ID A0A093HA82_STRCA Unreviewed; 1450 AA.
AC A0A093HA82;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=RNA uridylyltransferase {ECO:0000256|ARBA:ARBA00012472};
DE EC=2.7.7.52 {ECO:0000256|ARBA:ARBA00012472};
DE Flags: Fragment;
GN ORFNames=N308_15789 {ECO:0000313|EMBL:KFV78621.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV78621.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV78621.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV78621.1};
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}.
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DR EMBL; KL206075; KFV78621.1; -; Genomic_DNA.
DR STRING; 441894.ENSSCUP00000012816; -.
DR Proteomes; UP000053584; 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; 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:SF34; TERMINAL URIDYLYLTRANSFERASE 7; 1.
DR Pfam; PF03828; PAP_assoc; 2.
DR Pfam; PF19088; TUTase; 2.
DR Pfam; PF16631; TUTF7_u4; 1.
DR Pfam; PF00098; zf-CCHC; 3.
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; 3.
DR PROSITE; PS50158; ZF_CCHC; 3.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Nucleotidyltransferase {ECO:0000313|EMBL:KFV78621.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053584};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KFV78621.1};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 941..956
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 1323..1337
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 1428..1444
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1347..1415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1347..1383
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1399..1415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1450
FT /evidence="ECO:0000313|EMBL:KFV78621.1"
SQ SEQUENCE 1450 AA; 165927 MW; 216D775119ECC721 CRC64;
MGDAAKPCFA KQSTEQEILH EEELKGNPLQ EDYQVMDDYG NGHSNKIDIS LQKKKGAPAH
YGNSPRRGPR SALSSPNSLK NMSHNQGSKL LDIQKDQVKK WISDDHRGSS DSWREYRSAV
WIPMLNRTRK DSLQEIEAAG NRSVRRQLQK DLTSEDISDM QKGSSEIKKH RKPRRSRRTR
KDEYDQDEEA DGPVIDEAVL SAKELLGLQQ AEERLKRDCI YRLKKRPRSY PSAKYTCKLC
DVLIESVAFA HKHMKEKRHK KSIKEKQEEQ LLTVLPPPTP SQVRAIGVAI ENVVQEFGLN
NEDLEERLKI KTTMENVLHQ KLPESSLRLY GSSCSRFGFK TSDINIDIQF PANMAQPDVL
LLVQESLKNS ESFIEVDADF HARIPVVVCR EKQSGLICKV SAGNENACLT TNHLATLGKL
EPTVVPLVIA FRYWAKLCCV DRPEEGGLSP YVFALMVIFF LQQRKEPFLP VYLGSWIGGF
SLNKLTNFNL KEVENDTVVW EHNPIDDSDS PKETSPKNGK VPLVFDSGHQ CSAPVGQLWV
ELLRFYALEF NLADSVISIR LKETVSRELK DWPKKRIAVE DPYSVKRNVA RTLNSQIVYE
YILHCLRATY KYFALPHKKP TKFSQKSPLH ASEDKSQMLD LEEDAINHEN PELQSLDGKT
NRTTVEDCII ESTGIPQVHR IDPSKLCDGS ESLTEEELAD GLSHLGIAHE DSDCVIEEMI
SGDNEDFKPS CEDTESGNEE EDDEEENEQE RRWNNNFMPT DQGIDEDSES GDLPVTLHEH
DIEVGIMNDN ADLDEESTEG TDELDESPNK FIPSTQNQIS EMINSDGEDD EEEELSLLNC
TKSGDIRRAE GELDNRYTGS GDEDALSEEE EDLSIPIKYE DRHLKENVDG TLRINLGQED
LTERRSAFEE NAATEQCLDS ELAYEFSKPA FTKGKSPTVV CSLCKREGHL KRDCPEDFKK
IELDPLPALT PKFSFILDQV CVQCYQDFAP NIVEDQAREH IRQNLENFIR QDFPGTKLNL
FGSSKNGFGF KQSDLDICMT IDGLETAESL DCIRIIEDLA KVLKKHSGLR NVLPITTAKV
PIVKFFHVRS GLEVDISLYN TLALHNTRLL SSYAAIDPRV KYLCYTMKVF TKMCDIGDAS
RGSLSSYAYT LMVLYFLQQR NPPVIPVLQE IYKEPKKPEI LVDGWNVYFF DKIEELSVVW
PECGKNTESV GQLWLGLLRF YTEEFDFKEH VICIRRRNLL TTFKKQWTSK YIVIEDPFDL
NHNLGAGLSR KMTNFIMKAF INGRRVFGTP IKIFPKEYPS KMEYFFDPEV LTEGELAPND
RCCRICGKIG HFMKDCPMRR KLRRRHDYED IKSQRHAENK EKRSKEDKEI QNKTTERESS
IKEGKLLQCT PQKSKLARGV VETGRDKTPR QSAEKWKRLE DRDLREKRCF ICGREGHIKK
ECPQYKGATG
//
