ID A0A498P270_LABRO Unreviewed; 1858 AA.
AC A0A498P270;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 22-FEB-2023, entry version 11.
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 ORFNames=ROHU_000870 {ECO:0000313|EMBL:RXN38720.1};
OS Labeo rohita (Indian major carp) (Cyprinus rohita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Labeo.
OX NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN38720.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN38720.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN38720.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN38720.1};
RA Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA Shah T.M., Rai A., Jena J.K.;
RT "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family.
CC {ECO:0000256|ARBA:ARBA00024347}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXN38720.1}.
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DR EMBL; QBIY01004557; RXN38720.1; -; Genomic_DNA.
DR STRING; 84645.A0A498P270; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:UniProtKB-UniRule.
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; 4.
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:SF67; POLY [ADP-RIBOSE] POLYMERASE; 1.
DR Pfam; PF01661; Macro; 4.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF02825; WWE; 1.
DR SMART; SM00506; A1pp; 4.
DR SUPFAM; SSF56399; ADP-ribosylation; 1.
DR SUPFAM; SSF52949; Macro domain-like; 4.
DR SUPFAM; SSF117839; WWE domain; 1.
DR PROSITE; PS51154; MACRO; 4.
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:UP000290572};
KW Transferase {ECO:0000256|RuleBase:RU362114}.
FT DOMAIN 721..906
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT DOMAIN 923..1102
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT DOMAIN 1101..1263
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT DOMAIN 1257..1431
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT DOMAIN 1568..1643
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 1655..1858
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
SQ SEQUENCE 1858 AA; 205911 MW; 1C3BA36DD13B0B92 CRC64;
MEEKSLIVEG LPDDFDRVES KIQLYFKNKR RSGGEIVQIR EHPDDKRKAL LIYMKDEDFK
EIFGQKEHEF DITLEVYKEG RLGEELDPRR FILTGFDGAT DCKMISVFIG SCSKKAEHTW
ETLDEDRIVV TFKHDIDVTS FLKKCTSKQL QGRDVGVTRL ERTDSVLVQG DLEQLAEDVL
TLYFSNKKRS GGGDVQSFIW INRRKSAVIT FGNCDEAHAV AEQKHNVCGT EVHASLFYSS
LQKALTGEKP TLTDQISTKV NLPVSEELLR FFETNERCRK QLESDAKLFH AKVLIDSTAA
ANELILEMDV NKESLAALQI APTWETKLTR EVQSFLSGYD AAELTAEKDV WTRVEHECNG
LVTLDTALSY REINSKVVIA GVREEVRVLS DKIRTLLKNT AVEVEVERNT IEVAIKLDCR
ETFDLIKERV ESKLGQVSLS HDDKQHIVSL KGLKDQVHSV EMLIRQAQKN IITHQLKLSS
HMIQFLKSLD LQKFEQDYFL PSHIPAILLN RQDFFGILVE KENLKRAEDK IHEILKEEFI
PLTLKKTDET WTHFFRNLQD EIESFQKAHD IRITQSDVQV IICGFSSAVA DVTGKVRRYL
DNKEPTTENV PLKSEREVEF VDSCLNLSEL PELKRFGATV LAYRTSNSPC LKITAAKDNI
KDAVSVVRQQ LTSIVVERHK YCKAGEAKVL EKHEANVKTK AKEMQCSLYL SQEHVVKSSP
AKSFTHKIGN FVTLSITEGD LHHFTADALT CPMNGNLAFS NPVAQRFLQF GGDKITEVCK
TQQKEQQSLL PGDVVLSDAG KLSAGKLIYA VMPQKGQRLD SHYLQSAVHN SLLKAEGKGC
ASIALPAIGC ESFGFSVKDS CMALRAAVLQ FCSDRQNSPK NIRRISIVDS DEKIVEEYNA
LIQELGFPDT STTVPLQPLK LKHGSDTRVL INGVPICLKK GDITKETADV IVNSTNKSLD
LNTGVSGAIL KAAGKTVVDE CKKQAPLKAG AAVMTGGGAL QCKYIAQMVG PDNAADITSS
LEQVLNLCEA KTATTLAIPV IGTGMTASRR GGFAPKESIK AILTAIEKHL AAPNSSYLQS
ITIVAFDHQT FDALLKIGSV RIEVKKGDIT NETVRGIVNT TNRDMSLRGG VSGAIFKAAG
ASVEQESQKH GPLQNDVAAV TSGGNLHCDF ILHMVGPHSA AEVRSRVKKV LERCEEKQIT
TVSFPAVGTG GGGVQGADAI CAMLQGFEDH LSQNVSTVVK LIYIVIDRDN VLQEFQKANP
VEVMLGPIKV KVFCGDITKE TVEAIVNSTT TSLDLNTGVS GAILKASGQT VVNECKSKAP
QPADGMILTK AGDLTNIKHI VHMVGQTTEN GISSSMFKVL RMCEENKIQS VSFPALGTGA
GNLAAAGVAN AMTEALTDFV KDSPKHLKRV HIVIFQTKLL PDFQEAVKKC KKISRNASAR
QVKPLQQPAI PVPTQQPAFC LAKETAAVSF PVMAVDVYGT SPTNLAKVKK LLDELVSEER
ISKDVQSSHV TDLLEADKKA IVALSRANQV SVLVTSSDTL TLSGKKDDVL DAVLKINGFI
QEARDREMRE GEVKRLRETL CWEVVRGERW ESLEPSISYD IELAFHRKQK SFQYQEKGET
YTVDFNDLKV TNSKRESCRI KRTLLGDSDT AIIHPPPTWT KMDGRDLEII TLKSDSAEYK
NIEAAFLTSS KHANVSPVQV QQIDRIQSQS QWQRYSVLKQ AVDKKYPKQT NERQLYHGTT
KDICQKINKN GFNRSFCGRN AVVHGEGTYF AKEAWYSCHD QYSNPDDKGL KYIYRARVVT
GSLCKSRGGM KEPDPINPAD PRAGLHDCAV DEPQNPFVFV VFCDAGAYPE YLITFKST
//