ID F4W9V3_ACREC Unreviewed; 1234 AA.
AC F4W9V3;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
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};
DE Flags: Fragment;
GN ORFNames=G5I_02261 {ECO:0000313|EMBL:EGI69089.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI69089.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GL888033; EGI69089.1; -; Genomic_DNA.
DR STRING; 103372.F4W9V3; -.
DR EnsemblMetazoa; XM_011070778.1; XP_011069080.1; LOC105154960.
DR eggNOG; KOG4177; Eukaryota.
DR InParanoid; F4W9V3; -.
DR Proteomes; UP000007755; 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; 5.
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; 5.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF07647; SAM_2; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 17.
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; 13.
DR PROSITE; PS50088; ANK_REPEAT; 14.
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:UP000007755};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU362114}.
FT REPEAT 38..70
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 71..103
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 104..136
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 191..223
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 224..256
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 260..289
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 344..379
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 380..412
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 507..539
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 540..572
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 573..605
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 660..692
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 693..725
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 726..758
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 870..933
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 953..1177
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT REGION 791..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1014..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1176..1196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..810
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EGI69089.1"
SQ SEQUENCE 1234 AA; 134282 MW; B30B43C33A67762E CRC64;
DGGDPLRELF EACKTGDLAK VKALVNPKTV NARDTAGRKS TPLHFAAGYG RKDVVEFLLS
AGASIQARDD GGLHPLHNAC SFGHCDVVRL LLEAGASPNT RDNWNFTPLH EAAIKGKIDV
CITLLQHGAD VNIRNTEGKT ALEVADVSTK PVLTGEYRKD ELLEAARSGN EERLLQLLNP
LNVNCHASDG RRSTPLHLAA GYNRSRVVQI LLQNGADVHA KDKGGLVPLH NACSYGHFEV
TEALLKHGAA VNASDLWTFT PLHEAASKSR AEVCSLLLSE GADPTQLNCH SKSAIDVAPT
LELQERLAYE YKGHCLLDAC RQADLTKLKK YLSQEIVNFK HPYTGDTPMH CAVASPYPKR
KQVIEALIRK NAAMNEKNKD FLTPLHVATD HSHYDAMDIL LRHNAKVNAL DGLGQTALHR
CAREDNVQAC RILLSYNIDP SIISLQGYTA AQISAENVLK ILQDPPNGTD DVEAQLLEAS
KSGDLAAVER ILQANPHTVN CRDLDGRHST PLHFAAGFNR VPVVEYLLAH GADVHAKDKG
GLVPLHNACS YGHYEVTELL VKHGASVNVA DLWKFTPLHE AAAKGKYEIV RLLLRHGADA
TKKNRDGATP LDLVRDGDQD VADLLRGNSA LLDAAKKGNL ARVQRLVTQD NINCRDAQGR
NSTPLHLAAG YNNLEVAEFL LERGADVNAQ DKGGLIPLHN ASSYGHLDIA ALLIKYNTVV
NATDKWGFTP LHEAAQKGRT QLCALLLAHG ADPFLKNQEG QTPVDLASAD DVRCLLQDAM
ASQQIVPTVP SGNMVNSAGG NSISSRPPSI VSVPVTPPPP LTQETVIMPS GAAMTLCVPL
ARPTSCLSPM PPSEPCSEKE SKDICKEHNS TITTVAGFLQ SLGLEHLLEL FEREQITLDI
LAEMGHEDLK QVGVSAYGYR HKLIKGMDKL LNTATGSLWQ PSINPGTLLV DLLTEDKEFL
AVEEEMQSTI RQHRDNGHSG GIFSRYNIVR IQKVQNRKLW ERYAHRRQEV AEEVGAAAPA
SPSTGPRGVP SSTVSQANER MLFHGSPFIN AIVQKGFDER HAYIGGMFGA GIYFAEHSSK
SNQYVYGICG GTGCPAHKDR SCYICHRHLL LCRVTLGKSF LQFSAMKMAH APPGHHSVMG
RPSQGGLVFP EYVVYRGEQA YPEYLITYQI ARPQQASGGR DGGAERGSEX XXXXXXXXXX
XXXXXXRNES VRAARVRSLC CCQRPRTCGA LSRT
//
