ID A0A452F1Q2_CAPHI Unreviewed; 1488 AA.
AC A0A452F1Q2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
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:ENSCHIP00000018209.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000018209.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000018209.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000018209.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 EMBL; LWLT01000007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSCHIT00000026024.1; ENSCHIP00000018209.1; ENSCHIG00000017690.1.
DR GeneTree; ENSGT00940000156859; -.
DR Proteomes; UP000291000; Chromosome 8.
DR Bgee; ENSCHIG00000017690; Expressed in spleen and 17 other cell types or tissues.
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; 3.
DR PROSITE; PS50158; ZF_CCHC; 3.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Reference proteome {ECO:0000313|Proteomes:UP000291000};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 960..975
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 1342..1356
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 1447..1463
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1361..1422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..764
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..838
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1361..1403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1488 AA; 169783 MW; 958DE2F2B198A35E CRC64;
MGDATKPYFV RRPKERGTTD DEDFRRGHPQ QDYLIMDDYA KGHSSKMEKG LPKKKVTPGN
YGNTPRKGPY AVSNNPYAFK NPIYSQPTWI NDNHKDQSKR WLSDELASNS DSWREYKPGP
RIPVINRPRR DSFQESEDGY RWQDGRGCRT VRRLFHKELT NLDIMSEMEA GSPENKKPRS
RPRKPRRTRN DENEQDGDLE GPVIDESVLS TKELLGLQQA EERLKRDCID RLKRRPRNYP
TAKYTCKLCD VLIESIAFAH KHIKEKRHKK NIKEKQEEEL LTTLPPPTPS QINAIGIAID
KVVQEFGLHN ENLEQRLEIK RIMENVFQHK LPDCSLRLYG SSCSRLGFKN SDINIDIQFP
AIMSQPDVLL LVQECLKNND SFIDVDADFH ARVPVVVCRE KQSGLLCKVS AGNENACLTT
NHLTALGKLE SKLVPLVIAF RYWAKLCSID RPEEGGLPPY VFALMAIFFL QQRKEPLLPV
YLGSWIEGFS LSKLGNFNLK EIEKDSVVWE YTDNVAGDVD SAKEEAPKEM AVKRGQVSLI
FDSKQQPSVP VGQLWVELLR FYALEFNLAD LVISIRVKES ISRESKDWPK KRIAIEDPYS
VKRNVARTLN NQPVFEYILH CLRTTYKYFA LPHKVTKSSF PKPLSTVSCT SECSKEIAKH
DPEVQAKGDK LKNSVLAQGS GAASSTANTC KAQPLTLKET AKNFENPSAE KMGNSHISVH
LENSDCIKAK VSSGDSKDVE VHHQETGSKN KKEKSGKESK HPLTADDQAL SSSKCGALVT
CGSPGNKETD TTLDLEEYDE FPTSYAKADV DEESIEGTSE LGDAVSHFTP SRQSQISGIL
HSDEEEEDEE EEEEPRLSIS RREDEDDIAN GDELDNTFTG SGDEDALSEE DVELDGSAKY
EDLKECGKHH VDGNLLVELN KISLKEESVC EENSTVDQSD FFYEFSKLTF TKGKSPTVVC
SLCKREGHLK KDCPEDFKRI QLEPLPPLTP KFSNILDQVC IQCYKDFSPT VLEDQAREHI
RQNLENFIKQ EFPGTKLSLF GSSKNGFGFK QSDLDVCMTI NGLETAEGLD CVRTIEELAR
VLKKHSGLRN ILPITTAKVP IVKFFHLRSG LEVDISLYNT LALHNTRLLS AYAAIDPRVK
YLCYTMKVFT KMCDIGDASR GSLSSYAYTL MVLYFLQQRT PPVIPVLQEI YKGEKKPEIF
VDGWNIYFFD QIDELPNYWP EYGKNTESVG QLWLGLLRFY TEEFDFKEHV ISIRRKSLLT
TFKKQWTSKY IVIEDPFDLN HNLGAGLSRK MTNFIMKAFI NGRRVFGIPV KGFPKDYPSK
MEYFFDPDVL TEGELAPNDR CCRICGKIGH FMKDCPMRRK VRRRRDQEDT LNQRYPENKD
KRSKEDKEIQ NKYTEREVST KEDKPMQCTP QKAKPVRAAA EPGREKILRP PVEKWKRPED
KDLREKRCFI CGREGHIKKE CPQFKGSSGM DAHHALMFAL TSQGKSLF
//
