ID Q0CPK1_ASPTN Unreviewed; 653 AA.
AC Q0CPK1;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 24-JAN-2024, entry version 77.
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=ATEG_04383 {ECO:0000313|EMBL:EAU34830.1};
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU34830.1, ECO:0000313|Proteomes:UP000007963};
RN [1] {ECO:0000313|Proteomes:UP000007963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476599; EAU34830.1; -; Genomic_DNA.
DR RefSeq; XP_001213561.1; XM_001213561.1.
DR AlphaFoldDB; Q0CPK1; -.
DR STRING; 341663.Q0CPK1; -.
DR EnsemblFungi; EAU34830; EAU34830; ATEG_04383.
DR GeneID; 4320195; -.
DR VEuPathDB; FungiDB:ATEG_04383; -.
DR eggNOG; KOG1037; Eukaryota.
DR HOGENOM; CLU_004841_2_0_1; -.
DR OMA; QGENDRF; -.
DR OrthoDB; 5481368at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
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 CDD; cd01437; parp_like; 1.
DR CDD; cd07997; WGR_PARP; 1.
DR Gene3D; 3.90.228.10; -; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 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; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
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; PF00533; BRCT; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF02877; PARP_reg; 1.
DR Pfam; PF05406; WGR; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM00773; WGR; 1.
DR SUPFAM; SSF56399; ADP-ribosylation; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF47587; Domain of poly(ADP-ribose) polymerase; 1.
DR SUPFAM; SSF142921; WGR domain-like; 1.
DR PROSITE; PS50172; BRCT; 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 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:UP000007963};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362114}.
FT DOMAIN 1..95
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 160..256
FT /note="WGR"
FT /evidence="ECO:0000259|PROSITE:PS51977"
FT DOMAIN 286..412
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000259|PROSITE:PS51060"
FT DOMAIN 421..653
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT REGION 95..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 653 AA; 73346 MW; 5D430D25A0B5454D CRC64;
MAGGLFQSFV IALSGTFSGY KQAEVRALIE SHGAKFSHSV TSDLTHLITT QREIDNKNSK
YKQATKVYNC NIVSLDWLIE SDKAKKPLPE KSYVLGADSK DSKSDAKDGD TEKPEKKKRT
LEEALEIEED GANKKPKDGQ KKGAKSVVVP VDDCCYLRSS HSVHIDDAGL IWDATLNQTV
SANNNNKFYR IQMLTNRSGS EFMTWTRWGR VGETGQYSLL GDGSFDKAMA EFKKKFKDKS
GLTWDNRLDP PKKGKYTFIE KNYEEEGEED EGAEEAEGAK DKPEVESVLP GPVQDLMSFI
FNKDHFLSAM ASMSYDAKKL PLGKLSKRTL RSGFQLLKDL SELMNNPTLA TTKYDTSIAE
ATAYLSDQYF TTIPHDFGRN RPPVLNSEQA IKRELELLEA LTDMEVANGI MKESRDADTI
HQLDRQFQSL NMREMTPLSR TSTEFKELEA YLQLSRGATH HIKYSVMNIF RIEREGENDR
FMSSKYAKLK NSNRRLLWHG SRSTNFGGIL SQGLRIAPPE APATGYMFGK GVYFADMSSK
SAGYCCHYSS ANMGLLLLCD VELGERMLEL VNGNYNADQD SKKQGMIATL GQGMSVPGGW
KDAGCVHPSL QGVSMPDMET PLDRNTGKCL QYNEYIVYDV AQIRQRYLFQ VKM
//
