ID   C9SP42_VERA1            Unreviewed;       944 AA.
AC   C9SP42;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=DNA ligase IV {ECO:0000256|ARBA:ARBA00031942};
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP] 4 {ECO:0000256|ARBA:ARBA00030676};
GN   ORFNames=VDBG_06667 {ECO:0000313|EMBL:EEY20557.1};
OS   Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS   (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=526221 {ECO:0000313|Proteomes:UP000008698};
RN   [1] {ECO:0000313|Proteomes:UP000008698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136
RC   {ECO:0000313|Proteomes:UP000008698};
RX   PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA   Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA   Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA   Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA   Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA   Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA   Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT   "Comparative genomics yields insights into niche adaptation of plant
RT   vascular wilt pathogens.";
RL   PLoS Pathog. 7:E1002137-E1002137(2011).
CC   -!- FUNCTION: DNA ligase involved in DNA non-homologous end joining (NHEJ);
CC       required for double-strand break (DSB) repair.
CC       {ECO:0000256|ARBA:ARBA00043870}.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS985221; EEY20557.1; -; Genomic_DNA.
DR   RefSeq; XP_003003105.1; XM_003003059.1.
DR   AlphaFoldDB; C9SP42; -.
DR   STRING; 526221.C9SP42; -.
DR   GeneID; 9537149; -.
DR   KEGG; val:VDBG_06667; -.
DR   eggNOG; KOG0966; Eukaryota.
DR   HOGENOM; CLU_004844_1_1_1; -.
DR   OMA; IMLQHRT; -.
DR   OrthoDB; 8251at2759; -.
DR   Proteomes; UP000008698; Unassembled WGS sequence.
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: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   CDD; cd07903; Adenylation_DNA_ligase_IV; 1.
DR   CDD; cd17722; BRCT_DNA_ligase_IV_rpt1; 1.
DR   CDD; cd07968; OBF_DNA_ligase_IV; 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; IPR012309; DNA_ligase_ATP-dep_C.
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; 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; 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:EEY20557.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008698};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          389..514
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   DOMAIN          679..759
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          843..944
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          61..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   944 AA;  107488 MW;  448065C4B55155B6 CRC64;
     MSHREGQPSP SAAAIGEDER QYAVGGMTSQ EVNENYPGRP RNHSETFLFS ELFKSLFNPL
     MENKKQPPGS GPPRAKLGPH GPSKPSPSEQ RRHIIDRFIS RWRKNVGHDF YPAMRLILPD
     KDRDRGVYGL KENAIGKLLV KLMKIDKNSE DGYNLLHWKL PGQTTASRMA GDFAGRAFEV
     LSKRPMRIEV GDMTIADVNE LLDKLAGSSG ELENLEVFET FYERMNAEEL MWLIRIILKQ
     MKVGATEKTL LHLWHPDAET LFNVSSSLRR VCWELFDPQV RLEQENTGVT LMQCFQPQLA
     QFQMPASFQK MVDYLRPPRG SRGLKDDRGA WTRHLGKAFA AGVRNIILDG EMITWDPDTD
     KIMQFGTLKT AALAEQKNPY NNTGPRPLFR VFDILYLNDQ PLTRYTLRDR YNALRKAVIG
     VHRRIEVHEH EAATSADAIE PLLRKVVAEA SEGLVLKNPR SMYRLNSRND DWLKVKPEYM
     TEFGESLDCV VIGGYYGSGK RGGILSTYLC GLRVSENHIK AGANPEKCFS LFKVGGGFSV
     EDYAEIRHHT DGKWKDWDPK KPPNEYIELA HGFAEKPDVW IRPKDSFVLE AKASSVGPSD
     QFALGFTLRF PRFRKLRKDK SWDQGLSVQE FQDLRRRVEE EAQEKTMSVE NTKRRAVKRV
     KKELVIAGTD STPVQFEGEK SKVFEGLEFC VLSESLKPFK KTKTQLETTI KANGGRITQR
     HAARSDLILI ADKRVVSVAS LIKKGDVDII RPNWVQDCLA QETDDGLLPY EERHLFHATE
     GLREIARQNT DEFGDSYFRI VDVEELRQIL VDMSPHEKSE ERDEDAAEFA RQLKERGNDL
     GERDSAVFGR CVVHLHVLPG GELDAFRLRN YIAFGGGEVT DGLPVDSSTH IMLVGGRDAE
     KQDAAVSVRK DIGNRQKIPR VVASQWVEDS WKERTMLDEE RYRV
//