ID F7C464_HORSE Unreviewed; 1501 AA.
AC F7C464;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 4.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=RNA uridylyltransferase {ECO:0000256|ARBA:ARBA00012472};
DE EC=2.7.7.52 {ECO:0000256|ARBA:ARBA00012472};
GN Name=TUT7 {ECO:0000313|Ensembl:ENSECAP00000012771.4,
GN ECO:0000313|VGNC:VGNC:25180};
GN Synonyms=ZCCHC6 {ECO:0000313|VGNC:VGNC:25180};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000012771.4, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000012771.4, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000012771.4,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000012771.4}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000012771.4};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00024498};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR Ensembl; ENSECAT00000015846.4; ENSECAP00000012771.4; ENSECAG00000014831.4.
DR VGNC; VGNC:25180; TUT7.
DR GeneTree; ENSGT00940000156859; -.
DR TreeFam; TF315661; -.
DR Proteomes; UP000002281; Chromosome 23.
DR Bgee; ENSECAG00000014831; Expressed in bone marrow and 23 other cell types or tissues.
DR ExpressionAtlas; F7C464; baseline.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:UniProt.
DR GO; GO:0061157; P:mRNA destabilization; IEA:UniProt.
DR CDD; cd05402; NT_PAP_TUTase; 2.
DR Gene3D; 1.10.1410.10; -; 2.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 2.
DR Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002058; PAP_assoc.
DR InterPro; IPR045100; TUTase_dom.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR12271; POLY A POLYMERASE CID PAP -RELATED; 1.
DR PANTHER; PTHR12271:SF34; TERMINAL URIDYLYLTRANSFERASE 7; 1.
DR Pfam; PF03828; PAP_assoc; 2.
DR Pfam; PF19088; TUTase; 2.
DR Pfam; PF16631; TUTF7_u4; 1.
DR Pfam; PF00098; zf-CCHC; 3.
DR SMART; SM00343; ZnF_C2HC; 3.
DR SMART; SM00451; ZnF_U1; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 2.
DR SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 2.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 2.
DR PROSITE; PS50158; ZF_CCHC; 3.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Reference proteome {ECO:0000313|Proteomes:UP000002281};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 971..986
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 1353..1367
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 1458..1474
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 40..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1371..1433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1475..1501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..866
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..903
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1372..1414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1477..1501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1501 AA; 171493 MW; 223A52404910FA51 CRC64;
MGDAVKPYFM KRAKDRGNID DEDFRRGHPQ QDYLTMDDYA KGHSGKMEKG LPKKKISPGN
YGNTPRKGPY AVSSNPYAFK NPIYSQPAWI NDNHKDQSKR WLSDELAGNS DSWREFKPGP
RIPIINRPRK DLFQESEDGY RWQDGRGCRT VRRLFHKDLT SLETMSEMET GSPENKKQRS
RPRKPRRTRN EENEQDGDLE GPVIDESALS TKELLGLQQA EERLKRDCID RLKRKPRNYP
TAKYTCKLCD VLIESIAFAH KHIKEKRHKK NIKEKQEEEL LTTLPPPTPS QINAVGIAIE
KVVQEFGLHN ENLEQRLEIK RIMENVFQHK LPDCSLRLYG SSCSRLGFKN SDVNIDIQFP
AIMSQPDVLL LVQECLKNSD SFLDVDADFH ARVPVVVCRE KHSGLLCKVS AGNENACLTT
NHLTALGKLE SRLVPLVIAF RYWAKLCSID RPEEGGLPPY VFALMAVFFL QQRKEPLLPV
YLGSWIEGFS LNKLGNFNLK DIQKDVVLWE YSDNAAEDTD TAKEEAPKEV PVKRGQVSLT
FDLKHQPSVP VGQLWVELLR FYALEFNLAD LVISIRVKES ISRESKDWPK KRIAIEDPYS
VKRNVARTLN NQPVFEYILH CLRTTYKYFA LPHKITKSSL PKPLSTVMCI SEHSKEVAKR
DPAVQVKDDR LKNSILAQGS GAASSTANTC KVQSLTPKGT AASFESPPTQ EMGNAHVSVH
LENSDCIKAE VGCDDYEDIK VHHQETGGKT GKEKIKRESK KHLLTATIQA LSSSKHGELV
MCGSTQNDDT DSTLDLEGFQ NPTAKECDGY ASLDGKADVD EESMEGTDDL EDTLSHFAPS
RQGRTSGIIH SDEEEEEEEE EEEDEEPRLS VTRREDEDDI ANEDELDNIY TGSGDEDALS
EEDEELGRSA KYEDLKQSGK HVDGALLMEL NKISLKEENV HEENSAVHQS DFFYEFSKLT
FTKGKSPMVV CSLCKREGHL KKDCPEDFKR IQLEPLPPLT PKFSNILDQV CIQCYKDFSP
TILEDQAREH IRQNLESFIR QEFPGTKLSL FGSSKNGFGF KQSDLDVCMT INGLETAEGL
DCVRTIEELA RVLKKHSGLR NILPITTAKV PIVKFFHLRS GLEVDISLYN TLALHNTRLL
SAYSAIDPRV KYLCYTMKVF TKMCDIGDAS RGSLSSYAYT LMVLYFLQQR NPPVIPVLQE
IYRGEKKPEI FVDGWNIYFF DQIDELPSYW PEYGKNTESV GQLWLGLLRF YTEEFDFKEH
VISIRRKSLL TTFKKQWTSK YIVIEDPFDL NHNLGAGLSR KMTNFIMKAF INGRRVFGIP
VKGFPKDYPS KMEYFFDPDV LTEGELAPND RCCRICGKIG HFMKDCPMRR KVRRRRDQDD
TLNQRYPENK EKRSKEDKEI QNKYTEREAS TKEDKPAQCT PQKAKPVRAA GDLGRERLLR
PPAEKWKRQD DKDLREKRCF ICGREGHIKK ECPQFKGSAG SLSSKYMTQG KASAKRTQQE
S
//
