ID A0A091IFV3_CALAN Unreviewed; 1099 AA.
AC A0A091IFV3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, 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};
DE Flags: Fragment;
GN ORFNames=N300_07491 {ECO:0000313|EMBL:KFP07167.1};
OS Calypte anna (Anna's hummingbird) (Archilochus anna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC Trochilidae; Calypte.
OX NCBI_TaxID=9244 {ECO:0000313|EMBL:KFP07167.1, ECO:0000313|Proteomes:UP000054308};
RN [1] {ECO:0000313|EMBL:KFP07167.1, ECO:0000313|Proteomes:UP000054308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N300 {ECO:0000313|EMBL:KFP07167.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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 -!- SIMILARITY: Belongs to the ARTD/PARP family.
CC {ECO:0000256|ARBA:ARBA00024347}.
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DR EMBL; KL218641; KFP07167.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091IFV3; -.
DR STRING; 9244.A0A091IFV3; -.
DR Proteomes; UP000054308; 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; PTHR24189:SF66; M-PHASE PHOSPHOPROTEIN 8; 1.
DR PANTHER; PTHR24189; MYOTROPHIN; 1.
DR Pfam; PF00023; Ank; 2.
DR Pfam; PF12796; Ank_2; 6.
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; 13.
DR PROSITE; PS50088; ANK_REPEAT; 15.
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 Reference proteome {ECO:0000313|Proteomes:UP000054308};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU362114}.
FT REPEAT 1..23
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 24..56
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 57..89
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 144..176
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 177..209
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 210..242
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 297..332
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 333..365
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 366..398
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 459..491
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 492..524
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 612..644
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 645..677
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 DOMAIN 811..870
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 893..1098
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP07167.1"
FT NON_TER 1099
FT /evidence="ECO:0000313|EMBL:KFP07167.1"
SQ SEQUENCE 1099 AA; 119977 MW; 6B5AC214BDFE5B92 CRC64;
GFGRKDVVEY LLQSGANVHA RDDGGLIPLH NACSFGHAEV VNLLLRHGAD PNARDNWNYT
PLHEAAIKGK TDVCIVLLQH GAEPTIRNTD GRTALDLADP SAKAVLTGEY KKDELLESAR
SGNEEKMMSL LTPLNVNCHA SDGRKSTPLH LAAGYNRVKI VQLLLQHGAD VHAKDKGDLV
PLHNACSYGH YEVTELLVKH GACVNAMDLW QFTPLHEAAS KNRVEVCSLL LSYGADPTLL
NCHNKSTIDL APTPQLKERL AYEFKGHSLL QAARESDVAR IKKHLSLETV NFKHPQTHET
ALHCAAASPY PKRKQVCELL LRKGANINEK TKDFLTPLHV ASEKAHNDVV EVVVKHEAKV
NALDHLGQTS LHRAAYCGHL QTCRLLLSSG CDPSIVSLQG FTALQMGTES VQQLLQEGLP
LGNSDADRQL LEAAKAGDVD TVKKLCTVQS VNCRDIEGRQ STPLHFAAGY NRVSVVEYLL
QHGADVHAKD KGGLVPLHNA CSYGHYEVAE LLVKHGAVVN VADLWKFTPL HEAAAKGKYE
ICKLLLQHGA DPTKKNRDGN TPLDLVKDGD TDIQDLLRGD AALLDAAKKG CLARVKKLCS
PDNVNCRDTQ GRHSTPLHLA AGYNNLEVAE YLLQHGADVN AQDKGGLIPL HNAASYGHVD
VAALLIKYNA CVNATDKWAF TPLHEAAQKG RTQLCALLLA HGADPTLKNQ EGQTPLDLVT
ADDVSALLTA AMPPSALPTC YKPQVISVSQ TTGSTADSLS SVPSSPSSLS AASSLDNLSG
SFSELPSVVS TNSTEGATVL EKKEVSGVDF SINQFVRNLG LEHLIDIFER EQITLDVLVE
MGHKELKEIG INAYGHRHKI IKGVERLISG QQGLNPYLTL NTSGSGTILI DLSTEDKEFQ
SVEEEMQSTV REHRDGGHAG GVFNRYNILK IQKVCNKKLW ERYTHRRKEV SEENHNHANE
RMLFHGSPFV NAIIHKGFDE RHAYIGGMFG AGIYFAENSS KSNQYVYGIG GGTGCPIHKD
RSCYVCHRQL LFCRVTLGKS FLQFSAMKMA HSPPGHHSVT GRPSVNGLAL AEYVIYRGEQ
AYPEYLITYQ IMKPEATTE
//
