ID M7AW94_CHEMY Unreviewed; 1122 AA.
AC M7AW94;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=DNA ligase 1 {ECO:0000256|ARBA:ARBA00041131};
DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
DE AltName: Full=DNA ligase I {ECO:0000256|ARBA:ARBA00041666};
GN ORFNames=UY3_18893 {ECO:0000313|EMBL:EMP24048.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP24048.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
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 -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000256|ARBA:ARBA00007572, ECO:0000256|RuleBase:RU004196}.
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DR EMBL; KB603101; EMP24048.1; -; Genomic_DNA.
DR AlphaFoldDB; M7AW94; -.
DR STRING; 8469.M7AW94; -.
DR eggNOG; KOG0967; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
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:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd07900; Adenylation_DNA_ligase_I_Euk; 1.
DR CDD; cd07969; OBF_DNA_ligase_I; 1.
DR Gene3D; 3.30.1490.70; -; 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; 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; IPR049217; DUF5575_N.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR048315; ZSWIM9_RNaseH-like.
DR NCBIfam; TIGR00574; dnl1; 1.
DR PANTHER; PTHR45674:SF4; DNA LIGASE 1; 1.
DR PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 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; PF17738; DUF5575; 1.
DR Pfam; PF20783; DUF5575_N; 1.
DR SUPFAM; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 1.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 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 replication {ECO:0000256|ARBA:ARBA00022705};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EMP24048.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443}.
FT DOMAIN 852..988
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 268..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1085..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1122 AA; 124260 MW; 1BB09A3C773218CA CRC64;
MEEDELQEKE FFSWEEFSAF FDAWCERRKV LFFVKNSVPL SKCKWATAPP RPDVVEALKY
SSVRLVCKDF RGSSKPDQGG QQKGCCASIV LKMSPKKDRL IVTECQLAHN HALCPIEFAY
YFKKGYLMAN SCLPVRTTNK ISKQFVGGPD VRRLLSYCKS RDHGVLDVLT VLDGLFASDP
SAKVKLVFME DKVPEQLTCQ KGFASAWPAV TAPPTPPMMQ RPITSFFQPM KAVKEEEKIR
LPAEGDSASQ LSEAAVIQRN GVSLSVDSPV KSAAKRPLRR VLESDSDEEE AVLTAQAEVD
PIQEKSLEKA SSKEIPKRKI ELPTSRENNR DEEPSAKRCR EEQGPGDEVG RGAKEEAAMD
MQEVKGQHSE IELAEVNGTL EEGAVNKGEE DCTKGGAQEK PEPPKPSRAI SSFFAPKKVT
VARAGKADEH AAVEIPPAPT GSATASSNGS DGTAGSFSKP VVPLDPMEYN PSKSSYHPIQ
DACWGHGQRV PYLAVARTFE RIEEVSARLK NIETLSNLFR SVIALSPSDI LPCIYLCLNR
LGPAYKGLEL GIGETILMKA VAQATGRQLD QIKAEAQEKG DLGLVAESSR SNQRTMFTPP
KLSAAGVFSK LQEIARMTGS ASMNKKIDII KGLFVACRHS EARYITRSLG GKLRIGLAEQ
SALSAIAHAV SLTPPAQGES MGQGFPPEVL DAGQGKSAEA RKTWLEEQTQ ILKQTFCELP
SYDIIVPILL EHGVESLPQH CKITPGTGAM IVCSAHLDWG GTGSESVCAL GQHTVGMLGI
HILENGDVHI YSRNQEDNTS KYPDIISRIP KVKKGSVRSC ILDAEAVAWD PEKRQIQPFQ
VLTTRKRKDV EAAEIKVQVC LYAFDILYLN GESLVKKPFS RRRQLLHESF VETEGEFLFA
TSMDTSSLDE ISEFLDQSIK DSCEGLMVKS LEVDATYEIA KRSHKWLKLK KDYLEGVGDT
LDLVVIGAYL GKGKRVGMYG GFLLACYDEE SEEYQSICKI GTGFTEEILE KHYSFLKDHV
LEKPRPYYRW DSSTEPNHWL AAVQVWEVKC ADLSISPVHK AAIGLVDEEK GISLRFPRFL
RVRDDKKPEE ATTSSQVAEL YKQQQQIQNQ QPVEKAEEED FY
//