ID   B4DGT2_HUMAN            Unreviewed;       831 AA.
AC   B4DGT2;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG57893.1};
RN   [1] {ECO:0000313|EMBL:BAG57893.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:BAG57893.1};
RA   Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA   Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA   Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA   Sugano S., Nomura N., Isogai T.;
RT   "NEDO human cDNA sequencing project focused on splicing variants.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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};
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DR   EMBL; AK294754; BAG57893.1; -; mRNA.
DR   AlphaFoldDB; B4DGT2; -.
DR   PeptideAtlas; B4DGT2; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR   GO; GO:0090304; P:nucleic acid metabolic process; IEA:UniProt.
DR   CDD; cd18795; SF2_C_Ski2; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004179; Sec63-dom.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR47835; HFM1, ATP DEPENDENT DNA HELICASE HOMOLOG; 1.
DR   PANTHER; PTHR47835:SF2; SEC63 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF02889; Sec63; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00973; Sec63; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF158702; Sec63 N-terminal domain-like; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:BAG57893.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          1..162
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          203..404
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          791..831
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   831 AA;  94383 MW;  9CE891FAA27A7966 CRC64;
     MIACFLWQIC FLKNQMKLKM APIKALCSQR FDDWKEKFGP IGLNCKELTG DTVMDDLFEI
     QHAHIIMTTP EKWDSMTRKW RDNSLVQLVR LFLIDEVHIV KDENRGPTLE VVVSRMKTVQ
     SVSQTLKNTS TAIPMRFVAV SATIPNAEDI AEWLSDGERP AVCLKMDESH RPVKLQKVVL
     GFPCSSNQTE FKFDLTLNYK IASVIQMYSD QKPTLVFCAT RKGVQQAASV LVKDAKFIMT
     VEQKQRLQKY AYSVRDSKLR DILKDGAAYH HAGMELSDRK VVEGAFTVGD LPVLFTTSTL
     AMGVNLPAHL VVIKSTMHYA GGLFEEYSET DILQMIGRAG RPQFDTTATA VIMTRLSTRD
     KYIQMLACRD TVESSLHRHL IEHLNAEIVL HTITDVNIAV EWIRSTLLYI RALKNPSHYG
     FASGLNKDGI EAKLQELCLK NLNDLSSLDL IKMDEGVNFK PTEAGRLMAW YYITFETVKK
     FYTISGKETL SDLVTLIAGC KEFLDIQLRI NEKKTLNTLN KDPNRITIRF PMEGRIKTRE
     MKVNCLIQAQ LGCIPIQDFA LTQDTAKIFR HGSRITRWLS DFVAAQEKKF AVLLNSLILA
     KCFRCKLWEN SLHVSKQLEK IGITLSNAIV NAGLTSFKKI EETDARELEL ILNRHPPFGT
     QIKETVMYLP KYELKVEQIT RYSDTTAEIL VTVILRNFEQ LQTKRTASDS HYVTLIIGDA
     DNQVVYLHKI TDSVLLKAGS WAKKIAVKRA LKSEDLSINL ISSEFVGLDI QQKLTVFYLE
     PKRFGNQITM QRKSETQISH SKHSDISTIA GPNKGTTASK KTWEPRMQSS L
//