ID   A0A150GJ74_GONPE        Unreviewed;       418 AA.
AC   A0A150GJ74;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Polymerase nucleotidyl transferase domain-containing protein {ECO:0000259|Pfam:PF01909};
GN   ORFNames=GPECTOR_19g314 {ECO:0000313|EMBL:KXZ49863.1};
OS   Gonium pectorale (Green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Volvocaceae; Gonium.
OX   NCBI_TaxID=33097 {ECO:0000313|EMBL:KXZ49863.1, ECO:0000313|Proteomes:UP000075714};
RN   [1] {ECO:0000313|Proteomes:UP000075714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2863 {ECO:0000313|Proteomes:UP000075714};
RX   PubMed=27102219; DOI=10.1038/ncomms11370;
RA   Hanschen E.R., Marriage T.N., Ferris P.J., Hamaji T., Toyoda A.,
RA   Fujiyama A., Neme R., Noguchi H., Minakuchi Y., Suzuki M.,
RA   Kawai-Toyooka H., Smith D.R., Sparks H., Anderson J., Bakaric R., Luria V.,
RA   Karger A., Kirschner M.W., Durand P.M., Michod R.E., Nozaki H., Olson B.J.;
RT   "The Gonium pectorale genome demonstrates co-option of cell cycle
RT   regulation during the evolution of multicellularity.";
RL   Nat. Commun. 7:11370-11370(2016).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXZ49863.1}.
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DR   EMBL; LSYV01000020; KXZ49863.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150GJ74; -.
DR   OrthoDB; 323993at2759; -.
DR   Proteomes; UP000075714; Unassembled WGS sequence.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR   Pfam; PF01909; NTP_transf_2; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000075714}.
FT   DOMAIN          69..123
FT                   /note="Polymerase nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01909"
FT   REGION          144..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          379..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..162
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..418
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   418 AA;  44987 MW;  93A635E3AA4441AB CRC64;
     MDDALAAADA RGAGSGCTCP CYCGRRIPAR CSHTWKSCLP RAWLAENVER VINKALAQWR
     TSIGGDWAAQ VLVDGSIFKG TALEGSDVDL VVRTAFPVPR RLKHKLHRII RASLSAHFRA
     ADQVWGVKLL PRRKSAELEL EVALELEEEE EAEEEAEEER EEGDGTGREA PVRRPAAAAG
     GGDEDARFEV LCEPPASAAG CGSPHPKLVR LSADLLFERG TVGEPLSRIV NPFAGLDSAR
     LAVMALKLFQ KQAGSLSGPS NFVKEAMVVH VVTDCELRLP SWDTSGERPP PPTESAMQAF
     YMALSLFLAA DSAEHLDARV RPHCVVAAGC LFDRGPFAIW HNRVFRALGE LRVLMEELAA
     SGPAADQETA VQGLRRIFEG RKPPAGGDTV DPGCLPETAG HEQQQADQVQ APAAISAT
//