GenomeNet

Database: UniProt
Entry: A0A067CLY3_SAPPC
LinkDB: A0A067CLY3_SAPPC
Original site: A0A067CLY3_SAPPC 
ID   A0A067CLY3_SAPPC        Unreviewed;       891 AA.
AC   A0A067CLY3;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=SPRG_04994 {ECO:0000313|EMBL:KDO30210.1};
OS   Saprolegnia parasitica (strain CBS 223.65).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Saprolegnia.
OX   NCBI_TaxID=695850 {ECO:0000313|EMBL:KDO30210.1, ECO:0000313|Proteomes:UP000030745};
RN   [1] {ECO:0000313|EMBL:KDO30210.1, ECO:0000313|Proteomes:UP000030745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 223.65 {ECO:0000313|EMBL:KDO30210.1,
RC   ECO:0000313|Proteomes:UP000030745};
RX   PubMed=23785293;
RA   Jiang R.H., de Bruijn I., Haas B.J., Belmonte R., Lobach L., Christie J.,
RA   van den Ackerveken G., Bottin A., Bulone V., Diaz-Moreno S.M., Dumas B.,
RA   Fan L., Gaulin E., Govers F., Grenville-Briggs L.J., Horner N.R.,
RA   Levin J.Z., Mammella M., Meijer H.J., Morris P., Nusbaum C., Oome S.,
RA   Phillips A.J., van Rooyen D., Rzeszutek E., Saraiva M., Secombes C.J.,
RA   Seidl M.F., Snel B., Stassen J.H., Sykes S., Tripathy S., van den Berg H.,
RA   Vega-Arreguin J.C., Wawra S., Young S.K., Zeng Q., Dieguez-Uribeondo J.,
RA   Russ C., Tyler B.M., van West P.;
RT   "Distinctive expansion of potential virulence genes in the genome of the
RT   oomycete fish pathogen Saprolegnia parasitica.";
RL   PLoS Genet. 9:E1003272-E1003272(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         ECO:0000256|RuleBase:RU000617};
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|ARBA:ARBA00007572, ECO:0000256|RuleBase:RU004196}.
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; KK583202; KDO30210.1; -; Genomic_DNA.
DR   RefSeq; XP_012198898.1; XM_012343508.1.
DR   AlphaFoldDB; A0A067CLY3; -.
DR   STRING; 695850.A0A067CLY3; -.
DR   EnsemblProtists; KDO30210; KDO30210; SPRG_04994.
DR   GeneID; 24127408; -.
DR   KEGG; spar:SPRG_04994; -.
DR   VEuPathDB; FungiDB:SPRG_04994; -.
DR   OMA; WIKYKRD; -.
DR   OrthoDB; 961at2759; -.
DR   Proteomes; UP000030745; 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:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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; IPR012340; NA-bd_OB-fold.
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   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; PS00697; DNA_LIGASE_A1; 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, ECO:0000256|RuleBase:RU000617};
KW   DNA damage {ECO:0000256|RuleBase:RU000617};
KW   DNA recombination {ECO:0000256|RuleBase:RU000617};
KW   DNA repair {ECO:0000256|RuleBase:RU000617};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000617};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000617};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030745}.
FT   DOMAIN          614..759
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          1..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..62
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..107
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..172
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..202
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..233
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   891 AA;  97964 MW;  3C107FC679F674E7 CRC64;
     MSKRQQSIMS FFGSKPAGDE PAESPKAKPT PATPEAKQPS TKKPAPKKAT PAKEEAAPRK
     KKAGEASAAP GLQASLGHID DDDDDDDDDD PFATKKTPAK KPVVESDDEQ EDETMGAHED
     EDVAADNVES DDGVKAPEAS APKTATTPKK ATTPKKVTTP KKTATTKTAT PKRATTPKKE
     PTSKEPKPAD DTTDKKPADE LSSGFFAKKT ETPKKESAAT PAKATSTATM VQGKEKDPTK
     RGGWKAGDAV PYAALARVFA LIEETSGRLV IQDTLADFLR SVIELTPSEL VPCIYLCVCT
     ELAPAYENVQ IGIGDAILIK SIGEATGTNA KFVKELYQKE GDLGKVALNA RSKQSTLFTF
     QKPKLLSVQN VYSDMVKIAR MAGNNSQASK CSIIKSLLVR CDKASEEAKY VIRGLQGKLR
     IGLAGQSILM ALTQAFLHPK EANDKIKQAE ALKCVKRAFS EFPNYETLAQ ALLTIYDREN
     GGKGLHAPQF EELAAMCHLT PGVPVSPMLA RPTKSYAMVL DRFQDQPFTC EYKYDGERAQ
     IHILESGEIS IFSRNFENST ERFPDVKLSI LKAARKNNVT SCIVDAEVVA VDKTTNQRLP
     FQVLSTRSRK NVVLSDIKVQ VCIYAFDVIY LNGESLLKEP LRKRREILET MFEIEDGSFE
     LATSLNVTNT KEDDMETTVE IVRNFLEEAV KGNCEGLMVK TLEQEATYEP ANRSHKWLKL
     KKDYLDGIGD STDLVPVGAF YGKGKRTGVY GAYLLACYDP ETEMYQCITK LGTGLSDEVL
     QQFYTQFKDK TIDKPRNDYE INDAIKPDVW FEPSTVWEIL GADLSISPKY TAAIGHVAKD
     KGISLRFPRF IRLREDKRTT QATTAAQIAD LYRAQGLNTT NDGDNDDDDL L
//
DBGET integrated database retrieval system