ID A0A150GP30_GONPE Unreviewed; 338 AA.
AC A0A150GP30;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=DNA ligase ATP-dependent N-terminal domain-containing protein {ECO:0000259|Pfam:PF04675};
GN ORFNames=GPECTOR_12g508 {ECO:0000313|EMBL:KXZ51545.1};
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:KXZ51545.1, 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:KXZ51545.1}.
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DR EMBL; LSYV01000013; KXZ51545.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150GP30; -.
DR STRING; 33097.A0A150GP30; -.
DR OrthoDB; 8251at2759; -.
DR Proteomes; UP000075714; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:InterPro.
DR GO; GO:0051103; P:DNA ligation involved in DNA repair; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3260.10; DNA ligase, ATP-dependent, N-terminal domain; 1.
DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR InterPro; IPR012308; DNA_ligase_ATP-dep_N.
DR InterPro; IPR036599; DNA_ligase_N_sf.
DR InterPro; IPR029710; LIG4.
DR PANTHER; PTHR45997; DNA LIGASE 4; 1.
DR PANTHER; PTHR45997:SF1; DNA LIGASE 4; 1.
DR Pfam; PF04675; DNA_ligase_A_N; 1.
DR SUPFAM; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 1.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000075714}.
FT DOMAIN 20..206
FT /note="DNA ligase ATP-dependent N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04675"
FT REGION 237..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 338 AA; 37329 MW; 086DD40C6CCF6444 CRC64;
MSASQAPGPS GRPGSAAQLS FEDFTKLLDT LVRTPQKGQR KVRVLQRFTD TFLPRRDGND
LFHFYRLLLP SAQVDKERGN YQLKEAKLAA VLAGALGASP GDTERAKQWR GLNVSASGVF
HEVMYEVLLR KYLRADQAAT GPPLTLGEVN ARLDELAARG DSGAQQAVLR GLLLRCSPVA
AKWLVLILLR ELKIGMSPET ILGAYHPDAP DLLNGCMDLR RVLCELIDPR VRVKKKDVVP
GQPAKPQLAD RCEGGPAGAA KRMRGRRFVT EVHRTDQSSF NFFSRRGLDH GSRRDFAVLG
PALEQLLTQE RVILDGEMVV WNKTRWVGWM GGEGEDGP
//