ID A0A1S4E1E0_CUCME Unreviewed; 1156 AA.
AC A0A1S4E1E0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN Name=LOC103492544 {ECO:0000313|RefSeq:XP_016901805.1};
OS Cucumis melo (Muskmelon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3656 {ECO:0000313|Proteomes:UP000089565, ECO:0000313|RefSeq:XP_016901805.1};
RN [1] {ECO:0000313|Proteomes:UP000089565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DHL92 {ECO:0000313|Proteomes:UP000089565};
RX PubMed=22753475; DOI=10.1073/pnas.1205415109;
RA Garcia-Mas J., Benjak A., Sanseverino W., Bourgeois M., Mir G.,
RA Gonzalez V.M., Henaff E., Camara F., Cozzuto L., Lowy E., Alioto T.,
RA Capella-Gutierrez S., Blanca J., Canizares J., Ziarsolo P.,
RA Gonzalez-Ibeas D., Rodriguez-Moreno L., Droege M., Du L.,
RA Alvarez-Tejado M., Lorente-Galdos B., Mele M., Yang L., Weng Y.,
RA Navarro A., Marques-Bonet T., Aranda M.A., Nuez F., Pico B., Gabaldon T.,
RA Roma G., Guigo R., Casacuberta J.M., Arus P., Puigdomenech P.;
RT "The genome of melon (Cucumis melo L.).";
RL Proc. Natl. Acad. Sci. U.S.A. 109:11872-11877(2012).
RN [2] {ECO:0000313|RefSeq:XP_016901805.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000256|ARBA:ARBA00007572, ECO:0000256|RuleBase:RU004196}.
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DR RefSeq; XP_016901805.1; XM_017046316.1.
DR AlphaFoldDB; A0A1S4E1E0; -.
DR OrthoDB; 8251at2759; -.
DR Proteomes; UP000089565; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0051103; P:DNA ligation involved in DNA repair; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:EnsemblPlants.
DR GO; GO:0010165; P:response to X-ray; IEA:EnsemblPlants.
DR CDD; cd07903; Adenylation_DNA_ligase_IV; 1.
DR CDD; cd17722; BRCT_DNA_ligase_IV_rpt1; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 2.
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; IPR044125; Adenylation_DNA_ligase_IV.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
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; IPR029710; LIG4.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR NCBIfam; TIGR00574; dnl1; 1.
DR PANTHER; PTHR45997; DNA LIGASE 4; 1.
DR PANTHER; PTHR45997:SF1; DNA LIGASE 4; 1.
DR Pfam; PF16589; BRCT_2; 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 SMART; SM00292; BRCT; 2.
DR SUPFAM; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 1.
DR SUPFAM; SSF52113; BRCT domain; 2.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50172; BRCT; 2.
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|ARBA:ARBA00023172,
KW ECO:0000256|RuleBase:RU000617}; DNA repair {ECO:0000256|RuleBase:RU000617};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000617};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000617}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000089565};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 271..418
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT DOMAIN 591..680
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 742..850
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 848..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..869
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..963
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..978
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..1016
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1042..1065
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1156 AA; 130782 MW; E7B9219DC76AEC7C CRC64;
MSEPIKFAVL SSLFDWIQRS KSSAKKRSKF QTLTTLFVLS TGVKVVLRLV LMPVLQRRQG
MTPGGLTINE LNDLLDRLAS GENRAEKTAV LSTLIQKTNA QEMKWIVMII LKDLKLGVSE
KSIFHEFHPD AEDLFNVTCD LKLVCEKLRD RRQRHKRQDI EVGKAVRPQL ASRVSNANAA
WKKLHGKEVV AECKFDGDRI QIHKNGTEVH YFSRNFLDHS EYGHGMSDVI VQNVLSTRCI
LDGEMLVWDK SLNRFAEFGS NQEIARAAKD GFDSNRQLCY VAFDVLYVGD TSVIHRSLKE
RHELLRNVVK PVKGQLEVLV PNDGLNSDCA GCPWSIRAYN VDDVERFFKS TIENRDEGIV
IKDLGSKWEP GDRSGKWLKL KPDYVRAGSD LDALIIGGYY GSGRRGGEVA QFLMGLAERP
PSNAYPRRFV SFCRVGTGLT DEELDAVVNK LKPYFRKSEY PRKTAPSFYQ VTNNSKERPD
VWIESPEKSI ILSITSDIRT IKSEVFAAPY SLRFPRIDRV RYDKPWHECL DVQSFVELVH
STNGTTQRGT NNSGRQDSKG KYIKSIGKGR KKSVSVVPSH LLQTDITGIT EDSLIFSNML
FYIVNVPPTH SLDSLHKLIV ENGGTFSMNL NNSVTHSVAA DSKAGIKYEA AKRHGDVIHY
SWVLECCSQK KLLPLKPKHF LFLSDNSKKK LEEEIDEFAD SYFWDLELSE LKQLLSNVSI
SEDVKAIDYY RGKYCPKHDW CMFVGCQIYF LPLRLSLKSD WGILLELSIR RLKVEVSFRG
GKVSDDPVSA THIVVFEIPG APVRYETVLK SWNEAEKHAM LKDRIHIVAH QWLEDCLERA
QRLQEDSYNL NPNGKKSIEN INSGMDSETP LVSEDKDNPQ IPCPSMEYKD RGRNEAASGQ
QMLSHSIERS GGKKRGKPAT RSMQKAKSGV EQVRRAQTRK AKGPAKISEV ESDSSDNTDE
KTKAETGNIG TLCTENSEKH VFKTLENEIS NSKKRGRPTA GNAQREKAEA EKIRRTRARI
AKRSAKIGGS ESGNNDSADE ETNEEESKRE KEENEKTNEF KMLEDYDSKQ KGKAIEEVRA
DFKFVEKPEK LEVMKDPLEA MLLDMVPSLG MSGTKSSSSS ITTVVEEKKP FVENKGEAVK
KKVSYKDVAS ELLKDW
//
