ID A0A1S3PF58_SALSA Unreviewed; 1255 AA.
AC A0A1S3PF58;
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=LOC106585077 {ECO:0000313|RefSeq:XP_014026333.1};
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_014026333.1};
RN [1] {ECO:0000313|RefSeq:XP_014026333.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014026333.1};
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_014026333.1; XM_014170858.1.
DR AlphaFoldDB; A0A1S3PF58; -.
DR STRING; 8030.ENSSSAP00000120172; -.
DR PaxDb; 8030-ENSSSAP00000120172; -.
DR Ensembl; ENSSSAT00000155545; ENSSSAP00000120201; ENSSSAG00000081399.
DR GeneID; 106585077; -.
DR OrthoDB; 5477658at2759; -.
DR Proteomes; UP000087266; Chromosome ssa24.
DR Bgee; ENSSSAG00000081399; Expressed in testis and 14 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:SF33; ANKYRIN 2, ISOFORM U; 1.
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; 2.
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 142..174
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 175..207
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 208..240
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 295..327
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 328..360
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 361..393
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 448..483
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 484..516
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 517..549
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 610..642
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 643..675
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 676..708
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 763..795
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 796..828
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 829..861
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 958..1017
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 1040..1245
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT REGION 1..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1255 AA; 135007 MW; 20C5212705B0E4BF CRC64;
MAVSRRSSQQ QQQGNLQSPP RNSSLSVSPP DSLPIDLVTA TSVPPDGERG CSAGMENPSG
SPDLPAPALS TGSSTSPTTT TSGGESSSVS SPGSGGTSPG DGSSGIGGAF RDLFEACRNG
DVSRVKRLVD SVNVNAKDMA GRKSTPLHFA AGFGRKDVVE HLLQTGANVH ARDDGGLIPL
HNACSFGHAE VVSLLLCQGA DPNARDNWNY TPLHEAAIKG KIDVCIVLLQ HGADPNIRNT
DGKSALDLAD PSAKAVLTGE YKKDELLEAA RSGNEEKLMA LLTPLNVNCH ASDGRKSTPL
HLAAGYNRVR IVQLLLQHGA DVHAKDKGGL VPLHNACSYG HFEVTELLLK HGACVNAMDL
WQFTPLHEAA SKNRVEVCSL LLSHGADPNL LNCHSKSAVD LAPTPELKER LTYEFKGHSL
LQAAREADMA KVKKTLALEI ISFKHPQTNE TALHCAVASP HPKRKQVTEL LLRKGANVNE
KNKDFMTTLH VAAERAHNDI LEVLQKHGAK VNAVDTLGQT ALHRAALAGH IQTCRLLLSY
GADPAIVSLQ GFTASQMGNE AVQQILNENI PTRNSDVDYR FLEAAKAGDL DTVQQLCTPQ
NVNCRDLEGR HSTPLHFAAG YNRVAVVEYL LHHGADVHAK DKGGLVPLHN ACSYGHYEVA
ELLVRHGASV NVADLWKFTP LHEAAAKGKY EICKLLLKHG ADPTKKNRDG NMPLDMVKDG
DTDIQDLLRG DAALLDAAKK GCLARVQKLC SPENINCRDT QGRNSTPLHL AAGYNNLEVA
EYLLEHGADV NAQDKGGLIP LHNAASYGHV DIAALLIKFN TCVNATDKWA FTPLHEAAQK
GRTQLCALLL AHGADPTMKN QEGQTALDLA TADDIRALLM DAMPPDALPS CFKPQATVVS
AGSVISPAST PSCLSAASSI DNLAGPLNEL GAAGTSGVAD GAAGSDRKEG ELAMLDMNIG
QFLKSLGLEH IREIFEREQI SLDVLADMGH EELKEIGINA YGHRHKLIKG VERLLGGQQG
ANPYLTFHCA NQGTVLIDLA PDDKEGQSVE EEMQSSIREH RDGGNAGGVF SRYNIIKIQK
VVNKKLRERY THRQKEISDE NHNHHNERML FHGSPFINAI IHKGFDERHA YIGGMFGAGI
YFAENSSKSN QYVYGIGGGT GCPTHKDRSC YLCHRQMLFC RVTLGKSFLQ FSAMKMAHAP
PGHHSVIGRP SVNGLAYAEY VIYRGEQAYP EYLITYQILK PESTAASAAG AEQKS
//
