ID A0A0J7KX10_LASNI Unreviewed; 1162 AA.
AC A0A0J7KX10;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=RF55_5021 {ECO:0000313|EMBL:KMQ94809.1};
OS Lasius niger (Black garden ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Lasius; Lasius.
OX NCBI_TaxID=67767 {ECO:0000313|EMBL:KMQ94809.1, ECO:0000313|Proteomes:UP000036403};
RN [1] {ECO:0000313|EMBL:KMQ94809.1, ECO:0000313|Proteomes:UP000036403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole {ECO:0000313|EMBL:KMQ94809.1};
RA Konorov E.A., Nikitin M.A., Kirill M.V., Chang P.;
RT "Lasius niger genome sequencing.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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:KMQ94809.1}.
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DR EMBL; LBMM01002452; KMQ94809.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J7KX10; -.
DR STRING; 67767.A0A0J7KX10; -.
DR PaxDb; 67767-A0A0J7KX10; -.
DR OrthoDB; 5477658at2759; -.
DR Proteomes; UP000036403; Unassembled WGS sequence.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd09524; SAM_tankyrase1_2; 1.
DR CDD; cd01438; tankyrase_like; 1.
DR Gene3D; 3.90.228.10; -; 1.
DR Gene3D; 6.20.320.10; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 6.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR24123; ANKYRIN REPEAT-CONTAINING; 1.
DR Pfam; PF00023; Ank; 3.
DR Pfam; PF12796; Ank_2; 4.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF07647; SAM_2; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 15.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF56399; ADP-ribosylation; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 3.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 11.
DR PROSITE; PS50088; ANK_REPEAT; 12.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Glycosyltransferase {ECO:0000256|RuleBase:RU362114};
KW NAD {ECO:0000256|RuleBase:RU362114};
KW Reference proteome {ECO:0000313|Proteomes:UP000036403};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU362114}.
FT REPEAT 65..97
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 98..130
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 131..163
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 218..250
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 251..283
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 287..316
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 371..406
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 407..439
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 534..566
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 567..599
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 600..632
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 702..734
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 846..909
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 929..1153
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 988..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1162 AA; 125835 MW; C28F89C8C381DFC6 CRC64;
MAGRRSTLTT NAVDSLPGSG GGGGGGGGGG DPLRELFEAC KTGDLVKVKA LVTPKTVNAR
DTAGRKSTPL HFAAGYGRKD VVEFLLSAGA SIQARDDGGL HPLHNACSFG HCDVVRLLLD
AGASPNTRDN WNFTPLHEAA IKGKIDVCIT LLQHGADVNI RNTEGKTALE VADASTKSVL
TGEYRKDELL EAARSGNEER LLQLLNPLNV NCHASDGRRS TPLHLAAGYN RSRVVQILLQ
NGADVHAKDK GGLVPLHNAC SYGHFEVTEA LLKHGAAVNA SDLWTFTPLH EAASKSRAEV
CSLLLSEGAD PTQLNCHSKS AIDVAPTLEL QERLAYEYKG HCLLDACRQA DLTKLKKYLS
QEVVNFKHPY TGDTPMHCAV ASPYPKRKQV IETLIRKNAA MNEKNKDFLT PLHVATDHSH
YDAMDILLRH NAKVNALDGL GQTALHRCAR EDNVQACRIL LSYNVDPSIV SLQGYTAAQI
AAENVLKILQ DPPNGTDDVE AQLLEASKSG DLAAVERILQ VNPHAVNCRD LDGRHSTPLH
FAAGFNRVPV VEYLLAHGAD VHAKDKGGLV PLHNACSYGH YEVTELLVKH GASVNVADLW
KFTPLHEAAA KGKYEIVRLL LRHGADATKK NRDGATPLDL VRDGDQDVAD LLRGNSALLD
AAKKGNLARV QRLVTQDNIN CRDAQGRNST PLHLAVNATD KWGFTPLHEA AQKGRTQLCA
LLLAHGADPF LKNQEGQTPV DLASADDVRC LLQDAMASQQ IVPSVPSGNM VNSTGGNPVN
SRPPSIVSVP VTPPPPLTQE TVIMPSGAAM TLCVPLARPT SCLSPMPPSE PCSEKESKDL
CKEHNGSITT VAGFLQSLGL EHLLELFERE QITLDILAEM GHEDLKQVGV SAYGYRHKLI
KGMDKLLNTA AGSLWQPSIN PGTLLVDLLA EDKEFLAVEE EMQSTIRQHR DNGHSGGIFS
RYNIVRIQKV QNRKLWERYA HRRQEVAEEV GAAAPASPGT GPRGTSSSTV SQANERMLFH
GSPFINAIVQ KGFDERHAYI GGMFGAGIYF AEHSSKSNQY VYGICGGTGC PAHKDRSCYI
CHRHLLLCRV TLGKSFLQFS AMKMAHAPPG HHSVMGRPSQ GGLVFPEYVV YRGEQAYPEY
LITYQIARPQ QESGSNEGVE ER
//
