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Database: UniProt
Entry: G3GW01_CRIGR
LinkDB: G3GW01_CRIGR
Original site: G3GW01_CRIGR 
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
//
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