ID C3YS03_BRAFL Unreviewed; 2671 AA.
AC C3YS03;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE RecName: Full=Poly [ADP-ribose] polymerase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BRAFLDRAFT_75823 {ECO:0000313|EMBL:EEN56908.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN56908.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN56908.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN56908.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG666548; EEN56908.1; -; Genomic_DNA.
DR RefSeq; XP_002600896.1; XM_002600850.1.
DR eggNOG; KOG2633; Eukaryota.
DR InParanoid; C3YS03; -.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IBA:GO_Central.
DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0010629; P:negative regulation of gene expression; IBA:GO_Central.
DR CDD; cd02907; Macro_Af1521_BAL-like; 1.
DR CDD; cd02903; Macro_BAL-like; 1.
DR CDD; cd12547; RRM1_2_PAR10; 3.
DR CDD; cd12301; RRM1_2_PAR10_like; 1.
DR Gene3D; 3.30.70.330; -; 5.
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; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR034464; PAR10_RRM1_2.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
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 SMART; SM00506; A1pp; 2.
DR SMART; SM00360; RRM; 5.
DR SUPFAM; SSF52949; Macro domain-like; 2.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS51154; MACRO; 2.
DR PROSITE; PS50102; RRM; 2.
PE 4: Predicted;
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176}.
FT DOMAIN 6..82
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 1048..1124
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 2190..2381
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT DOMAIN 2415..2594
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT REGION 85..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2384..2416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..856
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2671 AA; 290447 MW; B168BB634BE20913 CRC64;
MSARARSVYV RGLPELSGLQ DKVSGYFQSG SLSAGGAVTR VKLLGPGQAL VTFGDETVAQ
NVLTQPQHTL QGTRIKVTAC PPHLDVPEES AEDTKETEKA AADKTEEVKE DTVLSEEEKK
VEQEEVEATA LQPEVVKEPP SIAKLPRDHS SDSDYATPPE SPTPKRLPVN VCHERKIDET
KPVIVNSLLV QKQANEVSSD SDAASQHVPQ LMAESCLFET LTETGHPEDD SPRMMGPSTP
PEIFLKKPKP LVLPKPYPKP TTSSTAPKET TATSLQHANT EGESIGNKQQ EHHPKPTPIP
AVTTEATVTA ASSQHPDMYT ASIDQPQQPF LKPATSSSAS TETSSDSHQH PNLPSGSTGE
QPRASPATTS SEPGGAMSAS LQAQQPNLSI ASREDHPLES NPIPTTTSSV PCGPTPASPQ
