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Database: UniProt
Entry: A0A165MHA8_9AGAM
LinkDB: A0A165MHA8_9AGAM
Original site: A0A165MHA8_9AGAM 
ID   A0A165MHA8_9AGAM        Unreviewed;       776 AA.
AC   A0A165MHA8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=DNA ligase/mRNA capping enzyme {ECO:0000313|EMBL:KZT18333.1};
GN   ORFNames=NEOLEDRAFT_1184374 {ECO:0000313|EMBL:KZT18333.1};
OS   Neolentinus lepideus HHB14362 ss-1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Gloeophyllales; Gloeophyllaceae; Neolentinus.
OX   NCBI_TaxID=1314782 {ECO:0000313|EMBL:KZT18333.1, ECO:0000313|Proteomes:UP000076761};
RN   [1] {ECO:0000313|EMBL:KZT18333.1, ECO:0000313|Proteomes:UP000076761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB14362 ss-1 {ECO:0000313|EMBL:KZT18333.1,
RC   ECO:0000313|Proteomes:UP000076761};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|ARBA:ARBA00007572}.
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DR   EMBL; KV425689; KZT18333.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165MHA8; -.
DR   STRING; 1314782.A0A165MHA8; -.
DR   InParanoid; A0A165MHA8; -.
DR   OrthoDB; 2788069at2759; -.
DR   Proteomes; UP000076761; Unassembled WGS sequence.
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:InterPro.
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   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR   InterPro; IPR012308; DNA_ligase_ATP-dep_N.
DR   InterPro; IPR036599; DNA_ligase_N_sf.
DR   InterPro; IPR029710; LIG4.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   PANTHER; PTHR45997:SF2; ATP DEPENDENT DNA LIGASE DOMAIN PROTEIN (AFU_ORTHOLOGUE AFUA_5G02430); 1.
DR   PANTHER; PTHR45997; DNA LIGASE 4; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF04675; DNA_ligase_A_N; 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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KZT18333.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076761}.
FT   DOMAIN          421..571
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          743..776
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        743..760
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   776 AA;  87241 MW;  3136B4F2E6ED3820 CRC64;
     MASFDLSLSS FTSLLENISH VAPRRTRSYS RGTHPQPVVE IFRHWVAQLK AGHGHVPAGA
     TSVVFRLLFP EEDVCRKYEL QETKLAQYLV KIFASAPTSA KQRLIHWNSE SSKGCLGIVV
     KDTQDEDAVP QPTLKDLDAL LSELASTSAY SARSNRSNQP KSRRRPRFEI LSSIYSRLTP
     SAASFITQII LKDLRPVLYT ITETHFTAAL KEYKSNAVTM LTKDDAMKIW DPSGVMWRAY
     KSTNSFEDAS MALESSLPPD LCKLQVGVPI QIPKCRKAQS CLHALQQFRS TDRVWAETKY
     DGERAQIHVQ VLNDGVPKIT IYSKSRRDST LDRIAVHPIV LRVLGFDNLT HSDNSNPTRR
     RCHSKIWKNI VLEAEMVAFS EELNKIDEFY HIRDLIEFTA QGVRGSRRFT AMAADNDSQT
     SASSPRHLAL VFFDLLLLNS VSLLSTPYAT RRALLESIIL PEPGYAMLAD RFLIGEVWEG
     GENGEGEEAR GQLREVFAQA LVRREEGLVL KAEKGWYGGW SPWVKLKKDY IPGHGDAVDL
     VLLAARWDKD RGRELRVAPG TYTTFYLGAL KNSAECKINS STKPDFQVLA EASYGLSREQ
     LEQLNFMIRS AESFVYGSHS PDQLTYTVSG MGCFPKPEVI LEVPLVVEVF GAGFTKERSS
     KYYALRFPRL TKVFRRAERT WADATPLGEY QSIALAAVGK DRPDKDVEDW CKGLWGHEAS
     PGVSCPVKRK REVEGWRERL MEADEGRAGK RRKTGDQEKR LALKPLASIT NTKGGD
//
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