ID Q53E04_CRIFA Unreviewed; 663 AA.
AC Q53E04;
DT 24-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 24-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Kinetoplast DNA ligase k alpha {ECO:0000313|EMBL:AAY22182.1};
GN Name=LIG k alpha {ECO:0000313|EMBL:AAY22182.1};
OS Crithidia fasciculata.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Crithidia.
OX NCBI_TaxID=5656 {ECO:0000313|EMBL:AAY22182.1};
RN [1] {ECO:0000313|EMBL:AAY22182.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15070723; DOI=10.1073/pnas.0305705101;
RA Sinha K.M., Hines J.C., Downey N., Ray D.S.;
RT "Mitochondrial DNA ligase in Crithidia fasciculata.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:4361-4366(2004).
RN [2] {ECO:0000313|EMBL:AAY22182.1}
RP NUCLEOTIDE SEQUENCE.
RA Sinha K.M., Hines J.C., Downey N., Ray D.S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|ARBA:ARBA00001968};
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; AY380335; AAY22182.1; -; Genomic_DNA.
DR AlphaFoldDB; Q53E04; -.
DR VEuPathDB; TriTrypDB:CFAC1_290022300; -.
DR BRENDA; 6.5.1.1; 1365.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd08041; OBF_kDNA_ligase_like; 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; IPR012310; DNA_ligase_ATP-dep_cent.
DR InterPro; IPR029319; DNA_ligase_OB.
DR InterPro; IPR025487; DUF4379.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR PANTHER; PTHR47810; DNA LIGASE; 1.
DR PANTHER; PTHR47810:SF1; DNA LIGASE B; 1.
DR Pfam; PF14743; DNA_ligase_OB_2; 1.
DR Pfam; PF14311; DUF4379; 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 DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Ligase {ECO:0000313|EMBL:AAY22182.1}.
FT DOMAIN 430..600
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 28..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 663 AA; 71078 MW; B9CB47138DBC5AB8 CRC64;
MKVTWLLRLH GGGGGGAIGG RTLRLLRQAK RHSSSSSSTS LAKGLRSSRQ PKRTSPRRAR
PASRVSISKN STALTAAMAT DAAPLSLADF HPAIARTWIA AASNKMLQPQ HVTPDSRKLA
WWICPSCHHQ YNRRIDLHLA AGGACPKCKA KPSLTPSAQS PGTQRQRRAS SSAAGTTPKT
TATTAKSRAS RSAASASSSL PTSTAAAATA AAGAVAVIAH RCRPNSAQSS LAADNANMLS
KSVADDQYLR VQETRNLLPM LAKNFENERA KIGEAEVIRV SPKLDGIRCV VAYRADTKQV
LFFSRSGTLF ECCDDLIEPA VRHLFEADPT LVLDGELYND SVNLAQLTAL QRKGKVFTSS
SSDPVANFYA QLLAATSITA REKKASSAEP SSGTKGSARG ARQVADPVVI GFEQLTSAIR
TTRQHLTPAV AALQQQLQYH VFDVLYAREF PGGSAATVPF SARYALLKSL LASATRHNMQ
HIPNYNPLVL RLVPNVACTV DQADAVLRAA MRVGYEGAMI RRETNDKNTS AQLLPAKDKL
KRAASAATRA SGGGYGYGKR SGTLLKYKVM QDAEFVIVGA AEGTGKWKGS LGSFVCVTPD
TQQRFNVSPA STDAEKRRMW RTWRAAYQGK ALTVQYQELS PDGVPRFPIG KSVRGAADGH
DWL
//
