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Database: UniProt/TrEMBL
Entry: A8N1F0_COPC7
LinkDB: A8N1F0_COPC7
Original site: A8N1F0_COPC7 
ID   A8N1F0_COPC7            Unreviewed;       803 AA.
AC   A8N1F0;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 2.
DT   29-OCT-2014, entry version 40.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=CC1G_11289 {ECO:0000313|EMBL:EAU93094.2};
OS   Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC
OS   9003) (Inky cap fungus) (Hormographiella aspergillata).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Agaricales; Psathyrellaceae;
OC   Coprinopsis.
OX   NCBI_TaxID=240176 {ECO:0000313|EMBL:EAU93094.2, ECO:0000313|Proteomes:UP000001861};
RN   [1] {ECO:0000313|EMBL:EAU93094.2, ECO:0000313|Proteomes:UP000001861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC   {ECO:0000313|Proteomes:UP000001861};
RX   PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA   Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W.,
RA   Borodovsky M., Burns C., Canback B., Casselton L.A., Cheng C.K.,
RA   Deng J., Dietrich F.S., Fargo D.C., Farman M.L., Gathman A.C.,
RA   Goldberg J., Guigo R., Hoegger P.J., Hooker J.B., Huggins A.,
RA   James T.Y., Kamada T., Kilaru S., Kodira C., Kues U., Kupfer D.,
RA   Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J., Mackey A.J.,
RA   Manning G., Martin F., Muraguchi H., Natvig D.O., Palmerini H.,
RA   Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA   Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA   Zolan M.E., Pukkila P.J.;
RT   "Insights into evolution of multicellular fungi from the assembled
RT   chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n) +
CC       (deoxyribonucleotide)(m) = AMP + diphosphate +
CC       (deoxyribonucleotide)(n+m). {ECO:0000256|RuleBase:RU000617}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|RuleBase:RU004196}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EAU93094.2}.
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DR   EMBL; AACS02000001; EAU93094.2; -; Genomic_DNA.
DR   RefSeq; XP_001828699.2; XM_001828647.2.
DR   GeneID; 6005130; -.
DR   KEGG; cci:CC1G_11289; -.
DR   InParanoid; A8N1F0; -.
DR   KO; K10747; -.
DR   OrthoDB; EOG7TXKRG; -.
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:0051103; P:DNA ligation involved in DNA repair; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.3260.10; -; 2.
DR   Gene3D; 2.40.50.140; -; 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; IPR012340; NA-bd_OB-fold.
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; SSF117018; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00574; dnl1; 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|RuleBase:RU000617};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001861};
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|RuleBase:RU000617};
KW   Ligase {ECO:0000256|RuleBase:RU000617, ECO:0000313|EMBL:EAU93094.2};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000617};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001861}.
SQ   SEQUENCE   803 AA;  89259 MW;  FD46F5CAEF3ED909 CRC64;
     MGRQQTLGKF FEMPKSMKPA PPQQSSLTEM WGKKRDVSTK SAPKKEEDAM EVDLKQEAQA
     GPSKRKESAL ETKNSPKVKK RRIIESSDEE DEVASRASQS IATSSRHVTP EPSEAASSSP
     VKKHVEGSRA VKPPHSDIDE ESIAASEPEA DEDRDDVLLE DDEELNPVGG TESKSARAAL
     LKKDEVDIKG GWKVGQPVPY AALAKTFSLI EATTKRLEKN AILTAFLLLV IQRSAKDDHK
     SLLQAVYLCI NRLSPDYVGI ELGIGESLLI KAIAESTGRS LAVIKADLKK EGDLGLVAMN
     SKNSQKTLFK PKPLTLPFVF TQLKDIALTT GNASQAKKVA LRANFALERR AICTGFSRTA
     AVLAERERAD KKWSQDKLTA RLEEGAEIMK AVYSELPSYD SVVPALLEGG IKGLRERCKL
     TPGIPLKPML AKPTKAIGEV LDRFENKRFT CEYKYDGERA QIHRLDDGTV GVFSRNSEDM
     SKKYPDLVDQ LSKCIKKNTK SFVLDSEAVA IDRTTGKLMP FQELSRRKRK DVKVEDIQVR
     VCIFAFDLLY LNGEPLINKP LVERRDLLRK HFQVVPGEFD FAKSSDGEST DEIQTFLEES
     VKDGCEGLMV KMLESDASNY EPSRRSVNWL KLKKDYLAGV GDSLDLVVVG AYYGKGKRTN
     YYGAFLLACY DADSEEYQTI CKIGTGFSDE ALQTHYETLK PLEQTKPRGD IKIGGAKPDI
     WFEPKVVWEV LTADLSLSPI YTAAQGLVEE RGISLRFPRF IRVRDDKDAD DATAPEQIAE
     MYERQSLAQA GSKKKGGDDD GFW
//
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