ID A0A091G6Y5_9AVES Unreviewed; 1589 AA.
AC A0A091G6Y5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=RNA uridylyltransferase {ECO:0000256|ARBA:ARBA00012472};
DE EC=2.7.7.52 {ECO:0000256|ARBA:ARBA00012472};
DE Flags: Fragment;
GN ORFNames=N303_03841 {ECO:0000313|EMBL:KFO76904.1};
OS Cuculus canorus (common cuckoo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO76904.1, ECO:0000313|Proteomes:UP000053760};
RN [1] {ECO:0000313|EMBL:KFO76904.1, ECO:0000313|Proteomes:UP000053760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO76904.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL447760; KFO76904.1; -; Genomic_DNA.
DR STRING; 55661.A0A091G6Y5; -.
DR Proteomes; UP000053760; Unassembled WGS sequence.
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 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 Nucleotidyltransferase {ECO:0000313|EMBL:KFO76904.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053760};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KFO76904.1};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 1254..1269
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 1297..1313
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1340..1423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1453..1488
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 48..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..683
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..830
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1460..1488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1589
FT /evidence="ECO:0000313|EMBL:KFO76904.1"
SQ SEQUENCE 1589 AA; 178953 MW; 862E15B360A61133 CRC64;
MEEAKSSKNG NHDPRKSVRL VCEEGKAVKV TNNQNYKHNR NDKSVKDVGR SSPSGNSSKK
SKQNDGFSEK QGDNKSCKVN SCIPGIKDAG SNGQDRSHGK AKKFSNVSAA VESLKQTKAQ
PVGENFPGSH VSGNGVSTES LTATQKGKLV LENPLGVHAL KTGVVQTGDP GKTASDQRKM
EHKPEDFNKI KNSESNKEHA LDATYLENTA VIDESNLTSE QQLGLKQAEE QDYITRLEKR
SPEYTNCQYL CKLCLVHIEN IQGAHKHIKE KRHKKNIMEK QEENELRALP PPSSAQLAAL
SFTLIEAANE QGISDDDFRI RQEIVSEMEK IIQQPLPDCS LRMYGSCLTR FAFKTSDVNI
DIKFPPKMSQ PDVLIQVLEI LKNSAVYSDV ESDFHAKVPV VFCKDVKSGL TCKVSARNDV
ACLTTDLLAA LGKLEPVLIP LVLAFRYWAR LCHIDCQAEG GIPSYSFALM VIFFLQQRKP
RILPSYLGNW IEGFDSKRPD DHQLKGIEEE FVRWEYKPPT NGAAKNSVGV ENKTKVEQQK
GGGKKVTSSE VDNQNNAKEK HGNSLLAFRT PHQVSLGQLW LELLKFYTLE FALEEYVISI
RVQELLTRES KNWPKRRIAI EDPFALKRNV ARSLNSQMVF EYILERFRTA YKYFACPQSK
DGIKAKPDTK KKEKGKMNNK KSTRSEEPVA NCCLPQGEKV VDKQNIGSGC NITENELECN
EAVEAVAKRC TSKNVDSLLL STLDSSYDED KEEALSRISN ECCELKQKSL KEKDELEISV
CVTEGELSHH DNCSEHQPDD MNSSNESTDA ESRQSLVTES SPKKCTGTPA TSPNCKAMVE
TPVLKDEGRL STEEMHYVFD KFILTSGKPP TIVCSICKRD GHSKNDCPED FKKIDLKPLP
PMTDRFREIL DIVCKRCFDE LSPPLSEQQN REQILASLER FIRKEYNDKA RLCLFGSSKN
GFGFRDSDLD ICMTLEGHEN AEKLNCKEII EGLAKVLKKH PGLRNILPIT TAKVPIVKFE
HRRSGLEGDI SLYNTLAQHN TRMLATYAAI DPRVQYLGYT MKVFAKRCDI GDASRGSLSS
YAYILMVLYF LQQRNPPVIP VLQEIFDGKQ IPQRMVDGWN AFFFDDMEEL KKRLPSLGKN
TESLGELWLG LLRFYTEEFD FKEYVISIRQ KKLLTTFEKQ WTSKCIAIED PFDLNHNLGA
GVSRKMTNFI MKAFINGRKL FGTPFYPAVG REAEYFFDSK VLTDGELAPN DRCCRVCGKI
GHYMKDCPKR RRLKKKDNEK DDEKEVKEDD RETREKRCFI CGDVGHVRRD CPEFKQTRQR
NNSVPGTQLV RSMVNSQLVA VSQQPVERPL RTRQSSECSD SHQSSYSPQP QQFTQNSSQP
ASINQTQPQP ISQSKHVPQP QQGAQPPHQV QLPLFNFPQS PPGQYSTLHN LGLLQMHHHH
QIQLPNTSWP IHGPVIHSAP SNPPHSTNVP FSMRSGSSST TNNQSSVSLN DPSIIFAQPA
ARPMGIPSTS HEGHWHNPVT PNSLVNNGTV GNSGQFGKMN PPSVPWDHGT PTHFPLLRGA
WPYNMPQNYM QQGNASYPPN KPFYPQGTR
//
