ID H3A4L8_LATCH Unreviewed; 502 AA.
AC H3A4L8;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
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 Name=PARP2 {ECO:0000313|Ensembl:ENSLACP00000004589.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000004589.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000004589.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-
CC ribosyl)n+1-acceptor + H(+).; EC=2.4.2.30;
CC Evidence={ECO:0000256|ARBA:ARBA00033987};
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; AFYH01238634; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01238635; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01238636; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01238637; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01238638; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01238639; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01238640; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01238641; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3A4L8; -.
DR STRING; 7897.ENSLACP00000004589; -.
DR Ensembl; ENSLACT00000004628.1; ENSLACP00000004589.1; ENSLACG00000004086.1.
DR eggNOG; KOG1037; Eukaryota.
DR GeneTree; ENSGT00940000158452; -.
DR HOGENOM; CLU_004841_2_2_1; -.
DR InParanoid; H3A4L8; -.
DR OMA; QGENDRF; -.
DR TreeFam; TF315407; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000004086; Expressed in post-anal tail muscle and 6 other cell types or tissues.
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 CDD; cd08003; WGR_PARP2_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:SF60; POLY [ADP-RIBOSE] POLYMERASE 2; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF02877; PARP_reg; 1.
DR Pfam; PF05406; WGR; 1.
DR SMART; SM00773; WGR; 1.
DR SUPFAM; SSF56399; ADP-ribosylation; 1.
DR SUPFAM; SSF47587; Domain of poly(ADP-ribose) polymerase; 1.
DR SUPFAM; SSF142921; WGR domain-like; 1.
DR PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS51977; WGR; 1.
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:UP000008672};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362114}.
FT DOMAIN 17..114
FT /note="WGR"
FT /evidence="ECO:0000259|PROSITE:PS51977"
FT DOMAIN 145..262
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000259|PROSITE:PS51060"
FT DOMAIN 270..502
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
SQ SEQUENCE 502 AA; 57291 MW; 274CEF73A597739F CRC64;
MKGKAPVDPE CKAKLGKAHV YCEGEDIYDA MLNQTNLQFN NNKYYIIQLL EDDNQKSFSV
WMRWGRVGKT GQNSLVACER DLQKAKDVFK KKFLDKTKNE WDQRQVFEKV AGKYDLLQLE
YGSDTKKEEE ETETEQEAVK RAKLESKLDP RVQALISLIC DIKTMEEMIL EMKYDTKKAP
LGKLTTEQIK AGYQSLKKIE DCINRNVHGR ALVAACNEFY TRIPHDFGLR TPPLIRTKEE
LKEKLQLLEA LSDIEIAIKV VKSEQKSSEH PLDRQYHSLH CSLTPLEHSS QQFKVIEKYL
QSTHAKTHND YTMTLLDVFE VDKEGEKEAL RSDIENRGGE SRMLLWHGSR LTNWVGILSK
GLRIAPSEAP VTGYMFGKGI YFADMSSKSA NYCFASRQNS VGLLLLSEVV VGECNELLAA
NYEGDKLPPG KHSTKGLGKV APDPSKSITL EGVTVPMGPV KDTGVQNPDR YTLNYNEFIV
YNTNQVRMKY LLKLQFNFDT LW
//
