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Database: UniProt
Entry: G1KHK6_ANOCA
LinkDB: G1KHK6_ANOCA
Original site: G1KHK6_ANOCA 
ID   G1KHK6_ANOCA            Unreviewed;      1530 AA.
AC   G1KHK6;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 3.
DT   27-MAR-2024, entry version 71.
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:ENSACAP00000008110.4};
OS   Anolis carolinensis (Green anole) (American chameleon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Iguania; Dactyloidae; Anolis.
OX   NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000008110.4, ECO:0000313|Proteomes:UP000001646};
RN   [1] {ECO:0000313|Ensembl:ENSACAP00000008110.4, ECO:0000313|Proteomes:UP000001646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000008110.4,
RC   ECO:0000313|Proteomes:UP000001646};
RG   The Genome Sequencing Platform;
RA   Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA   Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACAP00000008110.4}
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; 28377.ENSACAP00000008110; -.
DR   Ensembl; ENSACAT00000008282.4; ENSACAP00000008110.4; ENSACAG00000008282.4.
DR   eggNOG; KOG2277; Eukaryota.
DR   GeneTree; ENSGT00940000156988; -.
DR   HOGENOM; CLU_003287_0_0_1; -.
DR   InParanoid; G1KHK6; -.
DR   OrthoDB; 170176at2759; -.
DR   TreeFam; TF315661; -.
DR   Proteomes; UP000001646; Chromosome 4.
DR   Bgee; ENSACAG00000008282; Expressed in embryonic post-anal tail and 13 other cell types or tissues.
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; 1.
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; 2.
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:UP000001646};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT   DOMAIN          1211..1226
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   DOMAIN          1254..1270
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   REGION          1..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          486..530
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          626..659
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1294..1357
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..143
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..175
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        627..645
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1530 AA;  172369 MW;  FE0B0BDE94533453 CRC64;
     MEEGKSSKSG NHDTRKSVHT ACEKSKAVRV ATNPVYKTNK NDRSGKSSSS GSSLKKNKQN
     AVSPEKSGEN KSCKTDSCTP GCTKMGSSVQ DQSRSKAERL LNVSETTVNL HQLKNQHTDQ
     NPPSSYVSEN GAITETLPIA QRESSELKNL PGEDISKINR SGDSGKSNTK PPDSSKETNS
     EAKCLENVAV TGESTLIAEQ ELGLKQAEER LERDYIIRLE KRSPEYANCQ YLCKLCLVHI
     ENIQGAHKHI KEKRHKKNIM EKQEENELRA LPPPSPAQVA ALSFMLMEAA KEQGISDDDF
     KIRQDIVRDM EKIIQQHLPE CTLRMYGSCL TRFAFKTNIS CYQTEVFYIS CYSDVESDFH
     AKVPVIFCKD NKSGLTCKVS AGNDVACLTT DLLAALGKLE PVLVPLVLAF RYWARLCHID
     CQAEGGIPSY SFALMVIFFL QQREPRILPS YLGSWIEGFD SKKADDYQLK RIKDEKFVVW
     EYKPSNSGGK NVSAAEGKAK GEQHSGDKNA SSVETDSQHN AKEKNGSSPL ALEEPHQISL
     GHLWLELLKF YTLEFALEEY VISIRVQELL TRENKTWPKR RIAIEDPFAL KRNVARSLNS
     QMVFEYILER FRTAYKYFAC PQNKDGSKLK SDTRKKEKGK FGSKKPEEPA ANCSLPQQAN
     PAEKQSAGCA DNILECELNE CSEMEPTSRK RTSENSKSLL AKTPEILNTN CDSREETVSL
     IANECCELEH KSLEAKNDQE TTTEENRVFS EHRSFDADFV SELTDTENRQ NSIIEYPQIN
     MCSGTSTSAT SHNCQAVGEI QDTNDEIATE DMHYVFDKFI LTSGKPPTIV CSICKRDGHS
     KNDCPEDFKK IDLKPLPPMT SRFREILDLV CKRCFDELSP PFSEQQNREQ ILASLERFIR
     KEYNDKARLC LFGSSKNGFG FRDSDLDICM TLEGHENAEK LNCKEIIENL AKVLKKHPGL
     RNILPITTAK VPIVKFEHRR SGLEGDISLY NTLAQHNTRM LATYAAIDPR VQYLGYTMKV
     FAKRCDIGDA SRGSLSSYAY ILMVLYFLQQ REPPVIPVLQ EIFDGQQIPQ RMVDGWNAFF
     FDDTEELKKR LPSLGKNTES LGELWLGLLR FYTEEFDFKE YVISIRQKKL LTTFEKQWTS
     KCIAIEDPFD LNHNLGAGVS RKMTNFIMKA LINGRKLFGT PFYPVLGREA EYFFNSKVLT
     DGELAPNDRC CRVCGKIGHY MKDCPKRRRL KKKENEREDE KEVKEEDRDT REKRCFICGD
     VGHVRRDCPE FKQTRQRSNA AQLVRSLVNA QPVTGSIPQQ VERPLRTRQP SECSDSHPSS
     YSPQPQQFTQ NSSPPASINQ TQPQPIAPSN HVLQPQPGTQ VQLPLFNFAQ SPPGQYPNLP
     NLGLFQMHHH QIQLPNTSWP VIHSAPGNPS HSSLSLNDPS IIFAQPAARP VGIPSNSPEG
     HWHNSVTLSS LVNNGTVGNA GQFGKTNPSP AAAAAPWDHG SPAHFPLLRG TWPYSMSPNY
     VQQGNTFPSP LYILLIHCSI LRCKKKLLCS
//
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