ID W7MBM5_GIBM7 Unreviewed; 1012 AA.
AC W7MBM5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=ATP-dependent DNA ligase family profile domain-containing protein {ECO:0000259|PROSITE:PS50160};
GN ORFNames=FVEG_08168 {ECO:0000313|EMBL:EWG48371.1};
OS Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS fungus) (Fusarium verticillioides).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=334819 {ECO:0000313|EMBL:EWG48371.1, ECO:0000313|Proteomes:UP000009096};
RN [1] {ECO:0000313|EMBL:EWG48371.1, ECO:0000313|Proteomes:UP000009096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3125 / FGSC 7600 {ECO:0000313|Proteomes:UP000009096};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000256|ARBA:ARBA00007572}.
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DR EMBL; DS022251; EWG48371.1; -; Genomic_DNA.
DR RefSeq; XP_018754562.1; XM_018897003.1.
DR AlphaFoldDB; W7MBM5; -.
DR GeneID; 30065923; -.
DR VEuPathDB; FungiDB:FVEG_08168; -.
DR OrthoDB; 2788069at2759; -.
DR Proteomes; UP000009096; 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 PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000009096}.
FT DOMAIN 384..524
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 681..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..710
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..762
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..787
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1012 AA; 113528 MW; 8E3E9B0E251F1C07 CRC64;
MPLPFSLVCE LLEQSFLLSL SKKSCSDTVT KWFTRHRDYV DAHDTDLPTL LSTLLPEKRT
DRVYCIQSAR LERIIGRAYL LGSSRIKELA QYRQPGSVVD LADCVFRILT VTPSPSYDHK
NLVTVEEIDQ LLHSLAAKIK WSSPSIRASQ ASLTPSNRAD LESLYRRLSA TEAKWFTRLI
LKSYQPLALD PYLIYRLCDP ILPCVLKIQD DFATAITSLQ AIRGRLLPNC GRKTPREQIM
GAIKPQLGVK IGRQPWVKGR SIKHCLDMGH GRMSVEEKID GEYCQIHVDP SKGDQCLQIF
SKSGKDSTED RAALREIILE SLKIGQPDAR VKKACILEGE LVVYDDSQEK ILPFHRIRKH
VSRRGRFLNT ELDSLPGPQE HLMIIYYDVM LLEDQSLVNL RHSERFKILS NLVCCRKGWA
SLVPRQVIDF GQPLGASTLR KAFAMVILAR KEGLVLKPDE PYFDFTDQRR KFSSCCIKLK
KEYIGNFGDV GDFSAVGARY DPTKALSYRI PGLKWTHFYI GCLDNRQAVK SWGATPEFTI
VNVVELNEAL LREVVTYSNP EPVSPDDNEA LVLKLAPGVE RGSPPTFIFT RPLVFDLKCF
SFDRVGNTGF WSLRFPSVTK IHFDRDFTDT ISFEQLQALA KEATTAGRLE DSQENLQWIA
KLEAADPRGI AVDAVSQLTV TTMPTPSPRK STQNTTSTQS PTSSLATKSP VEATPCRGRS
ERLHRAPSLD LPSITATPSL RADPSSRTKL CTKHKRDLPS TVPTSQHKRL KSSNESSISQ
KDSPQIDLAS QPRAPLADRD NNPRPPPAMS SCALCCPASP SESFFGESSN SDGVNAGVLQ
FIIDPGTGEL QTETEPERLK PSITKVTAAL EGQCVYAGEH CMLAKAVVLV SPGLLTMKEE
AKTFLAQHGV DTPVTDIDAW LKAEKEARQK GKTTTPSKAY VVCDSDNKLA FKHLAGKFKE
LRKDNLFNKG THIEIHDWRF LSYLTTQEDE SIEEKYFHGF SDWRMRWKLH TI
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