ID F1S6H9_PIG Unreviewed; 1647 AA.
AC F1S6H9;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 4.
DT 27-MAR-2024, entry version 78.
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:ENSSSCP00000004175.5,
GN ECO:0000313|VGNC:VGNC:94593};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000004175.5, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000004175.5, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000004175.5,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000004175.5}
RP IDENTIFICATION.
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 STRING; 9823.ENSSSCP00000004175; -.
DR PaxDb; 9823-ENSSSCP00000004175; -.
DR Ensembl; ENSSSCT00000004271.5; ENSSSCP00000004175.5; ENSSSCG00000003859.5.
DR VGNC; VGNC:94593; TUT4.
DR eggNOG; KOG2277; Eukaryota.
DR GeneTree; ENSGT00940000156988; -.
DR HOGENOM; CLU_003287_0_0_1; -.
DR InParanoid; F1S6H9; -.
DR TreeFam; TF315661; -.
DR Proteomes; UP000008227; Chromosome 6.
DR Bgee; ENSSSCG00000003859; Expressed in mesenteric lymph node and 43 other cell types or tissues.
DR ExpressionAtlas; F1S6H9; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0050265; F:RNA uridylyltransferase activity; IBA:GO_Central.
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; 3.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 917..932
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 1297..1312
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 1361..1377
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 39..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1324..1344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1402..1469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..620
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1647 AA; 185325 MW; 7EFA3FA9A360587B CRC64;
MEESKTSKNE NHEPKKNAWA FSEESKAVKV ITNQTLKARN DKSIKEIGTN SPNKNTSKKN
KQNDICIEKT EVKSCKVNAA SVPGPKDLGL VLRDQSHCKA KKSPSSPVKA EKLPVSQAKV
ERAPILQAKA EKSPKSPNSR KAEKAPGSQM KSEKVPSLPT EAEKVPGLLL KENMGQTELQ
KIGKKIPSPI TSLDKVNIGV AEGVKSALEN SQPPQKQQTC TDNTGDSDDS ASGTEDISDD
LSKTKNDESN KENSSEMDYL ENATVIDEST LTPEQRLGLK QAEERLERDH IFRLEKRSPE
YTNCRYLCKL CLIHIENIQG AHKHIKEKRH KKNILEKQEE SELRSLPPPS PAHLAALSVA
VIELAKEQGI TDDDLRVRQE IVEEMSKVVT AFLPECSLRL YGSSLTKFAL KSSDVNIDIK
FPPKMNHPDL LIQVLGILKK SVLYLDVESD FHAKVPVVVC RDRKSGLLCR VSAGNDMACL
TTDLLAALGK MEPVFIPLVL AFRYWAKLCY IDSQTDGGIP SYCFALMVMF FLQQRKHPLL
PCLLGSWIEG FDPKRMDDFQ LKGIVEEKFV KWEYNSSSAT EKNSIAEENK AKADQPKDDT
KKTETDNQSN AMKEKHGKSP LTLETPNQVS LGQLWLELLK FYTLDFALEE YVICVRIQDI
LTRENKNWPK RRIAIEDPFS VKRNVARSLN SQLVYEYVVE RFRAAYRYFA CPQRKGGNKS
SVDSMKKEKG KISNKKPMKS DHMASACCIL LGESTEKINA EGGQPGKYDE VECTSQRCIT
EDDNLLINEL DLSEHGQESS PLSTNEGSEL APKSIKKQDV LAPSETCLKK ECSQCNCVVY
KSPEPDESAG TDCRSDLERE SSHTCYTCTD TSTTSCNCKA TEDASDLNDD DSHPTQELYY
VFDKFILTSG KPPTIVCSIC KKDGHSKNDC PEDFRKIDLK PLPPMTNRFR EILDLVCKRC
FDELSPPFSE QHNREQILIG LEKFIQKEYD EKARLCLFGS SKNGFGFRDS DLDICMTLEG
HENAEKLNCK EIIENLAKIL KRHPGLRNIL PITTAKVPIV KFEHRRSGLE GDISLYNTLA
QHNTRMLATY AAIDPRVQYL GYTMKVFAKR CDIGDASRGS LSSYAYILMV LYFLQQRKPP
VIPVLQEIFD GKQIPQRMVD GWNAFFFDKT EELKKRLPSL GKNTETLGEL WLGLLRFYTE
EFDFKEYVIS IRQKKLLTTF EKQWTSKCIA IEDPFDLNHN LGAGVSRKMT NFIMKAFING
RKLFGTPFYP LIGREAEYFF DSRVLTDGEL APNDRCCRVC GKIGHYMKDC PKRRSSLLFR
LKKKDSEEEK EGNEEEKDSR DLVDPRDLHD TRDFRDPRDL RCFICGDAGH VRRECPEVKL
ARQRNSSVAA AQLVRNLVNA QQVAGSSQQQ GDQSIRTRQS SECSDSPSYS PQPQPFPQNS
SQSTAITQAP SQPGSQPKLG PPQQGAQPPH QVQMPMYNFP QSPPTQYSPM HNMGLLPMHP
LQIPAPSWPI HGPVIHSAPG SAPSNIGLND PSIIFAQPAA RPVAIPSSSH DGHWPRTVAP
NSLVNNGTVG NSEPGFPGLN PPIPWEHAPR PHFPLVPASW PYGLHQNFMH QGNARFQHNK
PFYTQDRCAA RRCRERCPHP PRGNVSE
//
