ID A0A1S3NP82_SALSA Unreviewed; 1260 AA.
AC A0A1S3NP82;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
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 Name=LOC106580453 {ECO:0000313|RefSeq:XP_014017011.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014017011.1};
RN [1] {ECO:0000313|RefSeq:XP_014017011.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014017011.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family.
CC {ECO:0000256|ARBA:ARBA00024347}.
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DR RefSeq; XP_014017011.1; XM_014161536.1.
DR AlphaFoldDB; A0A1S3NP82; -.
DR STRING; 8030.ENSSSAP00000071442; -.
DR PaxDb; 8030-ENSSSAP00000071442; -.
DR Ensembl; ENSSSAT00000104314; ENSSSAP00000071140; ENSSSAG00000062901.
DR GeneID; 106580453; -.
DR OMA; TAETINC; -.
DR OrthoDB; 5477658at2759; -.
DR Proteomes; UP000087266; Chromosome ssa20.
DR Bgee; ENSSSAG00000062901; Expressed in brain and 15 other cell types or tissues.
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; 1.
DR Pfam; PF12796; Ank_2; 5.
DR Pfam; PF13606; Ank_3; 1.
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; 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; 15.
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}; Glycosyltransferase {ECO:0000256|RuleBase:RU362114};
KW NAD {ECO:0000256|RuleBase:RU362114};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU362114}.
FT REPEAT 140..172
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 173..205
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 206..238
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 300..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 453..488
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 489..521
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 522..554
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 615..647
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 648..680
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 681..713
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 768..800
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 801..833
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 834..866
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 963..1022
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 1045..1250
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1260 AA; 135666 MW; 03CC221136AB59C6 CRC64;
MAVSRRSSQQ QQGNLLSPPR NGSLSVSPPG SPSLNLVTAT LVPPDGERGC STGMENPLAS
PDLQTSALSS GSSTSPTTTT SGGGSSSVSS PGSGGTTPGD GSGIGGAFRE LFEACRNGDV
SRVKRLVDSV NVNAKDMAGR KSTPLHFAAG FGRKDVVDHL LQTGANVHAR DDGGLIPLHN
ACSFGHAEVV SLLLCQGADP NARDNWNYTP LHEAAIKGKI DVCIVLLQHG ADPNIRNTDG
KSALDLADPS AKAVLTGEYK KDELLEAARS GNEEKLMALL TPLNVNCHAS DGRKSTSQKM
LSTPLHLAAG YNRVRIVQLL LQHGADVHAK DKGGLVPLHN ACSYGHFEVT ELLLKHGACV
NAMDLWQFTP LHEAASKNRV EVCSLLLSHG ADPTLLNCHS KSAVDMAPTP ELKERLTYEF
KGHSLLQAAR EADMAKVKKT LALEIISFKH PQTNETALHC AVASPHPKRK QVTELLLRKG
ANINEKNKDF MTALHVASER AHNDILEVLQ KHGAKVNAVD TLGQTALHRA ALAGHIQTCR
LLLSYGADPA IVSLQGFTAS QMGNEAVQQI LNENVPTRNS DVDYRFLEAA KAGDLDTVQQ
LCTPQNVNCR DLEGRHSTPL HFAAGYNRVA VVEYLLHHGA DVHAKDKGGL VPLHNACSYG
HYEVAELLVR HGASVNVADL WKFTPLHEAA AKGKYEICKL LLKHGADPTK KNRDGNMPLD
MVKDGDTDIQ DLLRGDAALL DAAKKGCLAR VQKLCSPENI NCRDTQGRNS TPLHLAAGYN
NLEVAEYLLE HGADVNAQDK GGLIPLHNAA SYGHVDIAAL LIKFNTCVNA TDKWAFTPLH
EAAQKGRTQL CALLLAHGAD PTMKNQEGQT ALDLATADDI RALLMDAMPP DALPSCFKPQ
ATVVSAGSVI SPASTPSCLS AASSIDNLAG PLNELGAAGT SGVADGATGS DRKEGELVML
DMNISQFLKS LGLEHLRDIF EREQISLDVL ADMGHEELKE IGINAYGHRH KLIKGVERLL
GGQQGANPYL TFHCANQGTV LIDLAPDDKE GQSVEEEMQS TIREHRDGGN AGGVFSRYNI
IKIQKVVNKK LRERYTHRQK EISDENHNHH NERMLFHGSP FINAIIHKGF DERHAYIGGM
FGAGIYFAEN SSKSNQYVYG IGGGTGCPTH KDRSCYLCHR QMLFCRVTLG KSFLQFSAMK
MAHAPPGHHS VIGRPSVNGL AYAEYVIYRG EQAYPEYLIT YQILKPESTA TSAAGEDQKS
//
