ID A0A3P8ZAN6_ESOLU Unreviewed; 1523 AA.
AC A0A3P8ZAN6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=RNA uridylyltransferase {ECO:0000256|ARBA:ARBA00012472};
DE EC=2.7.7.52 {ECO:0000256|ARBA:ARBA00012472};
GN Name=TUT4 {ECO:0000313|Ensembl:ENSELUP00000025513.1};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000025513.1, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000025513.1, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000025513.1}
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 Ensembl; ENSELUT00000037213.2; ENSELUP00000025513.1; ENSELUG00000024167.2.
DR GeneTree; ENSGT00940000156988; -.
DR Proteomes; UP000265140; LG08.
DR Bgee; ENSELUG00000024167; Expressed in spleen and 15 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; IPR043519; NT_sf.
DR InterPro; IPR002058; PAP_assoc.
DR InterPro; IPR002934; Polymerase_NTP_transf_dom.
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:SF49; TERMINAL URIDYLYLTRANSFERASE 4; 1.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF03828; PAP_assoc; 2.
DR Pfam; PF19088; TUTase; 1.
DR Pfam; PF00098; zf-CCHC; 2.
DR SMART; SM00343; ZnF_C2HC; 3.
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; 2.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Reference proteome {ECO:0000313|Proteomes:UP000265140};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 1131..1146
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 1180..1197
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 1..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1147..1178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1220..1388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..754
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1257..1301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1352..1366
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1523 AA; 168566 MW; BCA01076687AE81B CRC64;
MEGTTSPVKS VKPSRCEARA KASSSASSSP LKEASGQRDS PGPKLAMACQ TKENTTTRED
DKTQGSKRGT GASRASTNGP QDPGKVKPRR LTGRTSSGER VKGKVGLGGQ LQQGGDSKPS
LATECNPGGG GTGVATVASS SEECLTPQTK PGPVKKSPGD MAGALVGPKQ PAVEVTGVGS
GVTETGQGGN MTSEQKLGLR QAEERLYRDY IHRLIKQSPD YPNYQYLCKL CSVHIENVQG
AHKHIKEKRH KKNIMEKQEE NELRALPAPS AAQIRAVDAA VIHVAQQHGI SDLEFLVRQE
VVTKMEAIIQ QHLSVCSLRL YGSCLTRFAF KTSDINIDVT YPSTMTQPDV LIQVLEILKN
STQFSEVESD FHAKVPVVFC RDVNSGLMCK VSAGNDVACL TTNHLAALAR LEPRLVPLVL
AFRLWAKLCH IDCQAEGGIP SYSFSLMVIF FLQQRREPIL PVYFGYWIEG FDVKHVDEYH
LTGIEMDIFV GWEHRAPSTE GRGDGRGEGG KAKPVQKKPV VKNRHTEGMT RLALDLGKGV
SLGQLWLELL RFYTLEFALE EHIISIRLKE LLSREMKNWP RRRLAIEDPF ALKRNVARSL
NSQMVFEYIQ ERFRTAYKYF ACPQSADRIP GGCQRAKKTA KHGGRKQVEG LSEKGADVEI
KINCLNVLRS ATRYDEEGDG GGDEELEADP SLEERALNSG LTDLVLSEGG SSTDGSGPEP
GDVKHSSASH LIQNGLLDSD EEEEEEEEEE EEKQGHIAPE DLHYVFDSMI FTGGKPPTVV
CSICKRDGHL KDECPEDFKK IELKPLPPMT DRFCAILDGL CRLCYQELSP SVGEQQKREQ
ILAILERFIR KEYNDKAQLC LFGSSKNGFG FRDSDLDICM TLEGHDTAEK LNCKEIIEGL
AKVLKKHTGL RNILPITTAK VPIVKFEHRQ SGLEADISLY NTLAQHNTRM LATYAALDSR
VQFLGYTMKQ REPPVIPVLQ EIFDGQTAPQ RMVDGWNAFF FDDIEELRRR LPQQQCNSES
VGELWLGLLR FYTEEFDFKE HVISIRQRKR LTTFEKQWTS KCIAIEDPFD LNHNLGAGVS
RKMTNFIMKA FINGRKLFGT PFYPQPGMEA SYFFDPKVLT DGELAPNDRC CRICGKIGHY
MKDCPKRRRY TGRDHQGMKK KENEKEEDVK EGEEHEPRER RCFQCGDMGH VRRDCPEYRH
VRQRVSAGPV PHMVRAMVSS QSIPIPPPPQ DRPGRTRQPS ECSDSRQTPP YSPQPAPFSQ
VSSQSSSSPQ SSSSKTSTGG GAPKQTQHPQ VPLSLFSFPP SHSHPGQYHH PGALTALGLL
PSHPSKHQHQ SHHQHHPSTS WPIHGPVLQT PNSPGGPSPP GLKFPLRQAP GPGNGNAGPG
GSPVGGAPMN LNDPSIIFAQ PAGRPIGLGG GPGRDGHWHN HLPQQGALVA NGTVGKSDPA
YQTQFGGVSQ QGSRTWEHGN AANYSLSPSW PYRMPQNFIQ QGNGGYPQPG KPFMSQGSVV
HPNQHFLTHG RHHVNLNYIQ QKK
//
