ID A0A3Q1JL24_ANATE Unreviewed; 1861 AA.
AC A0A3Q1JL24;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000015486.1, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000015486.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family.
CC {ECO:0000256|ARBA:ARBA00024347}.
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DR STRING; 64144.ENSATEP00000015486; -.
DR Ensembl; ENSATET00000015729.2; ENSATEP00000015486.1; ENSATEG00000010770.2.
DR GeneTree; ENSGT00940000154311; -.
DR InParanoid; A0A3Q1JL24; -.
DR OrthoDB; 5471082at2759; -.
DR Proteomes; UP000265040; Unplaced.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:UniProtKB-UniRule.
DR CDD; cd02903; Macro_BAL-like; 2.
DR CDD; cd01439; TCCD_inducible_PARP_like; 1.
DR Gene3D; 3.30.70.330; -; 2.
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; 3.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
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:SF88; POLY [ADP-RIBOSE] POLYMERASE; 1.
DR Pfam; PF01661; Macro; 3.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF02825; WWE; 1.
DR SMART; SM00506; A1pp; 3.
DR SUPFAM; SSF56399; ADP-ribosylation; 1.
DR SUPFAM; SSF52949; Macro domain-like; 3.
DR SUPFAM; SSF117839; WWE domain; 1.
DR PROSITE; PS51154; MACRO; 3.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS50918; WWE; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|RuleBase:RU362114};
KW NAD {ECO:0000256|RuleBase:RU362114};
KW Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW Transferase {ECO:0000256|RuleBase:RU362114}.
FT DOMAIN 839..1026
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT DOMAIN 1052..1237
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT DOMAIN 1262..1437
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT DOMAIN 1583..1661
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 1665..1861
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT REGION 161..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1861 AA; 206598 MW; D49EA6DFF0762F8B CRC64;
MADAYSFPVL VELEENDTPR LKNKLVKYFQ SKKSGGGDCE VDYEHGSRTA TLRFRTEEDQ
KNVCRRETHQ ISLDKGVLKM TVRLPADETT AQETSPEKFD KKSEPIIVKT IMAPPAEKKR
RVHAPQKFLE SNQERWSCLH ISSNTDIDIN LQGPAANVPV NNKQSSADEV TPAAEVQGDA
KHGDDDTPDE ELCSTMAVVG NINETLSQEF LEMLVENILR GLKASDSESL SQSYTLEIIP
HISSAVVTFQ SGKENTNFMT RCPENKTFKK NKLSVCSLEV TKKVLAEDIQ NLSEDIIRLY
FENEGGDVED IVLNQVEQSA IITFKEHQAV RNILKKNKHR IRQEEISVYP FYESLGIALY
GKDKPPLKLP ATISESIDDA MGRYLNRNQS ASATIHRDLA KHFCKADFTN QSTVYLSPVS
SLLHQKDAKV MIKEWRDTVK SAFAQAMSKF RSLKFHPDSE AWQESEEKLR QMLEKEDVDL
ISEKASGDLF VVGLVEQVNR LEKPLSEVLN KIAKRVRREK SSITQEIKMS PSTFHILCQD
GLQDKLLQVY PELKISFKKD CQDLTVTGLN DEIFAASKVM YDAMFALKRQ NLDIDQYVFD
LLKDEEQEEL TNTLLISNGI NAAFEISTHR VQLLAVSERD LSSAEGHLGR LLISHFIDVE
DSNVLQKPEW KHLVSQLEKA NSKSCRKIRI NTTGQQAVVS GHRESVMKVS EELDDFLKQN
AHVEEAVVVN HNAIVEYFKL DTSRLKTFQD RVVMSYRKDS ISLSGSRADV SNCKTLVEEL
VSSVFFESLK VAKAGAKKFF KDKESMYVNS LLSETHCLVQ LVDEISVGQD DLAHRQVPKP
VYQLQTPDGV EIAVCKADMC HYPVYAVVNS SNQDLNLNGG LGGALLKAAG PQLQDECDKV
INVRGPLKPG DCVLTNAGGQ LWCKKVIHAI GPKFDPAKPP KALALLRKAV KESLELAEMH
NIISVALPVI SRGQGFPLNL CAITIVKAAK EYCDEKFDDN TLKKIHFVNN DDGAVQAMEA
AVRQEFGNHG VSHSQQTPQT KAIKAPLGSD PNCLGQVKTK EGLEIILVKG NIENATTEVT
VNTVFEDLAL NRGAVSNAIL QEAGPTLQQL VKAKNASGIV GEIIVTDGCK LKSKQVFHAV
SPHWDKGQGT ADKILRGIFK DCMEKAENTG LTSISFPAIG TGNLRFPKDL VVNLMLDEIL
AFSSKKQPKH LKKVMIILYS GDAQTIQVFS KEFKKKFPNA TVIPVSASSP QSQGPFSKVT
SSSTMHETKM GSVAIQVVTG DITKETTDVI VNSSNESFSL KSGVSKAILD AAGQAVETEC
QNLVAAQSNP AMIMTQPGNL KCKKILHLVG QTDPVKIKNT VKDALQMCVK NTYTSVSFPA
IGTGQGSVQP GQVADAMLDA VIDVLNSNPS VPLKTIRIVI FQPPMLKDFY NSMEERAKIE
ASDTKEKGGF WGNIGSKIKS LFVGTADKPQ KEGDFVIEAL KVDPACFHIC GNSQTDVDSA
KKWINDLISK ELYSSNIQDN AIHSFSDADY KHLENIQKTL GVSIRTESKK GQASVTIEGL
SKDVLEGSNV IHEMLRKARD KQVLEKNIEL AGTVADWQYQ QQGFQFQSFD AMTNYNLEQA
LENNQKTVKV TIKGQDYTVT MPSGPATDSQ GRTLNIKRID KLKDDDIPEH WDAMPANTTC
QAITIKAGTG EYDEVQNLFK ASCNRTITKI ERIQNPGLWK SLQVKRRDME QRNGHGNNVR
RLFHGTCHTT VDWINEHGFN RSYAGRNATY YGNGTYFAVN ASYSAHDTYS KPNTNGEKFM
YLCQVLTGDF SLGQQGMIVP PEKSTGSVQK YDSVVDNMSK PSMFVIFHDS QACPEYLITF
K
//
