ID A0A182N904_9DIPT Unreviewed; 924 AA.
AC A0A182N904;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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};
OS Anopheles dirus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7168 {ECO:0000313|EnsemblMetazoa:ADIR004128-PA, ECO:0000313|Proteomes:UP000075884};
RN [1] {ECO:0000313|Proteomes:UP000075884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WRAIR2 {ECO:0000313|Proteomes:UP000075884};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Walton C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles dirus WRAIR2.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ADIR004128-PA}
RP IDENTIFICATION.
RC STRAIN=WRAIR2 {ECO:0000313|EnsemblMetazoa:ADIR004128-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 AlphaFoldDB; A0A182N904; -.
DR STRING; 7168.A0A182N904; -.
DR EnsemblMetazoa; ADIR004128-RA; ADIR004128-PA; ADIR004128.
DR VEuPathDB; VectorBase:ADIR004128; -.
DR OrthoDB; 8251at2759; -.
DR Proteomes; UP000075884; 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; 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; 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; 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; PF04679; DNA_ligase_A_C; 1.
DR Pfam; PF01068; DNA_ligase_A_M; 1.
DR Pfam; PF04675; DNA_ligase_A_N; 1.
DR SUPFAM; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
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; 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 345..478
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT DOMAIN 640..729
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 603..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..642
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 924 AA; 103309 MW; D40E2A3095C17D40 CRC64;
MSSSVKVESF GELSALLEQV KQSPRQQKES AFCKFFTTFE RHRQSFGDDA TSRPSIYTWL
RLLVPGLDRE RKAYGMRERT LTDAYIQALA LDRQSAEVRR LLDGGGDDLA ERLAPLLHGR
CPQDGDLTVA EVDRRLDAIG EGRAGARTEL VALLEHGSSL DHRWLVRIVL KNLRLGVSNR
RILQLYHPNA PSLYDSAGDL KRVVELLETT DGGGSQHLQQ HQGEIALRPM HFIRPMLCQR
VELRQVGELL GRDTYWLETK MDGERFQVHW DGTIFRYYSR NGYDYSDAFG RTPDQLDGTL
SPMLAALLAP SVRELVLDGE MMVFDRRELR YRDKCDGTDV KALRTGNTTL RPCFCAYDVL
YYNGRSLAGV PYAERARLLP EVVRPQFGFV AHCERERVQD ANHLIQLLNT AIDAQQEGVV
LKRENAHYQP NRRAGTGWYK IKPDYIAGLV VDFDLLVLGG FYNQRRTYVN AFLLGVAKTP
TEFVSVARVS MGLGTAEWQQ LNQTFRPHWR TGEAAAHGLH FGRTQPDVWI APASSLALEI
RGSELVRSES YAAGFTIRFP RIVTVRADKP SDEVCTLEEL EGLAGTTGST RKATKLAKRH
VTLADLSGPP APSQRRAGKR GAPRVERKPD APREREPSPF ADGMLHGRDV CVMSTGSDTS
TVAVEALVRR HGGRAVANPG SDTYAIVAGR ETFKVRKYMA TNRWDVVREE WLLRAGMSGR
LTPFRPEDVL AATEPTQQRL AAQYDRYGDS YTRPVTPTTF TALLRRVTVA GEALPPLSAG
EVIRAERALL GAEEARRVRL FRGCTARLYH DVDKTAANEE LEPAGMQVGA LRAMREMLRF
VRHGGRWLRD SEPGPVQYLF VASTAAEAAS SRLARNVSQW LGTVAGEDTG ETLLSVDWIG
RSIEAGSLCG LTEFIIDRDD RSIK
//
