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Database: UniProt
Entry: A0A2U4A452_TURTR
LinkDB: A0A2U4A452_TURTR
Original site: A0A2U4A452_TURTR 
ID   A0A2U4A452_TURTR        Unreviewed;      2683 AA.
AC   A0A2U4A452;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Probable helicase senataxin isoform X1 {ECO:0000313|RefSeq:XP_019775767.1};
GN   Name=SETX {ECO:0000313|RefSeq:XP_019775767.1};
OS   Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Delphinidae; Tursiops.
OX   NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019775767.1};
RN   [1] {ECO:0000313|RefSeq:XP_019775767.1}
RP   IDENTIFICATION.
RC   TISSUE=Spleen {ECO:0000313|RefSeq:XP_019775767.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_019775767.1; XM_019920208.2.
DR   STRING; 9739.ENSTTRP00000011529; -.
DR   GeneID; 101335263; -.
DR   InParanoid; A0A2U4A452; -.
DR   OrthoDB; 170190at2759; -.
DR   Proteomes; UP000245320; Chromosome 6.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   CDD; cd18042; DEXXQc_SETX; 1.
DR   CDD; cd18808; SF1_C_Upf1; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR045055; DNA2/NAM7-like.
DR   InterPro; IPR041679; DNA2/NAM7-like_C.
DR   InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR047187; SF1_C_Upf1.
DR   PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR   PANTHER; PTHR10887:SF525; HELICASE SENATAXIN-RELATED; 1.
DR   Pfam; PF13086; AAA_11; 1.
DR   Pfam; PF13087; AAA_12; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000313|RefSeq:XP_019775767.1};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Helicase {ECO:0000313|RefSeq:XP_019775767.1};
KW   Hydrolase {ECO:0000313|RefSeq:XP_019775767.1};
KW   Nucleotide-binding {ECO:0000313|RefSeq:XP_019775767.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245320}.
FT   DOMAIN          1940..2221
FT                   /note="DNA2/NAM7 helicase helicase"
FT                   /evidence="ECO:0000259|Pfam:PF13086"
FT   DOMAIN          2229..2428
FT                   /note="DNA2/NAM7 helicase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13087"
FT   REGION          604..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          710..732
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1171..1265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1354..1400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2510..2541
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2562..2683
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          2081..2140
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        604..621
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        622..640
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        717..732
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1189..1204
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1205..1229
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1354..1375
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1376..1397
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2510..2526
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2626..2646
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2660..2683
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2683 AA;  302456 MW;  C9E6F2F548C2932D CRC64;
