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Database: UniProt
Entry: Q5CU85_CRYPI
LinkDB: Q5CU85_CRYPI
Original site: Q5CU85_CRYPI 
ID   Q5CU85_CRYPI            Unreviewed;       825 AA.
AC   Q5CU85;
DT   12-APR-2005, integrated into UniProtKB/TrEMBL.
DT   12-APR-2005, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=cgd3_3820 {ECO:0000313|EMBL:EAK88972.1};
OS   Cryptosporidium parvum (strain Iowa II).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX   NCBI_TaxID=353152 {ECO:0000313|EMBL:EAK88972.1, ECO:0000313|Proteomes:UP000006726};
RN   [1] {ECO:0000313|EMBL:EAK88972.1, ECO:0000313|Proteomes:UP000006726}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Iowa II {ECO:0000313|Proteomes:UP000006726};
RX   PubMed=15044751; DOI=10.1126/science.1094786;
RA   Abrahamsen M.S., Templeton T.J., Enomoto S., Abrahante J.E., Zhu G.,
RA   Lancto C.A., Deng M., Liu C., Widmer G., Tzipori S., Buck G.A., Xu P.,
RA   Bankier A.T., Dear P.H., Konfortov B.A., Spriggs H.F., Iyer L.,
RA   Anantharaman V., Aravind L., Kapur V.;
RT   "Complete genome sequence of the apicomplexan, Cryptosporidium parvum.";
RL   Science 304:441-445(2004).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAK88972.1}.
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DR   EMBL; AAEE01000004; EAK88972.1; -; Genomic_DNA.
DR   RefSeq; XP_626929.1; XM_626929.1.
DR   AlphaFoldDB; Q5CU85; -.
DR   STRING; 353152.Q5CU85; -.
DR   EnsemblProtists; EAK88972; EAK88972; cgd3_3820.
DR   GeneID; 3373851; -.
DR   KEGG; cpv:cgd3_3820; -.
DR   VEuPathDB; CryptoDB:cgd3_3820; -.
DR   InParanoid; Q5CU85; -.
DR   OMA; WIKYKRD; -.
DR   OrthoDB; 162082at2759; -.
DR   Proteomes; UP000006726; Chromosome 3.
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:UP000006726}.
FT   DOMAIN          544..681
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          73..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..90
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   825 AA;  93061 MW;  1B9BD6A63ABAF8CA CRC64;
     MTGKCLDSLF NEEDDMNEII ETEDSIIDSK ETIINEKISL DSILGRELMS NVKKDEKRSK
     KIKLDSNIQQ KLSFNFGTGN TPSSVNKSKP TKLEKVPENE ESGDSCTKNG SESLSKKIKP
     SNAGLFSPFS INITTGDEDI QSPMFDPCNI SKEKIMAKGK SNSILFSVLT DAFSRIEQLK
     GSGSGSKKGC IVILANLFRL IIHHNPSDLI DAVYICMNKV APDYEGKESG VGDSILIKCI
     SESSDKSEKR IKEDQISGKF EDLGEIAAIC KKQMRLLFEP QRLTIHDVYS DLYSLTEITG
     KQSQQLKKDK IKKLLVSGKQ DEVKYIVRFL QGRLRIGIQQ TTVYQALASA FVLTKNIPGD
     NLASFSDYRL AKNEKKYKNL QELDCEILEM ETSLRSSLCQ LPNIEKIINV AIQGASSDEI
     SAKCKLTTGI PCEPMLARPT KGIQDVLNRF ENFLFTAEYK YDGERAQIHV YKDKSNKRVI
     KIFTRNLESA TDRYPDLIQY LNQSLNSSVE DCILDSEVVA YSKSEDKILP FQVLSTRKRK
     NVAFDDIQIQ ICLMLFDCMG FNGESLLKKS LFERRQYLRK CINEGQSEYI KFTTSTETNK
     LDHLDSFLSE SIENNCEGLM VKTLHDNASY EPSKRSLNWL KIKKDYVDGL TDSIDVVPIA
     ACYGKGKRNG VFGTFLLAVY NTEEEVYETV CKAGTGFSDE ILQSLYTSLK DHIIAEGAPK
     SYYKFDSSGQ LSSLKQDVWF EPKFVWEVKG ADLSLSPVHT AAIGTIDENR GIGLRFPRFI
     RIRDDKSPEQ ATSSIQIMEM YNSQLITNNT KNETNFSDDQ FQEDD
//
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