQKPQSQQQ QQQQQQQQQY GQHAYQVQQA
SGFPPTPLFQ GIDAGLMNSL RRGVAHAVEQ RSHEGRGGQR LHPPRPLHSK NGQQHQRR
//
