ID   H3BNM8_HUMAN            Unreviewed;       214 AA.
AC   H3BNM8;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=U6 snRNA phosphodiesterase {ECO:0000256|HAMAP-Rule:MF_03040};
DE            EC=3.1.4.- {ECO:0000256|HAMAP-Rule:MF_03040};
GN   Name=USB1 {ECO:0000256|HAMAP-Rule:MF_03040,
GN   ECO:0000313|Ensembl:ENSP00000454928.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000454928.1, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000454928.1, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA   Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA   Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA   Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA   Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA   Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA   Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA   Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA   Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA   Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA   Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA   Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA   Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA   Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA   Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA   Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA   DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA   Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA   Myers R.M., Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [2] {ECO:0000313|Ensembl:ENSP00000454928.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Phosphodiesterase responsible for the U6 snRNA 3' end
CC       processing. Acts as an exoribonuclease (RNase) responsible for trimming
CC       the poly(U) tract of the last nucleotides in the pre-U6 snRNA molecule,
CC       leading to the formation of mature U6 snRNA 3' end-terminated with a
CC       2',3'-cyclic phosphate. {ECO:0000256|HAMAP-Rule:MF_03040}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 3'-end uridylyl-adenosine-RNA = a 3'-end 2',3'-cyclophospho-
CC         uridine-RNA + adenosine; Xref=Rhea:RHEA:67896, Rhea:RHEA-COMP:17385,
CC         Rhea:RHEA-COMP:17386, ChEBI:CHEBI:16335, ChEBI:CHEBI:85644,
CC         ChEBI:CHEBI:176518; Evidence={ECO:0000256|ARBA:ARBA00029305};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67897;
CC         Evidence={ECO:0000256|ARBA:ARBA00029305};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 3'-end uridylyl-uridine-RNA = a 3'-end 2',3'-cyclophospho-
CC         uridine-RNA + uridine; Xref=Rhea:RHEA:46052, Rhea:RHEA-COMP:17384,
CC         Rhea:RHEA-COMP:17385, ChEBI:CHEBI:16704, ChEBI:CHEBI:85643,
CC         ChEBI:CHEBI:85644; Evidence={ECO:0000256|ARBA:ARBA00029300};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46053;
CC         Evidence={ECO:0000256|ARBA:ARBA00029300};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|HAMAP-Rule:MF_03040}.
CC   -!- SIMILARITY: Belongs to the 2H phosphoesterase superfamily. USB1 family.
CC       {ECO:0000256|HAMAP-Rule:MF_03040}.
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DR   EMBL; AC010543; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC012182; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001317497.1; NM_001330568.1.
DR   RefSeq; XP_011521631.1; XM_011523329.2.
DR   ProteomicsDB; 41243; -.
DR   Antibodypedia; 29032; 160 antibodies from 24 providers.
DR   DNASU; 79650; -.
DR   Ensembl; ENST00000561743.5; ENSP00000454928.1; ENSG00000103005.13.
DR   Ensembl; ENST00000698444.1; ENSP00000513726.1; ENSG00000103005.13.
DR   GeneID; 79650; -.
DR   UCSC; uc059uyv.1; human.
DR   CTD; 79650; -.
DR   HGNC; HGNC:25792; USB1.
DR   VEuPathDB; HostDB:ENSG00000103005; -.
DR   GeneTree; ENSGT00390000004596; -.
DR   HOGENOM; CLU_057212_2_0_1; -.
DR   OMA; YTNEERT; -.
DR   OrthoDB; 462025at2759; -.
DR   BioGRID-ORCS; 79650; 69 hits in 1163 CRISPR screens.
DR   ChiTaRS; USB1; human.
DR   GenomeRNAi; 79650; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   Bgee; ENSG00000103005; Expressed in granulocyte and 180 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.1140.10; Cyclic phosphodiesterase; 1.
DR   HAMAP; MF_03040; USB1; 1.
DR   InterPro; IPR027521; Usb1.
DR   PANTHER; PTHR13522:SF3; U6 SNRNA PHOSPHODIESTERASE 1; 1.
DR   PANTHER; PTHR13522; UNCHARACTERIZED; 1.
DR   Pfam; PF09749; HVSL; 1.
PE   1: Evidence at protein level;
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_03040};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_03040};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03040};
KW   Proteomics identification {ECO:0007829|EPD:H3BNM8,
KW   ECO:0007829|MaxQB:H3BNM8};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640}.
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..22
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        69
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03040"
FT   ACT_SITE        157
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03040"
SQ   SEQUENCE   214 AA;  24814 MW;  8BA7DFED0D127076 CRC64;
     MFPGTEEGPE DDSTKHGGRV RTFPHERGNW ATHVYVPYEA KEEFLDLLDV LLPHAQTYVP
     RLVRMKVFHL SLSQSVVLRH HWILPFVQAL KARMTSFHRF FFTANQVKIY TNQEKTRTFI
     GLEVTSGHAQ FLDLVSEVDR VMEEFNLTTF YQDPSFHLSL AWCVGDARLQ LEGQCLQELQ
     AIVDGFEDAE VLLRVHTEQV RCKSGNKFFS MPLK
//