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Database: UniProt
Entry: A0A1S3I9Y7_LINUN
LinkDB: A0A1S3I9Y7_LINUN
Original site: A0A1S3I9Y7_LINUN 
ID   A0A1S3I9Y7_LINUN        Unreviewed;       721 AA.
AC   A0A1S3I9Y7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=LOC106161740 {ECO:0000313|RefSeq:XP_013394219.1};
OS   Lingula unguis.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC   Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX   NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013394219.1};
RN   [1] {ECO:0000313|RefSeq:XP_013394219.1}
RP   IDENTIFICATION.
RC   TISSUE=Gonads {ECO:0000313|RefSeq:XP_013394219.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_013394219.1; XM_013538765.1.
DR   AlphaFoldDB; A0A1S3I9Y7; -.
DR   EnsemblMetazoa; XM_013538765.1; XP_013394219.1; LOC106161740.
DR   GeneID; 106161740; -.
DR   KEGG; lak:106161740; -.
DR   InParanoid; A0A1S3I9Y7; -.
DR   OrthoDB; 2960371at2759; -.
DR   Proteomes; UP000085678; Unplaced.
DR   GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd01439; TCCD_inducible_PARP_like; 1.
DR   Gene3D; 3.30.720.50; -; 1.
DR   Gene3D; 3.90.228.10; -; 1.
DR   Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 2.
DR   InterPro; IPR002589; Macro_dom.
DR   InterPro; IPR043472; Macro_dom-like.
DR   InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR   InterPro; IPR004170; WWE-dom.
DR   InterPro; IPR037197; WWE_dom_sf.
DR   PANTHER; PTHR14453; PARP/ZINC FINGER CCCH TYPE DOMAIN CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR14453:SF67; POLY [ADP-RIBOSE] POLYMERASE; 1.
DR   Pfam; PF01661; Macro; 2.
DR   Pfam; PF00644; PARP; 1.
DR   SMART; SM00506; A1pp; 1.
DR   SUPFAM; SSF56399; ADP-ribosylation; 1.
DR   SUPFAM; SSF52949; Macro domain-like; 2.
DR   SUPFAM; SSF117839; WWE domain; 1.
DR   PROSITE; PS51154; MACRO; 2.
DR   PROSITE; PS51059; PARP_CATALYTIC; 1.
DR   PROSITE; PS50918; WWE; 1.
PE   4: Predicted;
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU362114};
KW   NAD {ECO:0000256|RuleBase:RU362114};
KW   Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW   Transferase {ECO:0000256|RuleBase:RU362114}.
FT   DOMAIN          1..115
FT                   /note="Macro"
FT                   /evidence="ECO:0000259|PROSITE:PS51154"
FT   DOMAIN          137..310
FT                   /note="Macro"
FT                   /evidence="ECO:0000259|PROSITE:PS51154"
FT   DOMAIN          430..511
FT                   /note="WWE"
FT                   /evidence="ECO:0000259|PROSITE:PS50918"
FT   DOMAIN          519..721
FT                   /note="PARP catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51059"
SQ   SEQUENCE   721 AA;  80894 MW;  E5070B8DA92CBED0 CRC64;
     MSTGEMKKTD GFNLQCQKIY HVVCPDWGPA KEQTLSRLMS QCLEQAHQDG VSSIAFPALG
     TGNLKFPKDV VADVMFKEAL QFSAKNSQTK VKEIRFVLYP QDTQTITAFK MKLFEVQGRP
     KTVHFRRRKG ITMQLEKPNF MELSCNAVTV QVKQGNVMED TVDIIVNTVD PQLNMGVLGK
     HLVKAGGNDI KKELQTKKRH AQNGAVLDTT PGKLPFKRIY HVVIPPANQI HRSIQQCLLL
     AEKFGFSSIA FPAIGTGKAN LDPANCAKET LSGIFQTLQE NNIESLKMIC VTVYDQGQIP
     IFIDEARAQS TVTGRTRKGR RQSMRQRQSL TALQRVVLDV YGASDKVAET DEDIAAFIKQ
     NIQKETIELK GHTITQADIA EIRDLEVERG VTATIDTNTS TISIVGCPVD VSPTVSTIYK
     IIHKKIEDRA EEDKAAALQQ KIQWCWLAAK DQSREPFDKM TNYRVELAHR AREGSVVYEI
     EGSPCKLDFS TMTETDCSND IVTQVIREVK DPSLPSHWSP QPRDSDIPHA VHQVNIKAGD
     QEFNKVAEQF NAAFDTDGVR RKKIVQLLRI QNPHLYKQYK TYSAKLEREN QGMNNEMSLF
     HGTSEANCDY ISHQGFNRSF GGLNVGAIFG KGVYFAKKAT YSAQPCYCKP NAAGEQFMFL
     AKVLVGSYTK GHRKMLTPPP KDPDKPLETY NSVVDNTKTP TIFVIFYDAQ AYPEYLIKFK
     A
//
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