ID A0A094HH47_9PEZI Unreviewed; 899 AA.
AC A0A094HH47;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN ORFNames=V501_06281 {ECO:0000313|EMBL:KFZ07621.1};
OS Pseudogymnoascus sp. VKM F-4519 (FW-2642).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420914 {ECO:0000313|EMBL:KFZ07621.1, ECO:0000313|Proteomes:UP000029315};
RN [1] {ECO:0000313|EMBL:KFZ07621.1, ECO:0000313|Proteomes:UP000029315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4519 (FW-2642) {ECO:0000313|Proteomes:UP000029315};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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 ECO:0000256|RuleBase:RU000617};
CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000256|ARBA:ARBA00007572, ECO:0000256|RuleBase:RU004196}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFZ07621.1}.
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DR EMBL; JPKD01001948; KFZ07621.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094HH47; -.
DR STRING; 1420914.A0A094HH47; -.
DR HOGENOM; CLU_005138_0_1_1; -.
DR Proteomes; UP000029315; 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:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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; 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; 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; 2.
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; PS00697; DNA_LIGASE_A1; 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, ECO:0000256|RuleBase:RU000617};
KW DNA damage {ECO:0000256|RuleBase:RU000617};
KW DNA recombination {ECO:0000256|RuleBase:RU000617};
KW DNA repair {ECO:0000256|RuleBase:RU000617};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000617};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000617};
KW Reference proteome {ECO:0000313|Proteomes:UP000029315}.
FT DOMAIN 626..763
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 1..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..210
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 899 AA; 99455 MW; 073A7C79D5B9E140 CRC64;
MPPKQATLGR FFGGSSSANP APSKQTTLSF SSKSTNESKV KTPVKKEELE DEDTTNENRT
PKSDEDAVNE QLASELKASP SPNGKDSKKR IRDEALQYSK SEAAASDESK KLKEEQEEEE
DEEPVLKRSR RSGQESTVSK DASETKPNKK DTAAGNKKGK GKAAAKGIKK EVVEIEDDKP
LAKPERKASA TPEASSEVEE EIEEDEEDEK PELAAKTREK IQTTLKSNSK DPYPDWKPGE
PVPYAALCTT FSLIEMTTKR LIIAAHCSLF LRQVLRLTPD DLLPTVLLMI NKLAADYAGI
ELGIGESLIM KAIGEATGRS LAVIKQDQKE IGDLGLVAVK SRSNQPTMYK PKPLTVRGIH
RSLLSIAVMQ GNGAQTRKVD GIKKLLSAAD SGGGKVDLAK DKGGPSEAKF IVRFLEGKLR
LGLAEKTVLV SLAQAMVCHE TEAKGRDKVP STDQLAKGEQ VLKAVYSELP SYDVIIPAML
QHGIFNLRDN CKLQPGVPLK PMLAKPTKAI TEVLDRFEGQ TFTCEYKYDG ERAQIHYVSK
DSETKYQSSV PAAAKGTAGG LAAIFSRNSE DLSKKYPDIL EKLGTWVKPE TKSFVLDCET
VAWDTVEKKV LPFQQLMTRK KKDVKTEDVK VKVCVFAFDL LFLNGEAVVE KPLRERRSLL
HTAFTPVEGE FAFATSMNGQ EIDDIQTFLD DSVKASCEGL MVKMLDGVES GYEPSKRSRN
WLKIKKDYLA GIGDSLDLVV LGAYHGKGKR TSVYGAFLLA CYNPSTERYE TVCNIGTGFS
EEILETLHAQ LSDTVIDRPK PFYEHSKVNA HQPDVWFEPR YVWEVRTADL TLSPKYRAGY
KEGIAGDAEK GVSLRFPRFI KIRDDKKVDE ATSSRQIAEM YRRQESVSKG PAADDDFEY
//