ID   G2QJF5_THET4            Unreviewed;       547 AA.
AC   G2QJF5;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=ATP-dependent DNA ligase family profile domain-containing protein {ECO:0000259|PROSITE:PS50160};
GN   ORFNames=MYCTH_2308202 {ECO:0000313|EMBL:AEO59712.1};
OS   Thermothelomyces thermophilus (strain ATCC 42464 / BCRC 31852 / DSM 1799)
OS   (Sporotrichum thermophile).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothelomyces.
OX   NCBI_TaxID=573729 {ECO:0000313|EMBL:AEO59712.1, ECO:0000313|Proteomes:UP000007322};
RN   [1] {ECO:0000313|EMBL:AEO59712.1, ECO:0000313|Proteomes:UP000007322}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42464 / BCRC 31852 / DSM 1799
RC   {ECO:0000313|Proteomes:UP000007322};
RX   PubMed=21964414; DOI=10.1038/nbt.1976;
RA   Berka R.M., Grigoriev I.V., Otillar R., Salamov A., Grimwood J., Reid I.,
RA   Ishmael N., John T., Darmond C., Moisan M.-C., Henrissat B., Coutinho P.M.,
RA   Lombard V., Natvig D.O., Lindquist E., Schmutz J., Lucas S., Harris P.,
RA   Powlowski J., Bellemare A., Taylor D., Butler G., de Vries R.P.,
RA   Allijn I.E., van den Brink J., Ushinsky S., Storms R., Powell A.J.,
RA   Paulsen I.T., Elbourne L.D.H., Baker S.E., Magnuson J., LaBoissiere S.,
RA   Clutterbuck A.J., Martinez D., Wogulis M., de Leon A.L., Rey M.W.,
RA   Tsang A.;
RT   "Comparative genomic analysis of the thermophilic biomass-degrading fungi
RT   Myceliophthora thermophila and Thielavia terrestris.";
RL   Nat. Biotechnol. 29:922-927(2011).
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|ARBA:ARBA00007572}.
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; CP003006; AEO59712.1; -; Genomic_DNA.
DR   RefSeq; XP_003664957.1; XM_003664909.1.
DR   AlphaFoldDB; G2QJF5; -.
DR   STRING; 573729.G2QJF5; -.
DR   GeneID; 11506907; -.
DR   KEGG; mtm:MYCTH_2308202; -.
DR   VEuPathDB; FungiDB:MYCTH_2308202; -.
DR   eggNOG; KOG0967; Eukaryota.
DR   HOGENOM; CLU_005138_5_0_1; -.
DR   InParanoid; G2QJF5; -.
DR   OMA; IASYSTH; -.
DR   OrthoDB; 961at2759; -.
DR   Proteomes; UP000007322; Chromosome 5.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   CDD; cd07900; Adenylation_DNA_ligase_I_Euk; 1.
DR   CDD; cd07969; OBF_DNA_ligase_I; 1.
DR   Gene3D; 3.30.1490.70; -; 1.
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   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR   InterPro; IPR036599; DNA_ligase_N_sf.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR   PANTHER; PTHR45674:SF9; DNA LIGASE 3; 1.
DR   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   SUPFAM; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007322}.
FT   DOMAIN          192..390
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          282..335
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          520..547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        291..330
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        531..547
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   547 AA;  61194 MW;  7849BEBEE9BACD71 CRC64;
     MLIALSRAFL LSKPPGAEFA TKDPKALAKL KKEELAEIWA RSEELVKASY ARHPDYNDLI
     PVLLEIGISE ELLVRCGLTL HIPLRPMLGN ITRDLSEMLT KLQGRDFTCE YKYDGQRAQV
     HCDSNGKVSI FSRHLELMTD KYPDLVALVP KIRGEGVESF ILEGEVVAVD RATGELKNFQ
     TLTNRARKDV AIGAITIDVC LFAFDLMYLN GQPLLDQPFR HRRDLLRSLF VEIPHHFTWV
     RSLDATSQDS ESVLEFFKSA LDSKCEGIMV KTLDNLPDLE YCGDKEGPEQ TGPELNSSFT
     AKNSGSKSKR RDNGGSSNNN NNNNNNGPPK SRRKPLLATY EPDKRLDSWL KVKKDYSSSS
     DTLDLIPIAA WHGQGRKAKW WSPILLAVRN EETGCLEAVC KCMSGFTDAF YKANREFYDD
     GDEDSGVGRG RRNTHARKPG FVEYAGGVPD VWFEPCEVWE VAFADITVSP TYTAAIGLAK
     EDRGLSLRFP RFLRKREDKG IEEASTSAYL AALWRKQEAR APQAAETAGQ AAEEDELDDE
     EAAAAEE
//