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Database: UniProt/SWISS-PROT
Entry: DNLI4_COPC7
LinkDB: DNLI4_COPC7
Original site: DNLI4_COPC7 
ID   DNLI4_COPC7             Reviewed;        1025 AA.
AC   A8N936; D6RNV6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   10-MAY-2017, entry version 68.
DE   RecName: Full=DNA ligase 4;
DE            EC=6.5.1.1 {ECO:0000255|PROSITE-ProRule:PRU10135};
DE   AltName: Full=DNA ligase IV;
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP] 4;
GN   Name=LIG4; ORFNames=CC1G_14831;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003;
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., Canbaeck 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., Kuees 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   -!- FUNCTION: Involved in ds DNA break repair. Has a role in non-
CC       homologous integration (NHI) pathways where it is required in the
CC       final step of non-homologus end-joining.
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + diphosphate. {ECO:0000255|PROSITE-ProRule:PRU10135}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EFI27358.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AACS02000007; EFI27358.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_002910852.1; XM_002910806.1.
DR   ProteinModelPortal; A8N936; -.
DR   SMR; A8N936; -.
DR   EnsemblFungi; EFI27358; EFI27358; CC1G_14831.
DR   GeneID; 9379321; -.
DR   KEGG; cci:CC1G_14831; -.
DR   EuPathDB; FungiDB:CC1G_14831; -.
DR   InParanoid; A8N936; -.
DR   KO; K10777; -.
DR   OrthoDB; EOG092C18KW; -.
DR   Proteomes; UP000001861; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   CDD; cd00027; BRCT; 2.
DR   Gene3D; 1.10.3260.10; -; 1.
DR   Gene3D; 3.40.50.10190; -; 2.
DR   InterPro; IPR001357; BRCT_dom.
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; IPR029710; LIG4.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   PANTHER; PTHR10459:SF84; PTHR10459:SF84; 1.
DR   Pfam; PF16589; BRCT_2; 2.
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   SMART; SM00292; BRCT; 2.
DR   SUPFAM; SSF117018; SSF117018; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF52113; SSF52113; 2.
DR   TIGRFAMs; TIGR00574; dnl1; 1.
DR   PROSITE; PS50172; BRCT; 2.
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; Complete proteome; DNA damage; DNA recombination;
KW   DNA repair; DNA replication; Ligase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Nucleus; Reference proteome; Repeat.
FT   CHAIN         1   1025       DNA ligase 4.
FT                                /FTId=PRO_0000333259.
FT   DOMAIN      667    763       BRCT 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00033}.
FT   DOMAIN      915   1025       BRCT 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00033}.
FT   ACT_SITE    291    291       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10135}.
FT   METAL       349    349       Magnesium 1. {ECO:0000255}.
FT   METAL       447    447       Magnesium 2. {ECO:0000255}.
FT   BINDING     289    289       ATP. {ECO:0000250}.
FT   BINDING     296    296       ATP. {ECO:0000250}.
FT   BINDING     311    311       ATP. {ECO:0000250}.
FT   BINDING     452    452       ATP. {ECO:0000250}.
FT   BINDING     463    463       ATP. {ECO:0000250}.
FT   BINDING     469    469       ATP. {ECO:0000250}.
SQ   SEQUENCE   1025 AA;  116801 MW;  B216FFD40932868C CRC64;
     MMQPTPAPSS APGSPQRTQA EPEMETPSYP QPPQNVGTAP FSVLVKLFEK LATERKQERR
     RKLLDAWFRH WRREKGFDLY PVLRLLLPQK DRDRAVYGLK EKNLAKTYIK LIPLGMRDPD
     AIRLLNWKKP TERDKSSGDF PQVLCEVVSK RSSVIEGTLT IDELNEILDD IAKNMGKSDV
     QSKILRRIYN NSTADEQRWI IRIILKDMNI SVKETTVFAV FHPDAQDLYN TCSDLKKVAW
     ELWDPSRRLN AKDKEIQIFH AFAPMLCKRP TRKIEETVKA MGGSKFIIEE KLDGERMQLH
     KRGNEYFYCS RKGKDYTYLY GKHIGAGSLT PFIDSAFDSR IDDIILDGEM LVWDPVSERN
     LPFGTLKTAA LDRSKKENNP RPCFKVFDLL YLNGMSLLDK TVKFRKNNLR HCIKPIPGRI
     EFVEEYQGET ANDIRKRMEQ VMENRGEGLV IKHPKAKYIL NGRNTDWIKV KPEYMDNMGE
     TVDVLVVAGN YGSGKRGGGV STLICAVMDD RRPDSDDEPK YSSFVRIGTG LSFADYVWVR
     SKPWKVWDPK NPPEFLQTAK KGQEDKGDVY LEPEDSFILK VKAAEITPSD QYHMGFTMRF
     PRALAIRDDL SIADCMTATE VFESLKSERK RKMEDDAGIT TKKRKTTVKK VALLPEYSGP
     NLKKVAVKTD IFNGMKFVVF SDPKSRTGEA DKKELMKTIH ANGGTCSQIV NKNSEAIVIY
     GGSITPYDLK LVIDKGIHDV IKPSWITDSV TLGEPAPFKK KYFFHATEER KYADEYNEDD
     GEEEGAVPSA DEQERDVKSG TVEPGSETED EDEEQAPEIK EEQDGELHEW LKVDDRKSPA
     LPAHDEEDSV TEDDSDNADV ADEEEPDLDD WFQVKGETED EGAGALATAS RHRETTPDVD
     GDVKMGESEE AMDYDPDVIF KHLCFYLDSP ANAQRHGMAT RPKYEAAITK SFEEVEKLIK
     DNGGKIVDLD EPKLTHVVLD KRDDSRRVEL MKRTSKPRRR HLVLSDYIEA CIDEGTLLDE
     EGESF
//
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