     MSTCCWCTPG GISTIDFLQH YASETHSSEF QKADEDLCYC LECVAEYHKA RDELPSLHKV
     LWELETSRLI NHFEKAMKAE IGDDDELYIV DDNGEAQLFD FTGQDFENKL RVPLLEILKY
     PYLLLHERVN ELCVEALCRM EQANCSFQVF DKHPGIYLFL VHPNEMVRRW AILTARNLGK
     VDRDDYYDLQ EVLTCLFKVI ELGLLESPDI YTSSVLETGK LILLPSHMYD AANYKNYWLG
     ICMLLTILEE QAMDSLLLGS NKQNDFMQSI LHTMERQSDD DSVDPFWPAL HCFMVILDRL
     GSKVWGQLID PIEAFQTIIN NVSYNKEIQN IRNSSMRSKF KPESCLDDTV TCSQIVYNYN
     PEKTKKDSGW RSAICPDYCP NMYEEMETLA NVLQSDIGQD MRVHNSTFLW FIPFVQSLMD
     LKDLGVAYIV EVIHHLHSEV KDVLNQTDAV CDTVTEFFLL ILVSVIELHR NKKCLHLLWV
     SSQQWVEAIV KCAKLPTAAF ARSSEKSSGN CSKGTMISSL SLHSVPSNSV QRACVQLIRS
     LLKEGIEPGQ QALRKRFLDK LNLFLRGNSS LGCQLTSQET HELQTCLKQI IRNIKFKVPQ
     CSTSVDLTSP CKTPPASYNK EESEQTGKKS KKDRHCLENS SPTFSKEPMK ADACQVQESI
     FSKADNAIEE DNERTYIKDL KLKDHLSAEL CLKPSSKRLV NERARGQVKI STGKHKSVKE
     NSSYTPQNCT SRNGPEKVFD RGIITSTHLL TDSSNDSLEK VSTSNEDFSL KGDALGKTSK
     AKTKAHKDEI CAKLSHVVKK QHRKSITLEE NLTVSSIESF YSKDTGGQKG DGFIYNLSLG
     PNGILDDKNG EQKSENSLLL KKKQVKEEEL GILSTRELSC QILECHVGNK DLVSFTEMTN
     IFVEKTPPFK DPVTGLESRD MEIIKSTAQF SSDLREQVLS SPKSDTLTDS QVDRDLHKLS
     LVAQASVIKF PSDSTQKSLS QLQRKVKDDR RCFTANQNSV RETCCEQVII ISDSDEDDDD
     DERIVGFKKR IKQDKTCIEK ECPEQHASIA NTNVEQKVIR EENTGSPLQF EESDSQFFEF
     ESPCEVFSVW QDQKPDNKNS VQENEENSCL THVGDTTNDW GYGTDYVPEE VIKKAAEDIE
     EHAEPHSSSI SVEEFCEIEV KKPKRKRYQK AAMAEAPLRP SSPVKSEDQS DILNERDVTE
     NDFKSIDVRS TTPSSSVQRT TTVSLKKSPP KLRNCSKRVS RVSLSKTPKK TRSDTKTGQS
     KTSNILSCRT SPAIVLPKKF RQRPEPTSTV EKLGLKKVAR RAFDLSQPSL ERLADLRHHG
     RTVGAIDTRK KTKLISPQTL SVRNNEKLLT SQDRQLRRQL RPKSQRNRKR CFDYQSTDTT
     RAGPQGAQNS DKFVPESDTS DYSYKGGVEV TAKSKETELI KCVSSETEPV KAEYVSQVAD
     DPCLLNQGTS VVLHGEIPTN EVVVSTSGDP LGGGDLTVHH LAVAALREGD PESSNDIEED
     NIFLTQCDPE DMDLCSQMEK ENDKLVEVVH GKDTVQVEEG YVSRPQLESS SSTKCKYKDC
     VETLKNQGEY CSKHSEAKAA DEAIFRKPGL PLSASKPSRP PTAKIFSSSS TSRIAGLSKS
     LENTAALLPT LKNKSSGVQS VLKVPPVSLV SKKPVAEVKG LCNVLHSHAP NNSNRQGYKV
     PYCENRSFSA SPPVNVLLSA QSISDTFVKE VLKWKYEMFV NFDQCGPPST LCQSISRPVP
     VRFQDGGDYF NVFFPLMMLN TFETVAQEWI SSPNKEKFHW LHLRKFPSEY KKYWEFVVYL
     EECELAKQLH PKENDLVFLV PERLNGEEED IERNRMQDPY EYYCGYVHKF RRTSVMHNGK
     SECSVSIQTQ HNLPVNLNEF VKCLVISSLV TTQRKLKAMS LLSGRNQLAR AVLNPNPMDF
     CTKDLLTAAS EKIIAHLKDF NEDQKKAIET AYAMVRHSPA VAKICLIHGP PGTGKSKTIV
     GLLYRLLTER RGLSDENSNA KIKRNRVLVC APSNAAVDEL MKKIILQFKG KCKDKKNPLG
     NCGDINLLRL GPEKSINAEV LKFSLDSQVN HRMKKELPSH IQEMHRRKEF LDHQLDELSR
     QRALCRGGRE LQRQELDEKI ARVSKERQEL ASKVKEVQGR PQKTQNTIIL ESHIICCTLS
     TSGGLLLEAA FRGQGGVPFS CVIVDEAGQS CEVETLTPLI HRCNKLILVG DPKQLPPTVI
     SVKAQEYGYD QSMMARFYKL LEENVKHNMI GRLPVLQLTV QYRMHPDICL FPSNYVYNRN
     LKTNRITEAI RCSSDWPFQP YLVFDVGDGS EKRDNDSYVN VQEIKLVMEL VKLMKDKKRD
     FTYRNVGIIT HYKAQKMMIQ KDLDKEFDRK GPAEVDTVDG FQGRQKDCVI VTCVRANAMQ
     GSIGFLASLQ RLNVTITRAK YSLFILGHLR TLMENCHWNQ LIQDAQKRGA IVKTWDKNYR
     QDAVKILKLK PVLQRSLTHP PAIAPEVSRP QGGVPSNKLD SEFAKMSIAS SLYPSPSDSK
     EATVTVTAND PERPPIQDWL RDPRLLRRMG LGCEAKGKCL SELQPSSPQY PGAAPLSGEP
     GSPGRHQDPT SIGQQPPAKG AAVNNHRPHA QCDPPAASTD ASTSKRKCAQ EGEAVSHRRE
     TRAFPEGDQE TCGSLSHHTK RNSGWDERGL EEEDSSLKKR KLS
//
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