ID D2V206_NAEGR Unreviewed; 1569 AA.
AC D2V206;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
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=NAEGRDRAFT_56841 {ECO:0000313|EMBL:EFC49403.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC49403.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC49403.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
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DR EMBL; GG738848; EFC49403.1; -; Genomic_DNA.
DR RefSeq; XP_002682147.1; XM_002682101.1.
DR STRING; 5762.D2V206; -.
DR EnsemblProtists; EFC49403; EFC49403; NAEGRDRAFT_56841.
DR GeneID; 8862571; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_56841; -.
DR eggNOG; KOG0198; Eukaryota.
DR eggNOG; KOG4177; Eukaryota.
DR InParanoid; D2V206; -.
DR OMA; CETENHE; -.
DR OrthoDB; 5490222at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00180; PKc; 1.
DR Gene3D; 3.90.228.10; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR45740; POLY [ADP-RIBOSE] POLYMERASE; 1.
DR PANTHER; PTHR45740:SF2; POLY [ADP-RIBOSE] POLYMERASE; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56399; ADP-ribosylation; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF140860; Pseudo ankyrin repeat-like; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU362114};
KW Kinase {ECO:0000313|EMBL:EFC49403.1}; NAD {ECO:0000256|RuleBase:RU362114};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW Transferase {ECO:0000256|RuleBase:RU362114}.
FT DOMAIN 963..1217
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1369..1569
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT COILED 522..582
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 856..883
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 907..934
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1228..1315
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1569 AA; 180972 MW; 0F4E013F3B16E8C0 CRC64;
MEPLQIYRQP NLNQTPHSLM LGCGQLTTTQ PSTIFGNSLL DNRGDVTIIN NATREGNPNP
LLHTRKLSKH LSFVKTPPTE DSQQLLIAPN TTIPNIGNST NVQDPQNNRP PLQIPPKSAS
ITNIENKKKN LNVQIPPVEN NHFSIMKVSS HSAAASNATS ACSSVSSSPS TISTSSTNLS
IGSSAINKLN QQSHTIESGL IENMTSKKKR GTTRENIILL DSILRERRDI FYAILNNVTK
IRLYRKKRRN PTHNNRSMTT ANTTMMHTQT MTSPKEEFGN EYIVKLNNGL KCEAFETSTA
QEFETYGHKR QFKASMYYTQ NEMDRLENQS MMDPSPLLRE DKLSFLDQLH GLHKPSVQSY
RVIDLIHPYH LFSTELEIIE PKSGRDLGRV MKKSYSLRTQ YLIQTVEGVK KQANGNLSSH
DKYKYATLFI ITKHKSNGKK EEPSEKHVLD QFQVRNIEGE NVATITHKFN SDYELKGYTP
DYIKFTPLFI ACQKGNLEIV KLLLASPNIV VDNNLKINGK SISIIKQEVD KLEKERIEKE
RITKEMLEKK RLEKERADQI RFEQERIENE RLEQERIEKE KKQTFLSVFQ VFTELCSLNE
KVSQYRKQVT SQLNSVIPLS DQLSFDTELQ QVYSKINGVL SECCSTINDR LMNNKCDIEN
VEHVALINND MLNITNIVER INSENYLIQL NSYIQALDEK LQIFDEFVQN YLNQDQLQYY
NANDNLNKEL TIEKIQKTLK SLNGSTTDSN YEGKSKNVLQ NISTQLQNIA SSINNATSVN
LNGIANNLEI AMEMLSKEEL ELQKAISNTK NLLPELVQIG IYQIYCDYQN QFNNGNKLIQ
ETIPFIIEQH EQLQNIVNIM NDYKQLTEQY SALQRKKARV TRELTIIKLD IDGLRDELVH
VTNKTESMQI EDEIKEKETT LQEKKKVLKE CIEQTNEIKL KFLQLKTIGF NVESILSSSI
ASTMNIEEMS ADLFKEIKPI QDWNGNHHLF IGTDINDKKH IIKQYSIKDN KKLESLQKEL
KITKKLKHNN IIEIEGFYMS NDNSHSTNNV YIVMPYYSNG NLKEFLEKQR KSTKLEVLFW
ERTWRQVLIA IQHIHSRGVI HCDIKPENIF VGECNNGLYP IILGDFDVSL DVQSRTMNLY
TRTSVSGTYD YLSPELMNGQ SATFKSDMFA FGKTIKNCMT AQELNTYSSL NTLVQQCMTN
DPNDRPFASD ALVCEFFLKD TLLDEIKVQE QVKSISNQSK QLKEYEKQLN QVKFNLKQDK
SNLTQEIKKL EQKTKEFTNQ SVKEREEITN QISRLKSKEK KLQDMEKELE ESKSRQLNIV
LPSYWKRNTF TSYSKRFYIV DVTKYLKNTI QDIVNVSCNS ATLGTGRDQQ VKMNYSKLIV
SSVSRIENAT LFTSYKSRMN HLTSYQDPIK TIQVQTELLP KTSKSYEWMK TVGLNSGMNE
KYLWHGTKPE FVSTISEHGF DERVASLGGL FGAGVYFAEY CSKSDQYCTP DLNKEYTIFL
CRVVLGRQVY FTPQGMTNQR RPPEIVGKNR RVFDSVIGQS NTTSNSYREL IVYDRYQCYP
EYIIKYKRQ
//
