ID A0A1H5SUW8_9BACT Unreviewed; 1036 AA.
AC A0A1H5SUW8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
DE AltName: Full=NHEJ DNA polymerase {ECO:0000256|ARBA:ARBA00029943};
GN ORFNames=SAMN05421819_0342 {ECO:0000313|EMBL:SEF53607.1};
OS Bryocella elongata.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Bryocella.
OX NCBI_TaxID=863522 {ECO:0000313|EMBL:SEF53607.1, ECO:0000313|Proteomes:UP000236728};
RN [1] {ECO:0000313|EMBL:SEF53607.1, ECO:0000313|Proteomes:UP000236728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22489 {ECO:0000313|EMBL:SEF53607.1,
RC ECO:0000313|Proteomes:UP000236728};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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DR EMBL; FNVA01000001; SEF53607.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H5SUW8; -.
DR OrthoDB; 9802472at2; -.
DR Proteomes; UP000236728; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR CDD; cd07906; Adenylation_DNA_ligase_LigD_LigC; 1.
DR CDD; cd07971; OBF_DNA_ligase_LigD; 1.
DR CDD; cd04862; PaeLigD_Pol_like; 1.
DR Gene3D; 3.30.1490.70; -; 1.
DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR Gene3D; 3.90.920.10; DNA primase, PRIM domain; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR InterPro; IPR014146; LigD_ligase_dom.
DR InterPro; IPR014144; LigD_PE_domain.
DR InterPro; IPR014145; LigD_pol_dom.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR014143; NHEJ_ligase_prk.
DR InterPro; IPR033651; PaeLigD_Pol-like.
DR NCBIfam; TIGR02777; LigD_PE_dom; 1.
DR NCBIfam; TIGR02778; ligD_pol; 1.
DR NCBIfam; TIGR02779; NHEJ_ligase_lig; 1.
DR NCBIfam; TIGR02776; NHEJ_ligase_prk; 1.
DR PANTHER; PTHR42705; BIFUNCTIONAL NON-HOMOLOGOUS END JOINING PROTEIN LIGD; 1.
DR PANTHER; PTHR42705:SF2; MULTIFUNCTIONAL NON-HOMOLOGOUS END JOINING DNA REPAIR PROTEIN LIGD; 1.
DR Pfam; PF04679; DNA_ligase_A_C; 1.
DR Pfam; PF01068; DNA_ligase_A_M; 1.
DR Pfam; PF13298; LigD_N; 1.
DR Pfam; PF21686; LigD_Prim-Pol; 1.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000236728};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 482..607
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1036 AA; 113231 MW; 792A7EF7C43DCC43 CRC64;
MATSKKQAAG AAKKIATRKS AAKRPAKKGA SKAQAEPRLR AAAKTPVTSK VSSKSNSKVS
SPVSTRSKPE RSADLVDEQL ARYRSMRDFS ITSEPAGSGR QASSGKQAGP GTQAATKGTA
ARPATVKLKS KLSRGLPFVI QKHAASHLHY DFRLGWSGVL KSWAVAKGPS YFPGDKRLAV
QVEDHPMEYG GFEGIIPEGQ YGGGTVMVWD QGTWWPQLGH ENVEAGLREG SLKFEMNGGK
MKGKWTLVRM KPHTGANGKS WGSADKPNWL LIKEHDQFEQ PEGAKPITES KPNSALTGRT
LEEIALAEDH VWNSKDTAKG EGRAWYRQGA NSSTAALRTP ATRTVAARTT PTPAPARSTI
SAHKRPVRKA VAGSLGAALA RLPKERQPQF LTPQLALEAT NPPEGDGWLH ELKLDGYRIQ
ARKHGDKVEL LTRKGLDWTH RMPAIAAAVA ALPVDACTLD GEVVVLSANG TTSFADLQAA
FQEHAKHDLT YFVFDLLHLD GHNPRGLPLR ERKALLEQVL TPKDETVRYS EHLETGGAKM
FAKACSLQAE GIVSKRADSP YAGSRSNTWL KSKCRREQEL VIGGYTLSAE GNDRIGALVL
GYYDNGELIY AGRTGTGFTQ VTRRDLLTKL EHITRRSPAF DRIPADARRD VQWVEPKLVA
EVHFATWTAD KLVRQASFLG LREDKPANEV RLEEPAVKGD GKPANRRSSH RRAESAAHHS
GRDVAARVAA KRNLKSRASG AAAAPASIRL THPEKVLDPD SGLTKRQLAD YYWAYASHIL
PQITGRPLSL VRCPEGVGGE TFFQKHANHM LPAGVGSIQV PNKKTGEKEA YIAIDNAEAL
TSLAQIGVLE IHPWGSTSRD LEHPDRIIFD LDPDESLPWS ALTEAASDVR ARLKKAGLES
FLKLTGGKGL HVVAPIEPKL GWAEVKDATH RLVLAMERAR PELYLTKMSK SERKGRIFLD
YLRNERGATA VAAFSPRARP GVHVSLPLPW DALKETRRPE VSVQELLSSH DMSRADPWKC
ISTIKQSLDP SRFAEK
//
