ID A0A1J9QX65_9PEZI Unreviewed; 1327 AA.
AC A0A1J9QX65;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Atp-dependent dna ligase domain-containing protein {ECO:0000313|EMBL:OJD32992.1};
GN ORFNames=BKCO1_3400058 {ECO:0000313|EMBL:OJD32992.1};
OS Diplodia corticola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=236234 {ECO:0000313|EMBL:OJD32992.1, ECO:0000313|Proteomes:UP000183809};
RN [1] {ECO:0000313|EMBL:OJD32992.1, ECO:0000313|Proteomes:UP000183809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD32992.1,
RC ECO:0000313|Proteomes:UP000183809};
RA Fernandes I., De Jonge R., Van De Peer Y., Devreese B., Alves A.,
RA Esteves A.C.;
RT "Proteomics and genomics reveal pathogen-plant mechanisms compatible with a
RT hemibiotrophic lifestyle of Diplodia corticola.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000256|ARBA:ARBA00007572}.
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:OJD32992.1}.
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DR EMBL; MNUE01000034; OJD32992.1; -; Genomic_DNA.
DR STRING; 236234.A0A1J9QX65; -.
DR OrthoDB; 2788069at2759; -.
DR Proteomes; UP000183809; 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; 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:OJD32992.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000183809}.
FT DOMAIN 393..513
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 818..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 901..936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 957..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1131..1155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..851
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1025
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1044
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1059
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1086
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1327 AA; 148052 MW; 47187611491D9FFA CRC64;
MTFRFTWICD LLQAIEDIEC RDPPYLPDRR RVLVRTTIER WFRCHRKDIN HPDTDGAAIL
STLFPHTRTD RVYNIKAPRL EKLVARCLSY RAEKVRELGA WRLPGRGDLG ACLERIERIH
DSEPLPRGDA VTVEEVDCGL RDIASQVRFS SPAVQNHVSA DLPQNILAHI LLRIHSRDKK
WFVRLFLKDF GRVVLDENLV LGEFHFMLPP LLKFQNDFDA AMMLLKGPLA RYHAKPDPLS
QKLMLEQAAQ HLKPKVGVKI GRPTWYKARS MKNCLDMVGD GTWVIERKYD GEFCEVHVDL
GKSEPIQIFS KNGKDATRDR KDLLPAIRDS LRLDTAECQF NSKCILLGEM VVFNQLENAV
VDFDKIRKHV SRSGSFLGID KDSQPHPYEN LMIFYFDILL LDDEVTMALP HTRRRKRLSD
VVTKIEGRAK TVEWKPLDFA EHISRKSLLF HFSAALLYRC EGLVLKPNGP FFSLARDDTG
SWCRGFIKLK QDYMTDMGGA RDQADFAVVA ASYDVHEAQK CRQTNLKFTN LYLGCLVDDG
SYRLRPTFRI VAIVTASHCI PPKELEYLNQ IGQFHCREFD EDDPLQQFAI QWGKAPLPSV
VFTNPLVVEV LGSGFEKPPN ENFYMLRHPR VLRTHMDRSW EDCITMEGLA QTAREAKEAP
PDDDPQDIRD KVKYYMSKLS RSRDGSSLDS RKTTTTLLAT LKDVGRNYTS VTPSPAIISN
QSKALQHSAS SEASVKTPSP ATALIKARRT TVNPIVTANF AKGVTPVSPQ STQWTQTIVT
SPVSAGHPAH RTLSTISPPK RTFAASDAVP PVAIRFNSAK APPARADSEV SPYSDGPNTT
RLRQPQPQPH LLQSPIQKPP VKTLTERHGS NKDISVGDDA AGEKLSLYEE REAISLQQHI
NGLRRQNSKQ NPSKRHKTMR PDLRPHACPP SEITGSCSSS AFAHSRIAAP LKSAMAKVSP
GQQKDAEDII SKQRTLKMTV STERSTEPEE GLPTRPHYTG ASAYMLPPIP MLAGHPMPTP
PQSSPDGPIS KGNISATTPR SLFASPPSSS PPYPPTAATP PTISGKENTQ FTSKTTGINR
LDSTALRVPT ETPGRGLKRP ATGSVDDFAI GATPRKIPKW RSSVYARPNL PASIPTNKSN
GCRNTSTSTT AAKPSSSTFD HKAIFTSPNT PPPLPIPYNL AQTVIYLAPS LRKRHYPHHP
LHNILVEHYS PHVPIIINNL EHWRRGDGLQ TQYESQGSTV PESQAYDGYD RIALVDPTME
DECKEVVQGV EGLIGALGGS GRAKEGSVGL FDWRVLEELV EAAGDEEREK GVWMRRLRGA
VGMVRSC
//
