TUT3_TRYBB
ID TUT3_TRYBB Reviewed; 889 AA.
AC Q6B9Y8;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Terminal uridylyltransferase 3 {ECO:0000305};
DE Short=TUTase 3 {ECO:0000303|PubMed:15304317};
DE EC=2.7.7.52 {ECO:0000269|PubMed:15304317, ECO:0000269|PubMed:18191648};
DE AltName: Full=3' terminal uridylyl transferase {ECO:0000305};
DE AltName: Full=RNA editing 3' terminal uridylyltransferase 3 {ECO:0000305};
GN Name=TUT3 {ECO:0000303|PubMed:15304317};
OS Trypanosoma brucei brucei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=5702;
RN [1] {ECO:0000312|EMBL:AAT77544.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RX PubMed=15304317; DOI=10.1016/j.febslet.2004.07.004;
RA Aphasizhev R., Aphasizheva I., Simpson L.;
RT "Multiple terminal uridylyltransferases of trypanosomes.";
RL FEBS Lett. 572:15-18(2004).
RN [2] {ECO:0000305}
RP CATALYTIC ACTIVITY.
RX PubMed=18191648; DOI=10.1016/j.bbagrm.2007.12.007;
RA Aphasizhev R., Aphasizheva I.;
RT "Terminal RNA uridylyltransferases of trypanosomes.";
RL Biochim. Biophys. Acta 1779:270-280(2008).
CC -!- FUNCTION: Terminal uridylyltransferase which catalyzes the addition of
CC Us to the 3'-hydroxyl group of single-stranded RNAs (PubMed:15304317).
CC Does not mediate RNA-independent UTP polymerization (PubMed:15304317).
CC {ECO:0000269|PubMed:15304317}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=RNA(n) + UTP = diphosphate + RNA(n)-3'-uridine ribonucleotide;
CC Xref=Rhea:RHEA:14785, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17348,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:140395,
CC ChEBI:CHEBI:173116; EC=2.7.7.52;
CC Evidence={ECO:0000269|PubMed:15304317, ECO:0000269|PubMed:18191648};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15304317};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q8WQX6};
CC Note=Binds 1 Mg(2+) or Mn(2+) per subunit.
CC {ECO:0000250|UniProtKB:Q8WQX5};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=KM is 36-48 uM for UTP (at 27 degrees Celsius and with 12(U)
CC single-stranded RNA as substrate). {ECO:0000269|PubMed:15304317};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:15304317}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
CC {ECO:0000305}.
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DR EMBL; AY672414; AAT77544.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6B9Y8; -.
DR SMR; Q6B9Y8; -.
DR EnsemblProtists; EAN78138; EAN78138; Tb10.6k15.3370.
DR HOGENOM; CLU_324806_0_0_1; -.
DR OMA; RSICANG; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0050265; F:RNA uridylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0071076; P:RNA 3' uridylation; IDA:UniProtKB.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002058; PAP_assoc.
DR Pfam; PF03828; PAP_assoc; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW Nucleotidyltransferase; RNA-binding; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..889
FT /note="Terminal uridylyltransferase 3"
FT /id="PRO_0000450680"
FT DOMAIN 505..572
FT /note="PAP-associated"
FT /evidence="ECO:0000255"
FT ZN_FING 123..151
FT /note="C2H2-type; atypical"
FT /evidence="ECO:0000250|UniProtKB:Q8WQX5"
FT REGION 675..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 565..574
FT /note="Nucleotide recognition motif (NRM)"
FT /evidence="ECO:0000250|UniProtKB:Q8WQX5"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8WQX5"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8WQX5"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8WQX5"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8WQX5"
FT BINDING 225
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q381M1"
FT BINDING 236..239
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q381M1"
FT BINDING 237
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q381M1"
FT BINDING 239
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q381M1"
FT BINDING 286
FT /ligand="RNA"
FT /ligand_id="ChEBI:CHEBI:33697"
FT /evidence="ECO:0000250|UniProtKB:Q381M1"
FT BINDING 394..398
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q381M1"
FT BINDING 419
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q381M1"
FT BINDING 423
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q381M1"
FT BINDING 437..438
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q381M1"
FT SITE 387
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q381M1"
SQ SEQUENCE 889 AA; 99346 MW; EC68C060A904AE8A CRC64;
MIFFFKKRYH VFLKAPSIRL MPCSFFFFRS FIKVIFIIRC IFFSSLSGDS CPTQRSRSTL
ACMFTSVPVA PTVVPGVVYS SGVHEEWKEA EQKLLDGCLI HSEGDGATKQ IKEKLTSRNS
QSVRCDLCAK MIESRDEEQI QEHFQVHHAA LSLWCREILA SKDNLLHYGC IPSGHIVSCG
NFVLESAATL DMGRKTFDVI ERAFSQMSQV ISCFVRNLVL FPFGSCVSCG CWDGVSDADF
TAIGLQDMKK GKWPPEDEKK VILRLTAALR KAGFFFGELE PLVRTRVPVV RRVQKVRVPL
RSHGEHDTYS VVWSNSKEFS SPPRMLVEAA ISSTVERKDS DTVTFHFKDS LKAVKFFCNS
AMCGPRDMEV SWKTGSQLPE MFSLDFDLSC RAQGVRNSLF LRKYFQQDPF VRTGYLFLKK
WSKLYGINNA KNGYLTSYAM SILWVHFLLE NGLVKFVRPA DVEPIPDLSQ QKMSYLPLLR
DDGDGGERPS DVLKSPELTM LRGALGGLIP LFFLYYTRIR WDKVVVTLRV PGGGPPVTPD
SLGWVEANEV KCGPLRDRVW YRLCIDDPYE DNFNLGRHLS PDKASFVKVQ FMRALASIVA
GRPQQLLVDE QKFAEETMPA YVTRLSVQGE LRNLRPVTVS ALRQLLIDSA GADCVAIYEA
SHNWETLLDM ASTLNNKSKE GDDDAEGVTN NQEGEPPDHV ESCEAPRRHL LCSKMHSIDD
ALLVAGPLGV SDANIPAGLL GVYFLARGRA FRTAEDRDNF LMHAEAVSAA RARGCTTREE
ILERVADAIP SIVRNGTLLD DLLVSGSEEN ITVQSPVVVE TRCAETVQRK KSKGSKKRKN
AVRRGNHAGQ GTCSECGASG TDLWEASDKS ADDGLYCGAC WKAYNCQKN
