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Database: UniProt
Entry: A0A2U4C7H3_TURTR
LinkDB: A0A2U4C7H3_TURTR
Original site: A0A2U4C7H3_TURTR 
ID   A0A2U4C7H3_TURTR        Unreviewed;      1430 AA.
AC   A0A2U4C7H3;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   Name=BLM {ECO:0000313|RefSeq:XP_019801389.1};
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_019801389.1};
RN   [1] {ECO:0000313|RefSeq:XP_019801389.1}
RP   IDENTIFICATION.
RC   TISSUE=Spleen {ECO:0000313|RefSeq:XP_019801389.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00001665};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC       {ECO:0000256|ARBA:ARBA00005446}.
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DR   RefSeq; XP_019801389.1; XM_019945830.2.
DR   STRING; 9739.ENSTTRP00000015530; -.
DR   GeneID; 101340055; -.
DR   InParanoid; A0A2U4C7H3; -.
DR   OrthoDB; 5474026at2759; -.
DR   Proteomes; UP000245320; Chromosome 2.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd18016; DEXHc_RecQ2_BLM; 1.
DR   CDD; cd18794; SF2_C_RecQ; 1.
DR   Gene3D; 1.10.150.80; HRDC domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR012532; BDHCT.
DR   InterPro; IPR032439; BDHCT_assoc.
DR   InterPro; IPR032437; BLM_N.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR010997; HRDC-like_sf.
DR   InterPro; IPR002121; HRDC_dom.
DR   InterPro; IPR044876; HRDC_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032284; RecQ_Zn-bd.
DR   InterPro; IPR018982; RQC_domain.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   NCBIfam; TIGR00614; recQ_fam; 1.
DR   PANTHER; PTHR13710:SF105; BLOOM SYNDROME PROTEIN; 1.
DR   PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR   Pfam; PF08072; BDHCT; 1.
DR   Pfam; PF16204; BDHCT_assoc; 1.
DR   Pfam; PF16202; BLM_N; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00570; HRDC; 1.
DR   Pfam; PF16124; RecQ_Zn_bind; 1.
DR   Pfam; PF09382; RQC; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00341; HRDC; 1.
DR   SMART; SM00956; RQC; 1.
DR   SUPFAM; SSF47819; HRDC-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50967; HRDC; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245320}.
FT   DOMAIN          689..864
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          890..1037
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          1225..1305
FT                   /note="HRDC"
FT                   /evidence="ECO:0000259|PROSITE:PS50967"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          82..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          296..361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1305..1430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..324
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        325..346
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..361
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1343..1366
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1367..1401
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1430 AA;  160614 MW;  B24D767343336997 CRC64;
     MAAVPQNNLQ EQLERHSARK LNNKLSPSKP KSSGFTFKKK VSSANDVCVT SVSVAKAPVL
     NDKDVTITEA FSFSEPFPHT TNQQTKINDF KNTPAGQQTK RVGSKPLLPN LSQVPQEVLC
     TTQNTLLVKE SRDATFKKLE FSSSSDSLIT FSDWDDMDDF DTSGDSKAFV TPRQNHFIRV
     STAQKSKKSK RNFLKAHLGK TNTVKTDLTP SSSESKQAFL TKKQKDDSEW LNSDVICIDD
     DPNSEELINE DTQENHPLKT HLGEERDNCE KKKNLEEMEL HSFEKSSCVE LDEDDYDIDF
     VPPSPEEGMT STSSSSLKYS SVLKDLDTSD SKDGLSISED LSKSEKMTTK QPNQETSTSY
     DARQISLQQQ LIRVMDHICE LVDTIPDDKL KTLDCGNKLL QQRDIRRKLL AEADFNTSDA
     SVLGSLWRCR PDSLGSSVKD MASVSPPCAF PKGDSCPTGN SVKEFTFPNL PSNSISTGEC
     LLTPTPGKTG FSATTKNLFE RPLFNSHLQE SFVSSNWAET PRVEKRNESS YFPGNVLTST
     AVKDQNKHTT SMNDLEREIQ ASCDIDSFDI DDFDDDDDDW ENVMHNLAAS KSSTAAYQPI
     KEGRPVKSVS ERISSSAKTD CLLASTAQNK NFSESIQNYT DKSEQSLASR DLKHERFQSL
     NFPHTKEMMK IFHKKFGLHN FRTNQLEAIN AALLGEDCFI LMPTGGGKSL CYQLPACVSP
     GVTIVISPLR SLIIDQVQKL TSFDIPATYL TGDKTDSEAT NIYLQLSKKD PIIKLLYVTP
     EKVCASNRLI STLENLYERK LLARFVIDEA HCVSQWGHDF RPDYKRMNML RQKFPSVPVM
     ALTATANPRV QKDILTQLKI LRPQVFSMSF NRHNLKYYVL PKKPKKVAFD CLEWIRKHHP
     HDSGIIYCLS RRECDTVADT LQKDGLAALA YHAGLSDSAR DEVQHKWINQ DGCQVICATI
     AFGMGIDKPD VRFVIHASLP KSVEGYYQES GRAGRDGEIS HCLLFYTYHD VTRLKRLILM
     EKDGNHHTKE THFNNLYSMV HYCENITECR RIQLLAYFGE KGFNPYFCKK YPDVSCDNCC
     KTKDYKTRDV TDDVKNIVRF VQEHSSSQGT RNIKHVGPSG RFTMNMLVDI FLGSKSAKIQ
     SGIFGKGSAY SRHNAERLFK KLILDRILDE DLYINANDQP IAYVMPGNKA QHVLNGHLKV
     DFMETENSSS VKKQKALVTK VSQREEMVKK CLGELTEVCK SLGKVFGVHY FNIFNTVTLK
     KLAESLSSDP EVLLQIDGVT EDKLEKYGAE VIPILQKYSE WTLPAEDDSS RRSPSSSRGT
     GRNAPEELDE ETPISSHYFA NKTKNERKRK RMPASQRSKR RKTGFSGSKT KGGSSTCRRI
     PSKTKSSSIF GPSSALHGSQ AASGVSRKLG IMAPPKPVNR PFLKPSYAFS
//
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