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Database: UniProt
Entry: G3J9H1_CORMM
LinkDB: G3J9H1_CORMM
Original site: G3J9H1_CORMM 
ID   G3J9H1_CORMM            Unreviewed;      1019 AA.
AC   G3J9H1;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=ATP dependent DNA ligase domain protein {ECO:0000313|EMBL:EGX94948.1};
GN   ORFNames=CCM_03220 {ECO:0000313|EMBL:EGX94948.1};
OS   Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX   NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX94948.1, ECO:0000313|Proteomes:UP000001610};
RN   [1] {ECO:0000313|EMBL:EGX94948.1, ECO:0000313|Proteomes:UP000001610}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM01 {ECO:0000313|EMBL:EGX94948.1,
RC   ECO:0000313|Proteomes:UP000001610};
RX   PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA   Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA   Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT   "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT   valued traditional Chinese medicine.";
RL   Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(2011).
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|ARBA:ARBA00007572}.
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DR   EMBL; JH126400; EGX94948.1; -; Genomic_DNA.
DR   RefSeq; XP_006668434.1; XM_006668371.1.
DR   AlphaFoldDB; G3J9H1; -.
DR   STRING; 983644.G3J9H1; -.
DR   GeneID; 18165246; -.
DR   KEGG; cmt:CCM_03220; -.
DR   VEuPathDB; FungiDB:CCM_03220; -.
DR   eggNOG; KOG0966; Eukaryota.
DR   HOGENOM; CLU_004299_4_0_1; -.
DR   InParanoid; G3J9H1; -.
DR   OMA; RIDEFWR; -.
DR   OrthoDB; 2788069at2759; -.
DR   Proteomes; UP000001610; 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   CDD; cd08039; Adenylation_DNA_ligase_Fungal; 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; IPR012310; DNA_ligase_ATP-dep_cent.
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   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:EGX94948.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001610}.
FT   DOMAIN          388..548
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          686..722
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          745..874
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        775..820
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        848..862
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1019 AA;  113098 MW;  DE93E40D73DFC47B CRC64;
     MPLPFSAVCD LLEQSSQLCQ QRKSNAAAVL AWFRRHRAAV DAHDADLAAL LSTLLPEKRT
     DRVYCLQVPT LERIVGRALM LGASRMLELA TYKRPGAGVD FADCVERILS VTPNPIQESG
     HQVTVEQVDE LLHSLAARIR WSAPAIRQSS ACMSHQSRGD LDAMYRRLSA RDAKWFTRLV
     LKDYQPLFFD AHLLYRACDP VLPCLLQIRD DFTEALGAIP IARGALLPIA APRDSRPLCA
     RRVLAAVKPK LGVKVGRQQW HKGRSIKHCM SMGSGRMSVE TKLDGEYCQI HVDMSKPKKR
     VQIFSKSGKD STEDREKVIP AIERALRLNT TECVFKKACI LEGELLVYND LEKTIMPFHK
     IRGHVTRRGR YFNTEQDSQP KPYEHLMIVY YDIFLLDDQG LMDVQHSERL KLLEKVIHYE
     RGVAELVPRE TIDFGHSLAA STLRKAFAKV VVERGEGLVL KPDEPYIVIG PNGRTAPCRC
     IKMKKEYIGA FGDVGDFALV GAGFHAAKAK TYRIPNLKWT HFYVGCLNNK EQVKRWGHKP
     DFTVVCAVEL SEALLQSFLA LGELSAVSRA ANVATTLTVP PGIQCPANLT VAFTNPMVVD
     LRCFSFDKPG NTGGLWTPRF PAVTKIHADR DYADVLTLDE LQALAKEAVE KPVLEDSQEN
     LHWIARLEGA DPRGVAVDAV SQATATTMPT PSPANMTPST ASDSQSSKGA TEPSRRSQSL
     ASAPVVNEVK GWRDASVSII SIPTTSTAEA VSPTKAAMQA PAKRVPEMAS PEQSLKRPRT
     ASFRNTSPRK PLGNIDVNVS YSDSQSTNSQ DSQATVKRGP PRAQTVQRDV IEIPSSDAED
     DDLQQPPSQE RHPQAVSHPP ASSQEEKDSK DQHWSCKHVG EKCGFVGKTM LLASPALLRV
     AELTTLFGDH GVDVQRVLPC VETWWRSAGL RTAGAAVPQQ QKGCVVLLVD SVQQATETKA
     LVARLNAARR QARREERDWI TVYDWRVLRH LSIAEDASVT KKYYDGFQDP WRRWYCGLV
//
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