ID A0A1R2BZ47_9CILI Unreviewed; 716 AA.
AC A0A1R2BZ47;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=5'-3' exoribonuclease {ECO:0000256|PIRNR:PIRNR037239};
DE EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR037239};
GN ORFNames=SteCoe_17518 {ECO:0000313|EMBL:OMJ81927.1};
OS Stentor coeruleus.
OC Eukaryota; Sar; Alveolata; Ciliophora; Postciliodesmatophora;
OC Heterotrichea; Heterotrichida; Stentoridae; Stentor.
OX NCBI_TaxID=5963 {ECO:0000313|EMBL:OMJ81927.1, ECO:0000313|Proteomes:UP000187209};
RN [1] {ECO:0000313|EMBL:OMJ81927.1, ECO:0000313|Proteomes:UP000187209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM001 {ECO:0000313|EMBL:OMJ81927.1};
RA Slabodnick M., Ruby J.G., Reiff S.B., Swart E.C., Gosai S., Prabakaran S.,
RA Witkowska E., Larue G.E., Fisher S., Freeman R.M., Gunawardena J., Chu W.,
RA Stover N.A., Gregory B.D., Nowacki M., Derisi J., Roy S.W., Marshall W.F.,
RA Sood P.;
RT "The macronuclear genome of Stentor coeruleus: a giant cell with tiny
RT introns.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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:OMJ81927.1}.
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DR EMBL; MPUH01000361; OMJ81927.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R2BZ47; -.
DR OrthoDB; 167745at2759; -.
DR Proteomes; UP000187209; 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 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; 2.
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:UP000187209};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 227..242
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
SQ SEQUENCE 716 AA; 83627 MW; 63F23E1930FA3D08 CRC64;
MGVPTFFKWL SLRYPKSIVQ SNSAQHELPN FDNLYLDMNG IIHPCCNPPE GDKPTSEEQM
FENIFKYVEE LVNLVKPRNL IYLAIDGVAP RAKMNQQRAR RYRKIQEERE RPRAQTSDFR
FDSNVITPGT PFMYRLSEAI HKFVLKKLQT SWKNLQVIFS DSNNPGEGEH KILEFVRIQR
SLPNYNPNTK HVIFGADADL IMLSLITHEA HFYIIRESLI DFRTLYCKTC GQTGHFEQDC
ERIARSDQPS TSSKFQFIKV PVLRQYLFYE FKDLTKFPIF DFERIIDDFV FLCFFVGNDF
LPHLPSMHIR DGAIDGLIYL YGKIFPKLGG YLTENGKVVL YRVDMIMAEV GKIEEEYFKE
KEEREMFIRK RYEGSKKKND IKEDNVGSSD NPIEVEDIIK LGQEGWKLRY YSEKFKVEGE
EVEEFRRRIH TSYMEGLSWV FEYYFQGCAS WGWYFPFHYA PFASDLYNSA SLRLKFEYGN
PFQPYAQLLS VLPAESCTAL PIALRPLITE DISEISDFYP RDFHLDINGK RFAWQGVMLL
PFIEENRLLQ ALQEKISLLD IDDIERNSEG ETFLYSNKEI PGVNMNFISK KPKFRMYTID
EGCTIRFDVV QNHVKGKHQS KKLDGVVDAD LEVDESIFRA GDRRGFGASN MISMIAKNFA
MDPYNDKWRP QNRNFKVCEI VKNDPKPEKK PRAEPPQETL VDNIKKLVAL LGGGKK
//
