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Database: UniProt
Entry: F0UP51_AJEC8
LinkDB: F0UP51_AJEC8
Original site: F0UP51_AJEC8 
ID   F0UP51_AJEC8            Unreviewed;      1087 AA.
AC   F0UP51;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=ATP-dependent DNA ligase {ECO:0000313|EMBL:EGC46910.1, ECO:0000313|EMBL:QSS53089.1};
GN   ORFNames=HCEG_06125 {ECO:0000313|EMBL:EGC46910.1}, I7I53_00241
GN   {ECO:0000313|EMBL:QSS53089.1};
OS   Ajellomyces capsulatus (strain H88) (Darling's disease fungus) (Histoplasma
OS   capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=544711 {ECO:0000313|Proteomes:UP000008142};
RN   [1] {ECO:0000313|EMBL:EGC46910.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H88 {ECO:0000313|EMBL:EGC46910.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA   Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA   Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA   McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT   "Annotation of Ajellomyces capsulatus strain H88.";
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000008142}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H88 {ECO:0000313|Proteomes:UP000008142};
RA   Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA   Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA   Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA   McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT   "Annotation of Ajellomyces capsulatus strain H88.";
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:QSS53089.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=H88 {ECO:0000313|EMBL:QSS53089.1};
RA   Voorhies M., Cohen S., Shea T.P., Petrus S., Munoz J.F., Poplawski S.,
RA   Goldman W.E., Michael T., Cuomo C.A., Sil A., Beyhan S.;
RT   "Chromosome-level genome assembly of a human fungal pathogen reveals
RT   clustering of transcriptionally co-regulated genes.";
RL   Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|ARBA:ARBA00007572}.
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DR   EMBL; DS990640; EGC46910.1; -; Genomic_DNA.
DR   EMBL; CP069104; QSS53089.1; -; Genomic_DNA.
DR   AlphaFoldDB; F0UP51; -.
DR   STRING; 544711.F0UP51; -.
DR   VEuPathDB; FungiDB:I7I53_00241; -.
DR   HOGENOM; CLU_004299_1_0_1; -.
DR   OMA; LRRHIMR; -.
DR   Proteomes; UP000008142; Unassembled WGS sequence.
DR   Proteomes; UP000663419; Chromosome 3.
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   SUPFAM; SSF50249; Nucleic acid-binding proteins; 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:EGC46910.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008142}.
FT   DOMAIN          393..535
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          724..751
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          829..851
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1052..1071
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        726..747
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        835..851
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1087 AA;  121436 MW;  98D7944F538EC2F9 CRC64;
     MGFKFSYVCD LFTSLENNLT LRASTASRHR NPDVATIANW FSQHGKQIHG GETDRLALLS
     CLFPERRPER VFGLKEPSLV KIIGRCLLLG ISRRQALDSY KICGNGDLGQ CVERVMRQAE
     NDNPEDSGVT VEDIDTVLNH IASRCRFSGP DVRRRRTAAG VDEVLGPILR HLTSCEAKWL
     IRIILKDLSP LTLPARLILQ NFHFLLPDLL LLQDSLGAAV ALLSRDPMKR FPWRPDPDYA
     KLLASFAFSR ISLDVGVKVG RPTFYKARGI KHCCKMAGKR TMSVERKYDG EYCQIHVDLS
     KGSGCIQIFS KSGKNSTMDR VGIHSTVKEC LRIGKVGCKI SRNCILEGEL LVWSDVESKI
     LPFHKLRKHV IRSGSFIGTE NDSPPHSYEH LYIMLFDVLL IDDQACLPKS YRERRALLKE
     ISHPIDGRAG IAEQEYIDFS LPESQEMLTT AFATAISQRW EGLVLKASDE PYFVIEQQEH
     SNFGHWIKLK KDYIAGIGDT ADFALIGARY DAREAAKLQS IKGVQWTSFF VGCRDTGSKY
     PYDARPLFRV VDVLNRHNVN IQLLRTLNQS GRFCSCDVDD EDAPFIIKTD QIQLPKVQVL
     FKTPFVVEMV GSGFEKPAGA NYFTLRFPRV LKIHMDRDVE DATTLEELQV LAEAANSVPK
     DELSQNTAWW AERLDAVDGE PGYIIDTSEH SPISVVSISQ PTNLENAPSD TPLRRHLVAN
     EQKVVTSMGK RREIDVSPRD SRKVSRKQPK IARSLSPCIA IHSDHTQTTA NTHLSHSQDS
     VGARHLSNIS NLSQPNPIPT YASVGDCEDA VATTSLGNKI ECSTTLRKLD EDGLSRSPQP
     SQQKSAGQNP YQEQQCFAQL ELGLAGSSPS VGPLDTLSFL SETPILLGTG VSRDKVDSIP
     LDPKLLTTSI TEFLEKLLDP NFPDKSHFHH SNPDAAQNFS KCSGIVLVES NTTKASQAAS
     DIARIGNALA INQRTGRLPS KRGKLIFLRC EAMLQHGLFE RNQAGHPENI RERWESHGKQ
     LFAGSLEWGY GISRQRKRRK FDFKSTDVDC EESSRVGRTK ANDSPSPPTM GVDVQLSWDW
     REVLSLV
//
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