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Database: UniProt
Entry: G3PSW6_GASAC
LinkDB: G3PSW6_GASAC
Original site: G3PSW6_GASAC 
ID   G3PSW6_GASAC            Unreviewed;       920 AA.
AC   G3PSW6;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   Name=HFM1 {ECO:0000313|Ensembl:ENSGACP00000020702.2};
OS   Gasterosteus aculeatus (Three-spined stickleback).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC   Gasterosteus.
OX   NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000020702.2, ECO:0000313|Proteomes:UP000007635};
RN   [1] {ECO:0000313|Ensembl:ENSGACP00000020702.2, ECO:0000313|Proteomes:UP000007635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGACP00000020702.2}
RP   IDENTIFICATION.
RG   Ensembl;
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};
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DR   AlphaFoldDB; G3PSW6; -.
DR   STRING; 69293.ENSGACP00000020702; -.
DR   Ensembl; ENSGACT00000020741.2; ENSGACP00000020702.2; ENSGACG00000015686.2.
DR   eggNOG; KOG0952; Eukaryota.
DR   GeneTree; ENSGT00550000074822; -.
DR   InParanoid; G3PSW6; -.
DR   OMA; HCKNKHT; -.
DR   TreeFam; TF328936; -.
DR   Proteomes; UP000007635; Unassembled WGS sequence.
DR   Bgee; ENSGACG00000015686; Expressed in testis.
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   CDD; cd18023; DEXHc_HFM1; 1.
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; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00973; Sec63; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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:UP000007635}.
FT   DOMAIN          22..209
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          250..435
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          793..834
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        819..834
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   920 AA;  103470 MW;  126D9AC2ADA987E1 CRC64;
     AKFRSVFKEF PFFNYVQSKA LDDVLYTSKN FVACAPTGSG KTVLFELAII CLLMESSEPW
     RDVKAVYMAP IKALCSQCFE SWKKKFGPLG LTCKELTGDT EIDDFFEIQD SHIILTTPEK
     WDSMTRKWKD NCMLQLVRLF LIDEVHVVKD ATRGATLEVV VSRMKAVHAY RTAQNPETGL
     SMRFVAVSAT IPNTSDIADW LSDDSGPATY LDMDESYRPV KLRKVVLGFP PTPNQTEFKF
     DLLLNYKMAN IIQTYSDQKP ALVFCSTRKG VQQAATVLAK DARFMMSIEH KQRLTKYANS
     ILDSKLRDLV VLGVGYHHAG VDLSDRKLIE EAFTQGDLPV LFTTRTLAMG VNLPAHLVVI
     KSTMQYVSGS CEEYSEADLL QMIGRAGRPQ FDTSATAVIM TKTQTKDKYM KLMNGVETIE
     SSLHSHLVEH LNAEIVLQTI RDVNMALDWI RSTFLYIRAL KNPTHYGFPA NLDRYGIEAK
     LQELCLKNLN SLSSIGLIDM DEEINIKPTE GGRLMARYCV AFDTMTQFSK ASGTESLSDL
     VELVSKSREF SDIQLRMNEK RSLNTFNRDK NRITIRFPIQ GKIKTSQMKV NCLIQAQLGS
     ISIQEFGLTQ DTAKIFRNGM RISRCMSTLS TAMVNAGLTT FSRIEQINAR ELELIVNRHP
     PFGNQIKESA TNLPKYEVTL EQLPRYSCAT AEIVLKVNLK NQAQLLSRRT APDDHYISLI
     IGNSDNAVVF LQKLTDLVLL KCGTWSKKIE VAKASKGEEI SVNLISSQYV GLDIQQRFNV
     YYSGARRFGN EILSNTPFDP TGQRPQHAAL KPHSTDQAAG HRENATSATE QGTAPQCNHY
     CKNKDLCGHD CCKVGVAVAK KRPANQESSF SSYLKDLRNR CDTLSQTPVK RLKIKMSDYS
     VPVDIQEFAY KPKERLPTAS
//
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