ID U3JST8_FICAL Unreviewed; 1626 AA.
AC U3JST8;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 62.
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:ENSFALP00000005842.1};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000005842.1, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000005842.1, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000005842.1}
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 RefSeq; XP_016155677.1; XM_016300191.1.
DR STRING; 59894.ENSFALP00000005842; -.
DR Ensembl; ENSFALT00000005869.2; ENSFALP00000005842.1; ENSFALG00000005607.2.
DR GeneID; 101819427; -.
DR CTD; 23318; -.
DR eggNOG; KOG2277; Eukaryota.
DR GeneTree; ENSGT00940000156988; -.
DR HOGENOM; CLU_003287_0_0_1; -.
DR OMA; HCKAKKL; -.
DR OrthoDB; 170176at2759; -.
DR Proteomes; UP000016665; Chromosome 8.
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; 1.
DR PROSITE; PS50158; ZF_CCHC; 2.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Reference proteome {ECO:0000313|Proteomes:UP000016665};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 1259..1274
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 1302..1318
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 33..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1345..1428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1458..1493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..834
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1465..1493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1626 AA; 183433 MW; F341C0109DA888B7 CRC64;
MEEAKSSKNG NHDPRKSVRL VCEEGKTVKV TINQNYKYNR NDKSVKDLGR SSPSGNSSRK
SKQNDVCSEK QGENKSCKVN SCIPGTKDLG SNVQDRSHGK TKKFSNLSSA MENLKQTKAQ
PVGENAPGSH VAGNGVSMES LAATQKGKLV LENPVGVHTL KTSVDQAGDP GKTAADQRKM
EHKPDDFSKI KNSESAKEHT LEADYLENTG VIDESNLTVE QQLGLKQAEE RLERDYISRL
EKRSPEYTNC QYLCKLCLVH IENIQGAHKH IKEKRHKKNI MEKQEENELR ALPPPSSAQL
AALSFTLIEA ANEQGISDED FRIRQEIVNE MEKIIQQPLP DCSLRMYGSC LTRFAFKTSD
VNIDIKFPPK MSQPDVLIQV LEILKNSAVY SDVESDFHAK VPVVFCKDVK SGLTCKVSAR
NDVACLTTDL LAALGKLEPV LIPLVLAFRY WARLCHIDCQ AEGGIPSYSF ALMVIFFLQQ
RKPRILPSYL GNWIEGFDSK RPDDHQLKGV EDEEFVRWEY KPPTNGAAKN SVGAESKAKV
EQQKGGGKKA TSSEVDNQSN AKEKHGISLL AFKTPHQVSL GQLWLELLKF YTLEFALEEY
VISIRVQELL TRENKNWPKR RIAIEDPFAL KRNVARSLNS QMVFEYILER FRTAYKYFAC
PQSKDGIKSK PDTKKKEKGK INNKKSTRSE EPVANCCLPQ EENVVDKEVT GSGCNIPENE
VECNQVEEAV AKRCTSHDTD SVLLSTLDSS YEEDREEALS LIPNECCELK EESPKERDDL
EISVCLTEGE LSHHCNCSAH QPEDTNSSTE FSDAESRQSL VTESSPQTTF TGTPATSASC
KAVLETQDLK EEGRLSTEEM HYVFDKFIFT SGKPPTIVCS ICKRDGHSKN DCPEDFKKID
LKPLPPMTDR FREILDIVCK RCFDELSPPL SEQQNREQIL ASLERFIRKE YNDKARLCLF
GSSKNGFGFR DSDLDICMTL EGHENAEKLN CKEIIEGLAK VLKKHPGLRN ILPITTAKVP
IVKFEHRRSG LEGDISLYNT LAQHNTRMLA TYAAIDPRVQ YLGYTMKVFA KRCDIGDASR
GSLSSYAYIL MVLYFLQQRN PPVIPVLQEI FDGKQIPQRM VDGWNAFFFD DMEELKKRLP
SLGKNTESLG ELWLGLLRFY TEEFDFKEYV ISIRQKKLLT TFEKQWTSKC IAIEDPFDLN
HNLGAGVSRK MTNFIMKAFI NGRKLFGTPF YPAVGREAEY FFDSKVLTDG ELAPNDRCCR
VCGKIGHYMK DCPKRRRLKK KENEKDDEKE VKEDDRETRE KRCFICGDVG HVRRDCPEFK
QTRQRNNSVP GTQLVRSMVN SQLVAVGQQQ VERPLRTRQS SECSDSHQSS YSPQPQQFPQ
NSSQPASINQ TQPQSISQSK HVPQPQQGAQ PPHQVQLPLF NFPQSPPGQY STLHNLGLLQ
MHHHHQIQLP NTSWPIHGPV IHSAPSNPPH STNVPFSMRS GSSSTTNNQS SVSLNDPSII
FAQPAARPMG IPSTSHEGHW HNPVTPNSLV NNGTVGNSDQ GFQGQFGKMN PPSVPWDHGT
PTHFPLLRGA WPYNMPQNYM QQGNASYPPN KPFYPQAGPL MQSNQRFSLL SQGHPHLNLN
YIQQKK
//
