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Database: UniProt
Entry: L5LGQ7_MYODS
LinkDB: L5LGQ7_MYODS
Original site: L5LGQ7_MYODS 
ID   L5LGQ7_MYODS            Unreviewed;       504 AA.
AC   L5LGQ7;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Poly [ADP-ribose] polymerase {ECO:0000256|RuleBase:RU362114};
DE            Short=PARP {ECO:0000256|RuleBase:RU362114};
DE            EC=2.4.2.- {ECO:0000256|RuleBase:RU362114};
GN   ORFNames=MDA_GLEAN10023231 {ECO:0000313|EMBL:ELK25071.1};
OS   Myotis davidii (David's myotis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK25071.1, ECO:0000313|Proteomes:UP000010556};
RN   [1] {ECO:0000313|Proteomes:UP000010556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(2013).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the ARTD/PARP family.
CC       {ECO:0000256|ARBA:ARBA00024347}.
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DR   EMBL; KB112367; ELK25071.1; -; Genomic_DNA.
DR   AlphaFoldDB; L5LGQ7; -.
DR   eggNOG; KOG1037; Eukaryota.
DR   Proteomes; UP000010556; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   CDD; cd01437; parp_like; 1.
DR   Gene3D; 3.90.228.10; -; 1.
DR   Gene3D; 1.20.142.10; Poly(ADP-ribose) polymerase, regulatory domain; 1.
DR   Gene3D; 2.20.140.10; WGR domain; 1.
DR   InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR   InterPro; IPR004102; Poly(ADP-ribose)pol_reg_dom.
DR   InterPro; IPR036616; Poly(ADP-ribose)pol_reg_dom_sf.
DR   InterPro; IPR036930; WGR_dom_sf.
DR   InterPro; IPR008893; WGR_domain.
DR   PANTHER; PTHR10459; DNA LIGASE; 1.
DR   PANTHER; PTHR10459:SF66; PROTEIN MONO-ADP-RIBOSYLTRANSFERASE PARP3; 1.
DR   Pfam; PF00644; PARP; 1.
DR   Pfam; PF02877; PARP_reg; 1.
DR   Pfam; PF05406; WGR; 2.
DR   SMART; SM00773; WGR; 2.
DR   SUPFAM; SSF56399; ADP-ribosylation; 1.
DR   SUPFAM; SSF47587; Domain of poly(ADP-ribose) polymerase; 1.
DR   SUPFAM; SSF142921; WGR domain-like; 2.
DR   PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR   PROSITE; PS51059; PARP_CATALYTIC; 1.
DR   PROSITE; PS51977; WGR; 2.
PE   3: Inferred from homology;
KW   ADP-ribosylation {ECO:0000256|ARBA:ARBA00022765};
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU362114};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU362114};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362114}.
FT   DOMAIN          20..110
FT                   /note="WGR"
FT                   /evidence="ECO:0000259|PROSITE:PS51977"
FT   DOMAIN          132..255
FT                   /note="PARP alpha-helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51060"
FT   DOMAIN          201..288
FT                   /note="WGR"
FT                   /evidence="ECO:0000259|PROSITE:PS51977"
FT   DOMAIN          331..504
FT                   /note="PARP catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51059"
SQ   SEQUENCE   504 AA;  56418 MW;  E85084BB41B92B84 CRC64;
     MTPSSLPSQG LLCRGVQSDP CEVHEDYDCT LNQTNIGNNN NKFYIIQLLE VSGGFACWNR
     WGRVGEVGQS KLGDIKPLED AKKDFEKKFK DKTKNSWAER EHFVAQPGKY TLIKEDVVKV
     ESLCAQVEGG PVRTVVQRVQ PCSLDAPTQR LITNIFSKEM LMNLDVKKMS LGKLSKQQLL
     KGLDALGALE AALKGQEDRA GGRSLEDLSS DFYTLIPHNF GRSRPPPINS LELLRAKEDI
     LLGEVGQSKL SYFPSLEDAK KDFEKKFKDK TKNSWAEREH FVAHPGKYTL IEVQGEMEAQ
     EAVVKVLADI ELAQTLQAAP EEGEEVEEVT HPLDRDYQLL RCQLQLLDPE APEYKVIHTY
     MKQTSGSPRG PVLRHAWKVN RDGEEDRFQT HSTLGNRRLL WYSNTVAVTV AAILTRGLRI
     MPHSGGRVGK GIYFASENSK SASYVTTMKC EGHRIAYMFL AEVALGREHH ITADDDNLKQ
     APPGFDSVIA RGRTEPASAL APRR
//
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