ID A0A0A2K821_PENEN Unreviewed; 1423 AA.
AC A0A0A2K821;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN ORFNames=PEX2_087070 {ECO:0000313|EMBL:KGO60525.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO60525.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO60525.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO60525.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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 -!- 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}.
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:KGO60525.1}.
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DR EMBL; JQFZ01000070; KGO60525.1; -; Genomic_DNA.
DR RefSeq; XP_016601582.1; XM_016745977.1.
DR STRING; 27334.A0A0A2K821; -.
DR GeneID; 27681397; -.
DR HOGENOM; CLU_004844_1_1_1; -.
DR OrthoDB; 8251at2759; -.
DR Proteomes; UP000030143; 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: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 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; 1.25.40.20; Ankyrin repeat-containing domain; 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; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
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; IPR021536; DNA_ligase_IV_dom.
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; PF12796; Ank_2; 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 Pfam; PF11411; DNA_ligase_IV; 1.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00292; BRCT; 2.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
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; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50172; BRCT; 2.
DR PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
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:UP000030143};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REPEAT 361..390
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 845..970
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT DOMAIN 1135..1220
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 1312..1421
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 475..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1423 AA; 162200 MW; B4BCC5E18DC233B8 CRC64;
MSSKSIKVIS LSKNVGRLSQ LYKRVKMENV KVLLAREVGT VKARKIHSAL GDPACWIHEL
LIETLVDDFV VEIRNKEAGT LQVAFQALDS QVWDLQHHEH DTFIWLLSWD KIVKRARFPY
AGKGVCTLIF QTGSDVRIDG LLWPHDPNLP AQEQLFRKFG SVKVAKHEVQ ESAVPQTSHR
LLDMPNLYKD LRLAIENGDT ETTTKLLDNG LGIEDHHFRT ATVNKYIDIV EQFLSRGWGI
HTDMSNTAPS ALGIPLKMWD FPSGFSATAR TQTKGAVFGT ARHYPTRSGM VLLMPSSFFL
KMEVKSKMGS FCITPRCEPK MTTTKQLIYN QDPDYNKLCV NKLLDEGTLE YSMSESSGLG
TPLHYAARSG SAKMVTFLVE QGGAPDLQDP YRRTPISYAI RNGHHDIEQF LKKLNFSYLT
SPSMDSDEIL GQDLLKPENE EDLDEKYPNR PHNRAPTLPF HDLYLNLFNP LSELKKKPSG
PAPARRKVGP HGKGATSLNP FERRRDVIER FISRWRKDVG DDIYPALRLI LPDKDRDRPM
YGVKEKAIGK MLVKTMKINK ESEDGYNLLN WKLPGQGATT RMAGDFAGRC FDVLSKRPMR
TEPGDMTIDE VNEKLDKLSA ASKEDEQLPI LTEFYRRMNP EELLWLIRII LRQMKVGATE
RTLFDVWHPD AQNLYSISSS LRRVCWELHD PNIRLEGEER GIALMQCFQP QLAQFQMHSF
EKIIARMKPA EDDNVFWIEE KMDGERMQLH MAPDDSTKGG RKFGFWSRKA KEYTYLYGNG
IYDENGALTR HLKDAFVDGV QSIILDGEMI TWDPEQDAMV PFGTLKTAAL AEQRNPFSNG
PRPLFRIFDI LHLNGRDLTK YTLRDRRNAL EKTVRPVHRR FEIHPYEEAT TTTEVEAALR
KVVAEASEGL VLKNPRSPYR LNERHDDWMK VKPDYMTEFG ESLDVVVIGG YYGSGHRGGA
LSSFLCGLRV DDSTQAAEKC WSFCKVGGGF TAADYQEVRH HTEGKWKAWD AKKPPTTFIE
LAGGDAQHER PDMWIKPSDS IVLCVKAASV AISDQFRMGL TLRFPRFKKL RKDKDWKSAL
SVQEFLDLKS NAEQEHREKD FSVDNSRKKR VKRTTKKPLT VAGYDNNVDV QYLGPSGHVF
DELNFFIMTE STIPEKKTKL QLEQLVKANG GKIYQTRTAA VETLCVAERR TVKVASLQKS
GEQNIIRPSW LIDCIKQNEI DAGLPDLLLP FEPRHMFFMT EDNEEEVAAN VDKFMDSYAR
DTTVEELKDI FKQMEKNEEQ PDHVPDPETI QRVEARIQEK VNAGYTVPCG WLFRGLKFYF
YSNGSQPDEP ASRELRKEDQ RLHFACNTAR FAGAESASSL KSSGTTHVIV DPETVSSADI
SSLRKSLAEK PGAKMPHLVS VSWVEECWKN GTLLDEERFP VPR
//
