ID   E0W2H3_PEDHC            Unreviewed;       891 AA.
AC   E0W2H3;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=DNA ligase 4 {ECO:0000256|ARBA:ARBA00022073};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
DE   AltName: Full=DNA ligase IV {ECO:0000256|ARBA:ARBA00031942};
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP] 4 {ECO:0000256|ARBA:ARBA00030676};
GN   Name=8232803 {ECO:0000313|EnsemblMetazoa:PHUM592850-PA};
GN   ORFNames=Phum_PHUM592850 {ECO:0000313|EMBL:EEB19829.1};
OS   Pediculus humanus subsp. corporis (Body louse).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Psocodea; Phthiraptera; Anoplura; Pediculidae;
OC   Pediculus.
OX   NCBI_TaxID=121224;
RN   [1] {ECO:0000313|EMBL:EEB19829.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=USDA {ECO:0000313|EMBL:EEB19829.1};
RA   Kirkness E., Hannick L., Hass B., Bruggner R., Lawson D., Bidwell S.,
RA   Joardar V., Caler E., Walenz B., Inman J., Schobel S., Galinsky K.,
RA   Amedeo P., Strausberg R.;
RT   "Annotation of Pediculus humanus corporis strain USDA.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEB19829.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=USDA {ECO:0000313|EMBL:EEB19829.1};
RG   The Human Body Louse Genome Consortium;
RA   Kirkness E., Walenz B., Hass B., Bruggner R., Strausberg R.;
RT   "The genome of the human body louse.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblMetazoa:PHUM592850-PA}
RP   IDENTIFICATION.
RC   STRAIN=USDA {ECO:0000313|EnsemblMetazoa:PHUM592850-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) 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   -!- 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   EMBL; AAZO01007226; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DS235878; EEB19829.1; -; Genomic_DNA.
DR   RefSeq; XP_002432567.1; XM_002432522.1.
DR   AlphaFoldDB; E0W2H3; -.
DR   STRING; 121224.E0W2H3; -.
DR   EnsemblMetazoa; PHUM592850-RA; PHUM592850-PA; PHUM592850.
DR   GeneID; 8232803; -.
DR   KEGG; phu:Phum_PHUM592850; -.
DR   CTD; 8232803; -.
DR   VEuPathDB; VectorBase:PHUM592850; -.
DR   eggNOG; KOG0966; Eukaryota.
DR   HOGENOM; CLU_004844_2_0_1; -.
DR   InParanoid; E0W2H3; -.
DR   OMA; EGIMIKH; -.
DR   OrthoDB; 8251at2759; -.
DR   Proteomes; UP000009046; 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; 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; 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; PF00533; BRCT; 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; 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; 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};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EEB19829.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009046};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          348..483
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   DOMAIN          796..891
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
SQ   SEQUENCE   891 AA;  102161 MW;  E252DFE0E852D929 CRC64;
     MSLAKKISFG NFCQLCSKIK SADHEKKIII LRNYISNWKK KAKDIESDGL NLDDSFFPIF
     RLLIPHLDRE RGAYGIKERT LAKIYISILS LPKDGEDALK LLNCKNPKTS YFNNCDFASI
     AFCILRNRCA EGGQLSVEEV NKHLDKISTS HAANEPRNVD AELISLLKST NAEEQKWLIR
     ILLKDVKLGL SENVIFKCYH PDARELYDSS NSLRKICDLL NDPEIRLNEI QIQLFTPFKP
     MLSEECDIQK IDYYLKRSCH FFIETKLDGE RFQLHFEEGN FKYFSRNGYD FTTNFGSSKR
     EGNLSPRIFK RIPPHVKSFV LDGEMMSWDR ITRSFSSKGK NLDVKNLKEG NHYQSCFCVF
     DILLYNGEVL TNKPLIARLE ILEKIIEPEE GTIIILNRKQ ISSNSEVIDS LNEAIDNREE
     GIVMKESMSV YKPNVRKNGG WYKIKPEYTD GLAETLDLLI IGGYYGRGHL KGSVNHFLLG
     AAVNVSDDNI LFYSTGRVGS GYSIKDLEDL SLKLKPYWKE AKNDRMPLSV KWGKEKPDVW
     IKPDKSYILE IKASEIVSSA IFKSGYALRF PRVEKIRYDK TWKECLTLHN LEEIAKIASG
     KLTASHFSQS NIPSFLPKKK AKTSIWNINS ENFDFSGIKC ISKLLQGKEI CVFSGFKNIK
     KLDLEKKVVE FGGKLVKNPG KNTFCILAES DNHTRIKNII KCGSYDILYS SCFFSFLKIE
     NVKMPKLKPE HFLAMSKGTK EEFSKSYDKY GDHFTKKSTF DAIKHSLNAA SQEGKNIVLT
     SDEIYEMDVN LFGKTSPYSI FRNHVGYFDQ FKIVSDSSSK FSSDLDLFKI DFRFYGGKCS
     DAIDDSTVTH VITLSSDSSR INEINNENHK RKRKFHVVNE KWIESCIKEN A
//