ID G3GW01_CRIGR Unreviewed; 1451 AA.
AC G3GW01;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=RNA uridylyltransferase {ECO:0000256|ARBA:ARBA00012472};
DE EC=2.7.7.52 {ECO:0000256|ARBA:ARBA00012472};
GN ORFNames=I79_001907 {ECO:0000313|EMBL:EGV97940.1};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGV97940.1, ECO:0000313|Proteomes:UP000001075};
RN [1] {ECO:0000313|Proteomes:UP000001075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX PubMed=21804562; DOI=10.1038/nbt.1932;
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL Nat. Biotechnol. 29:735-741(2011).
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};
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DR EMBL; JH000045; EGV97940.1; -; Genomic_DNA.
DR STRING; 10029.G3GW01; -.
DR PaxDb; 10029-XP_007648930-1; -.
DR eggNOG; KOG2277; Eukaryota.
DR InParanoid; G3GW01; -.
DR Proteomes; UP000001075; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
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 GO; GO:0031123; P:RNA 3'-end processing; 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 Nucleotidyltransferase {ECO:0000313|EMBL:EGV97940.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001075};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EGV97940.1};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 791..806
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 1171..1186
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 1217..1233
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1188..1209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1260..1341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1416..1451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1189..1209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1260..1285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1286..1313
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1314..1341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1451 AA; 162377 MW; 3E4A8A8805B6C91F CRC64;
MKAQKGSSQA KVEKTPSLQA KAEKLPKSPN LPVKAEKIPC TAAAATTIEK ALNSQKKEEN
IPTSQMKLQK TSSSPLEPEN QPSLLLKESM KQTESQQTGK KLVSSVVSVD KRNSEAPQGV
KSTLENLSPS QKQQTRTDNI GDSDDSASGI EDTSDELSKM KSEESNKENS SEMDYLENAT
VIDESALTPE QRLGLKQAEE RLERDHIFRL EKEKQEESEL RSLPSPSPAH LAALSIAVVE
LAKEQGITDD DLRVRQNIVE EMSKVIMTYL PECSLRLYGS SLTKFALKSS DVNIDIKFPP
KMNHPDLLIQ VLGILKKSTL YVDVESDFHA KVPVVVCKDR KSGLLCRVSA GNDMACLTTD
LLAALGKVEP VFTPLVLAFR YWAKLCYIDS QTDGGIPSYC FALMVMFFLQ QRKPPLLPCL
LGSWIEGFDP KRMDDFQLKG IVEEKFVKWE YNSSSATERN LIADENKAKA DQPKDDTKKT
ETDNQSNAMK EKHGKSPLTL EAPNQVPLGQ LWLELLKFYT LDFALEEYVI CVRIQDILTR
ENKNWPKRRI AIEDPFSVKR NVARSLNSQL VYEYVVERFR AAYRYFACPQ RKGGNKSTVD
FKKKEKGKIS SKKPVKSDCM ATNCCTLGES TEKVNTERGQ PAKCDEMEFT SQRCIVDSDS
LLANELGLAD HGQESSSLST ASEGCELEQK SAEKQGDLTP SETSLKKELS QCNCIGSPDG
AESAGTDCRS NLEMESSHQI VCNSITATSC NCKATEVASD FIDGDNLPSQ ELYYVFDKFI
LTSGKPPTIV CSICKKDGHS KNDCPEDFRK IDLKPLPPMT NRFREILDLV CKRCFDELSP
PCSEQHNREQ ILIGLEKFIQ KEYDEKARLC LFGSSKNGFG FRDSDLDICM TLEGHENAEK
LNCKEIIENL AKILKRHPGL RNILPITTAK VPIVKFEHRR SGLEGDISLY NTLAQHNTRM
LATYAAIDPR VQYLGYTMKV FAKRCDIGDA SRGSLSSYAY ILMVLYFLQQ RKPPVIPVLQ
EIFDGKQIPQ RMVDGWNAFF FDKTEELKKR LPSLGKNTES LGELWLGLLR FYTEEFDFKE
YVISIRQKKL LTTFEKQWTS KCIAIEDPFD LNHNLGAGVS RKMTNFIMKA FINGRKLFGT
PFYPLIGREA EYFFDSRVLT DGELAPNDRC CRVCGKIGHY MKDCPKRKRL KKKDSEEEKE
GNEEEKDSRD LDSRDLRCFI CGDAGHVRRE CPEVKMARQR NSSVAAAQLV RNLVNAQQVA
GSAQQQGDQS IRTRQSSECS DSPSYSPQPQ PFPQNSPQPT AIPQPPSQPG SQPKLGPPQQ
GGQPPHQVQM PLYNFPQSPP AQYSPMHGMG LLPMHPLQIP APSWPIHGPM LHSAPGSTPS
NIGLNDPSII FAQPAARPMA IPSSSHDGHW PRTVAPNSLV NNGAVGNSAD RCATRRCRER
CPHPPRGNVS E
//