QPNLTNTSRG DLLQQPHLNP SITPSVPSGT TLASAQQPNV PNAPRVDIPQ QPHPNMTTAS
SEPRTALPSP QHPNLPNTRD QPQQLHPIPQ STSSVTTEAT RISSQPSSIP NMPMEDQMQQ
PHPSPTTISS VPTGTTSPFP QQPNLLDAPR EDLPQQPHPV TTSSAPGTAS PSPLYPNLPS
TSMGGYPQPQ HGPFYHWPPP PHMGMMYPRP PLYPPQLPGS QAHFMTPGVR MPYGDPRHGF
PWAGIGSIPP SGVQFQDQGH PPSGPQSAFF PQASHHTTGG PQQAHYMFPG QPASSIPLTA
ARSSPSSEVL HPYHHQPTSS QSPSWGSPRT GSPVSLPLPQ QDRNRGCDYL PDQASSVHSR
QTPTDLMSVW SDGESTFVDA SDSVSNVGSM ASDADSFVTS QGRNEATRPL GAAAKSDHHP
SYKERNRKDA KLKRKAPYTM SRGASKTDVQ AKKPFVGLSR SIVVSGFTSA PDVDLLGLYF
ESERRSGGGE VEEVKVRGTD EVIITFKDPS VTQRVLAREH VLNGQTLNVK ELTSSPAEAI
LDTDISPPSN ITIQVSGFTS SPNKEMMMLY FENKKRSGGG EIEDIQVRDN KVFIVFKDPT
DFDKMVTKAQ SRLLEGQQLT MERVPVTDAI IVTGLPDNVS RDLLELYFER EIGSSGGSVT
EIKMDSSTGT AVVQFDDANT VNSVHQKSSH ILNNTPISVQ PYYECLGEVV DDNAPEAFQM
PQPINVKIEP QLILFVIAMP KFIEQLTSKL AEVHAEVDMS VTDIVTVSPT LTPEMKGVRK
LAKQWEDESR RCVEQFFSQF QATEITMATQ IWERAKDRLE EVSEKVSTSN RNDVWIEGSD
DKDGEGAVTL IGTKETVKEA ELICKTIIKE TEALLKWEAS IVTDHIDNMK AAKLKILQLN
NFTGKHPDVE IRLNVDNQSV EFKGQQALVQ KAKIDLYETT NKIAEERVAL SRGKLSYLKS
DKGMKHLEDS LKKSDIKAAF AIENEEITIL AQFSVEVKAA KDLLPQVVSE SPIAIAEESR
DLLTKQRFVT YSTNLRQKLS VDIHVAKDKV WVVGAVEKVV AASKDIKAYI ATNTIVTINM
DVTEGEAKYL DCYRSSAVKD VEKNHAEQLV KVMIGQGKLT VRGTKDGTQS AKKQLQVLID
DVTTGTMNIT KPVTQRVLAR KHDLNSQTLN VKEFTSSSEE AIPNTDTSLP SNITIQVSGF
TSSPNKEMMT LYFENKKRSG GGEIQDIQVR DNKVFIVFKD PTAVNSVHQK SPHILNNTPI
SVQPYYECLG EVVDDNAPGA FQMPQPINVK IKPQLILFVI AIPTFIEQLT SKLAEVHAEV
DMSVTDIVTV SPTLTPETKG VRKLAKLWED KSRCCVEQFF TQFQAMEIRV ESQIWQRAKD
RFEEASEKVS TSNRDDVWIE PSDDKDGGRV VTLIGTTEAV TEAELVCKTI IKEIEELLMW
EASIVTDHIT NMKAAKLKIL QLNNFPGKHP DVEIRLNVDN QSVEFKGQQA LVQKAKIDLY
ETTNKIAEER VALSRGKLSY LKSDKGMKHL EDSLKKSDIK AAFAIENEEI TILAQFSVEV
KAAKDLLPQV VSESPIAIAE ESRDLLTKQR FVTYSTNLRQ KLSVDIHVAK DKVWVVGAVE
KVVAASKDIK AYVATNTIVT INMDVTEGKA KYLDCYRSSA VKDVEKNHAE QLVKVMIGQG
KLTVKGTKDG TQSAKKQLQV LIDDVTTGTM NITKPGMHKF FTKGSGSGLL KGIEREVKCV
IQVGGKPPGV PVRDMGGART AAAPAAPGGL KQICYHTTER RKLVVVQGNL TSHRVDVMVN
TANGSLSHGG GLAAAIVKAG GQEIQRDCTN YIKDNGKLTE GQVMSTKGYK LPCKMVVHAV
GPLWIADQKD SKEKALKMAV ENALLEARDY HSIAIPAISS GEELILLCIS GYPIKPCVAA
IVAAVTAFFN TNPDCALSEV HFAEMDPQKT DAFRDELLNR FGGDKVTMTG SSDTTPSRPV
PTPRPRAAGS DAATSPSNTL ITPEGIIIQL KKGNITAEKA DVLVNTTSGD LDLSQGGVAR
AFGQAGGQEL QQLCNNHGKA NAGDIVITLR AGTLRCKQVY HAVLPNWQES DQPLRTMVQD
CLESADQGGY TSISFPAMGT GNLKYPRDVA ASCMYDEILS FSQSNPGTTL QDVGIIVFDQ
PTVQAFETEL RVRQGVPGAS GTASGSGPYS AVTTPMPGQQ QMTIGNVTLQ IQGGDLTAEN
VDCIVNVTSK DLGNKIRFMG YLCDVKWQSG S
//
