ID A0A182Q4E3_9DIPT Unreviewed; 1538 AA.
AC A0A182Q4E3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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};
OS Anopheles farauti.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=69004 {ECO:0000313|EnsemblMetazoa:AFAF002853-PA, ECO:0000313|Proteomes:UP000075886};
RN [1] {ECO:0000313|Proteomes:UP000075886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FAR1 {ECO:0000313|Proteomes:UP000075886};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles farauti FAR1 (V2).";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AFAF002853-PA}
RP IDENTIFICATION.
RC STRAIN=FAR1 {ECO:0000313|EnsemblMetazoa:AFAF002853-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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 -!- SIMILARITY: Belongs to the ARTD/PARP family.
CC {ECO:0000256|ARBA:ARBA00024347}.
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DR EMBL; AXCN02000193; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 69004.A0A182Q4E3; -.
DR EnsemblMetazoa; AFAF002853-RA; AFAF002853-PA; AFAF002853.
DR VEuPathDB; VectorBase:AFAF002853; -.
DR OrthoDB; 5477658at2759; -.
DR Proteomes; UP000075886; Unassembled WGS sequence.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:UniProtKB-UniRule.
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; PTHR24189:SF66; M-PHASE PHOSPHOPROTEIN 8; 1.
DR PANTHER; PTHR24189; MYOTROPHIN; 1.
DR Pfam; PF00023; Ank; 4.
DR Pfam; PF12796; Ank_2; 4.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF07647; SAM_2; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 16.
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 3: Inferred from homology;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU362114}; NAD {ECO:0000256|RuleBase:RU362114};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU362114}.
FT REPEAT 56..88
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 89..121
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 122..154
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 209..241
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 242..274
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 275..307
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 362..397
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 398..430
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 525..557
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 558..590
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 591..623
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 678..710
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 711..743
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 744..776
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 893..952
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 969..1175
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT REGION 1262..1340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1368..1387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1424..1497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1265..1284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1368..1382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1432..1465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1466..1480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1481..1497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1538 AA; 163632 MW; 74E7889EE5745D9E CRC64;
MSANRSRSML SVNLEAAAMA NDPLRELFEA CKTGDLTKVK KLITPQTVNA RDTAGRKSTP
LHFAAGYGRR DVVEFLLANG ASIQARDDGG LHPLHNACSF GHADVVRLLL EAGANPNTRD
NWNYTPLHEA ASKGKIDVCI ALLQHGADPS IRNSENKIPL DLADPCTRPV LTGEYRKDEL
LEAARSGSEE RLLELLTPLN VNCHASDGRK STPLHLAAGY NRIRVVQILL QHGADVHAKD
KGGLVPLHNA CSYGHFEVTE LLIKHGGNVN ANDLWAFTPL HEAASKSRVE VCSLLLSEGA
DPTLLNCHNK SAIDSAPTRE LQEKIAYEYK GHCVLDACRQ ADIQRLKKNL TTETVNFVHP
YTGDTPVHAV AQSVYPKRKQ VLEVLIRKGA LLNEKNKDFL TPLHIAADNS HYELMDVLLR
HGAKVDALDG LGQTALHRCA REDNIQACRL LLSYAIDTGI VSLQGYTAAQ LATENVLKIL
QDPPSDTVDL ECQLLEAAKA GDLDTVRRIV LSSPMTVNCR DLDGRHSTPL HFAAGYNRVP
VVEFLLEHGA EVHASDKGGL VPLHNACSYG HYEVTELLVK HGANVNVADL WKFTPLHEAA
AKGKYEIVKL LIKHGADVTK KNRDGATPLD LVREGDQDVA DLLRGNAALL DAAKKGNLAR
VQRLVSSDNI NCRDAQGRNS TPLHLAAGYN NLEVAEYLLE HGADVNAQDK GGLIPLHNAS
SYGHLDIAAL LIKHNTVVNA TDKWGYTPLH EAAQKGRTQL CSLLLAHGAD PFMKNQEGQT
SLDLATAEDV KCLLQDAMVA SQGTAAGGGP SGGSSQQGAG ILAANGALLA TSCSPTTETV
TLPTGASMTL SVPVPQLPIR SCLSPAQGAE ANVDGIVVDH DDKMPSVPSI ESSVSVFLTS
LQLEHLIDLF EREQITMDIL AEMGHEDLKQ VGVSAYGFRH KILKGIATLR ATTGLGLTPN
PGTLLVDLLP DDKEFLAVEE EMQATIREHR DNGHSGGYFN RYNIVRIQKV QNRKLWERYV
HRRQEISEEN GHQASERMLF HGSPFINAIV QKGFDERHAY IGGMFGAGIY FAEHSSKSNQ
YVYGIGGGIG CPTHKDKSCY QCHRQLLLCR VALGKSFLQF SAMKMAHAPP GHHSVIGRPS
AGGLHFPEYV VYRGEQNNNI LVSVGGGVGG GGGVVSAATG GTSGSNSAGG SGGTVGVGLI
AGGNDGGSGG TATTGTGGSN FTRIRSTTRS TMAKATAVRV STGKKFSQLL IITPAVAIDS
TEQDDYHGPF NSSSLDSGCG GSSEGSLSDD GLIDENEQQQ RRRRRQQSSG GGGGASVVVG
DRRNNNGTLG GPLLGGGRRD TGATTGSWRW CGLICSAVKC FRAAAATTTG SRRSQQGGGA
SLRQPLAGTA VRYTTTEGDG GAAGTRRPGV ARFSSNHVYE YTIKSYRQPS REQRRTNGGA
GTVTLPVTAT GGGSRSGSIS SDSSVLAETD HDHINNNDDD DGDNGAGTSN GNIPSLLQNA
SGTTALIVTA SGCSSGSSSP TIETTARLPD RNAIMYKL
//
