ID A6RCE0_AJECN Unreviewed; 790 AA.
AC A6RCE0;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 24-JAN-2024, entry version 80.
DE RecName: Full=DNA ligase 1 {ECO:0000256|ARBA:ARBA00041131};
DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
DE AltName: Full=DNA ligase I {ECO:0000256|ARBA:ARBA00041666};
GN ORFNames=HCAG_07298 {ECO:0000313|EMBL:EDN10837.1};
OS Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN10837.1, ECO:0000313|Proteomes:UP000009297};
RN [1] {ECO:0000313|Proteomes:UP000009297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP +
CC diphosphate.; EC=6.5.1.1; Evidence={ECO:0000256|ARBA:ARBA00034003};
CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000256|ARBA:ARBA00007572, ECO:0000256|RuleBase:RU004196}.
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DR EMBL; CH476662; EDN10837.1; -; Genomic_DNA.
DR AlphaFoldDB; A6RCE0; -.
DR STRING; 339724.A6RCE0; -.
DR VEuPathDB; FungiDB:HCAG_07298; -.
DR HOGENOM; CLU_005138_0_1_1; -.
DR OMA; WIKYKRD; -.
DR OrthoDB; 961at2759; -.
DR Proteomes; UP000009297; 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:UniProtKB-EC.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR InterPro; IPR000977; DNA_ligase_ATP-dep.
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; IPR012308; DNA_ligase_ATP-dep_N.
DR InterPro; IPR036599; DNA_ligase_N_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR NCBIfam; TIGR00574; dnl1; 1.
DR PANTHER; PTHR45674:SF4; DNA LIGASE 1; 1.
DR PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR Pfam; PF04679; DNA_ligase_A_C; 1.
DR Pfam; PF01068; DNA_ligase_A_M; 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.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000009297}.
FT DOMAIN 511..648
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 20..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..790
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 790 AA; 86752 MW; 5A024F168DD0CA8D CRC64;
MAQKGGGGAK QATLGKFFGA NAGSASLPKK QATLAFSTSS GSREKRQNGS ATQADEEEAL
VNGDKDVDMN NDAKKKEPKI DSRGSETPAA ESRESDSDSA AEKSLSHSDS DFPDSKKLKR
EKSPMEDSDE SDVQPVTKRR KRAPSNRETA GKKPSASQNQ NKRTRSPNKA REKPVAEDKE
SSSAEQEDII SDNDDDLAEE KPKIAQKKRE TVQQALKGSR EDPYPDWKAG EPVPYAALCT
TFSLIEMTTK RLIILSHCSL FLRQVLRLTP KDLLPTVQLM LNKLAADYAG VELGIGESFI
MKAIGESTGR SLAVIKADQH EIGDLGLVAA KSRSNQPTMF KPKPLTVRGV HEGLLAIAKT
QGHGSQEKKI SAIKKLLSSA DATLAGKGSK GIDITQNKGG PSEAKFIIRF LEGKLRLGLA
EKTVLVALAH AMVAHEVELQ GKKAPSTEEL GKGEAILKSK YPDILGKLEN WVKQGTTSFV
LDCETVAWDT VNKKVLPFQQ LMTRKRKDVK AEDVKVKVCV FAFDLLFLNG EPTVKMTLRE
RRARLHDAFT PIEGEFVFAQ HGDTNDLDEI QTLLDESVKA SCEGLMVKML DTEESGYEPS
KRSRNWLKVK KDYLAGIGDS LDLVVLGAYY GRGKRTSVYG AFLLAAYNTS TQTFQTVCNI
GTGFSEALLE ELHKSLSPLV IDCPKPFYDH SSVPKDQPDV WFEPKYVWEV KAADLTLSPR
YKAAADEFMG TSHGAGKGIS LRFPRYIKSR DDKKPEEATA TRQVAEMYRR QESVSKDTAG
KGGVDDDFEY
//
