USB1_NEUCR
ID USB1_NEUCR Reviewed; 364 AA.
AC Q7SEZ0;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=U6 snRNA phosphodiesterase 1 {ECO:0000250|UniProtKB:Q12208};
DE AltName: Full=3'-5' RNA exonuclease USB1 {ECO:0000250|UniProtKB:Q12208};
DE EC=4.6.1.- {ECO:0000250|UniProtKB:Q12208};
GN Name=usb1; ORFNames=NCU02073, NCU20780;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- FUNCTION: 3'-5' RNA exonuclease that trims the 3' end of oligo(U)
CC tracts of the pre-U6 small nuclear RNA (snRNA) molecule, leading to the
CC formation of a U6 snRNA 3' end-terminated with a 2',3'-cyclic phosphate
CC (By similarity). Participates in the U6 snRNA 3' end processing that
CC prevents U6 snRNA degradation (By similarity).
CC {ECO:0000250|UniProtKB:Q12208}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03040}.
CC -!- SIMILARITY: Belongs to the 2H phosphoesterase superfamily. USB1 family.
CC {ECO:0000255|HAMAP-Rule:MF_03040}.
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DR EMBL; CM002236; EAA35364.2; -; Genomic_DNA.
DR RefSeq; XP_964600.2; XM_959507.2.
DR AlphaFoldDB; Q7SEZ0; -.
DR SMR; Q7SEZ0; -.
DR STRING; 5141.EFNCRP00000001230; -.
DR EnsemblFungi; EAA35364; EAA35364; NCU02073.
DR GeneID; 3880740; -.
DR KEGG; ncr:NCU02073; -.
DR VEuPathDB; FungiDB:NCU02073; -.
DR HOGENOM; CLU_050234_1_0_1; -.
DR InParanoid; Q7SEZ0; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:1990838; F:poly(U)-specific exoribonuclease activity, producing 3' uridine cyclic phosphate ends; IEA:UniProtKB-UniRule.
DR GO; GO:0034477; P:U6 snRNA 3'-end processing; IBA:GO_Central.
DR HAMAP; MF_03040; USB1; 1.
DR InterPro; IPR027521; Usb1.
DR PANTHER; PTHR13522; PTHR13522; 1.
DR Pfam; PF09749; HVSL; 1.
PE 3: Inferred from homology;
KW Hydrolase; Lyase; Nuclease; Nucleus; Reference proteome.
FT CHAIN 1..364
FT /note="U6 snRNA phosphodiesterase 1"
FT /id="PRO_0000420794"
FT REGION 1..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 182
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03040"
FT ACT_SITE 289
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03040"
FT BINDING 182..184
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ65"
FT BINDING 279
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ65"
FT BINDING 279
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ65"
FT BINDING 281..291
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ65"
FT BINDING 287..291
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ65"
SQ SEQUENCE 364 AA; 39920 MW; 7083FCFB2C0C9376 CRC64;
MKRPLVDYDS GSGSESECGS SSDGPKSSST NIPPQLKKRR NGDIGTRAPP SAPASTPIAP
LGRSSGTHTI PPKPAPKSTS SLPPISDRFN DLYASNTRTA VSDDPSLHQG RQRQVPHIPG
NWPSHVYIDW DPSSGDRELL SSLVDKLQTR VAAAAQRYPD LEGVKISTAL RDPELPVDKP
LHISLSAPLT LTSKNKDAFL DDVTRALRSS GVSPFVVDFS GGVNWYRSEE STRSFLVLRV
REVQNTGMTT ADSSPNPRLT TLLQRCNKTA KEYGQPPLYD SQDMGYRFHV TIAWTHARPS
ESLKQLTDSI FDDCKTMYSE NMSIRDKLCT GSSFRVETVK VKIGNHVTRF ELPDKGLALP
VKTT
