ID V9L675_CALMI Unreviewed; 324 AA.
AC V9L675;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=RNA uridylyltransferase {ECO:0000256|ARBA:ARBA00012472};
DE EC=2.7.7.52 {ECO:0000256|ARBA:ARBA00012472};
DE Flags: Fragment;
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|EMBL:AFP07107.1};
RN [1] {ECO:0000313|EMBL:AFP07107.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Ovary {ECO:0000313|EMBL:AFP07107.1};
RX PubMed=24402279; DOI=10.1038/nature12826;
RG International Elephant Shark Genome Sequencing Consortium;
RA Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA Wilson R.K., Brenner S., Warren W.C.;
RT "Elephant shark genome provides unique insights into gnathostome
RT evolution.";
RL Nature 505:174-179(2014).
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};
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DR EMBL; JW874590; AFP07107.1; -; mRNA.
DR AlphaFoldDB; V9L675; -.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro.
DR CDD; cd05402; NT_PAP_TUTase; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR045100; TUTase_dom.
DR PANTHER; PTHR12271; POLY A POLYMERASE CID PAP -RELATED; 1.
DR PANTHER; PTHR12271:SF40; POLY(A) RNA POLYMERASE GLD2; 1.
DR Pfam; PF19088; TUTase; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
PE 2: Evidence at transcript level;
FT DOMAIN 150..253
FT /note="TUTase nucleotidyltransferase"
FT /evidence="ECO:0000259|Pfam:PF19088"
FT REGION 64..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 324
FT /evidence="ECO:0000313|EMBL:AFP07107.1"
SQ SEQUENCE 324 AA; 36878 MW; AAC5E184FE5BA661 CRC64;
MFPNSPNLGR QPYSPVFFPH QQFINSHNFR NVTFPGTILT GEVSPGPSQV WPFYNAYPVF
TQNLPNSHGR KRRSDERSGP YDVKRQRFQS PQSQPPSSAV PFRADRRHSV PSPGISSLLP
LIDYPQNDLQ VARDKLSQQI LELFHDCQQQ SIDLDKKDLC RAELQREIQR IFPQTKLYLV
GSSLNGFGTR SSDADLCLVL IDKQINQKSE ALHILTLIQQ LFYRLSYIER PQLIRAKVPI
VKFRDKVSGV ECDLNVNNVV GIRNTFLLRT YAYTLPEPVI PSLQKEHPEC FDPTMQLHLV
HQGGSKISPY LSLNSSNLGD LLVG
//
