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Database: UniProt
Entry: A0A1X2I5S6_9FUNG
LinkDB: A0A1X2I5S6_9FUNG
Original site: A0A1X2I5S6_9FUNG 
ID   A0A1X2I5S6_9FUNG        Unreviewed;      1245 AA.
AC   A0A1X2I5S6;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   ORFNames=BCR42DRAFT_441510 {ECO:0000313|EMBL:ORZ09953.1};
OS   Absidia repens.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX   NCBI_TaxID=90262 {ECO:0000313|EMBL:ORZ09953.1, ECO:0000313|Proteomes:UP000193560};
RN   [1] {ECO:0000313|EMBL:ORZ09953.1, ECO:0000313|Proteomes:UP000193560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 1336 {ECO:0000313|EMBL:ORZ09953.1,
RC   ECO:0000313|Proteomes:UP000193560};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) 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};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ORZ09953.1}.
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DR   EMBL; MCGE01000026; ORZ09953.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X2I5S6; -.
DR   STRING; 90262.A0A1X2I5S6; -.
DR   OrthoDB; 57056at2759; -.
DR   Proteomes; UP000193560; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
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   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   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:UP000193560}.
FT   DOMAIN          116..296
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          328..513
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          65..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          942..973
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          994..1075
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        994..1045
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1245 AA;  141084 MW;  E0F18B5801B5ABF7 CRC64;
     MWTSSEQQYT NSQTNGWLEE EEAFLDQFTS KQQESTNAYT VQSIEGITPT NRSFNYCSTK
     TFLPPNPDYG HQTANTSSPL ASTSSNHLRS VMEIPKEYQP IFKYSYFNRM QSEAMDQLLH
     SNENIVVSAP TGTGKTVLLE MAMIRCLLVY QTQQNYQQGS IKMIYMAPTK SLCAEKVAHW
     KNSFGPLGIV CEEFTGDSDY ATIDSIKNSN IIVTTPEKWD SMTRRWIDHR RLVEMIKLLM
     IDEIHILKET RGATLEVCVS RMKAMDHGMR IVAVSATIPN LQDITTWLNA SALTFSEEYR
     PIFLERYVYG YPSRGTNSYA FEKSLDWKLL DIIVKHGDNK SVLIFCSTRT ATQSACDTLL
     KLMDRKNITL KLPNDNVELK NKKLYGFVQR GIGFHHAGLD STDRHVVEQL FLSRKIGIVA
     TTSTLAVGVN LPAHLVIIKS TKGYQNGGLE EYSDIDILQM IGRAGRPGLD TSGCAVIMTT
     SDMEHKFKSL ISCQSVIESS LHRNLTEHLM SEICIGTVVD MDSSTKWLGS TFLYVRVKQN
     SYYYQQLYND ESLTKNPNQV MKDICLKDMK LLIDHNLVSV FGEGYNAKYE PTFYGSTMDR
     YYVQFKTMVK IMQSKNWCSI KDVLELVSQS EEFETYRYNA HEKTILNDLR SNADIRFPLK
     NKVSDVSDKV YVMIQCVLGE ISLYHPLIGN LMNTASHMIL QKACIIDCSA YEKDAIKLKH
     SLDLYRCMQA KMWSTSPFIL KQIDGIGIQI AKSLSQRNIS SFEQLRDCDP GQLEMILHRN
     PPFGTKIHSS LSFLPQYYLD LKQKPKQKYQ SQPIISLSVS IETSDHDLVD FRRIKTENLS
     KRHSELNFDV KVTSPSMTVI CHLQSEDYVG LDVMKQLKPN VDPTQFITLT DPIAHSTPAP
     PLIPVTLQPT ITTEQNSDAM KNDKNASLDT WIDALEDIDD SKTIKAEPST PRLKKKSTRS
     KKTDNEPCKH HCKDKQSCKH QCCKRATPLE DNRITSYPEF SRSFNNNSTS PSNKQISTSS
     PTDSSNRIIK SGSSGNGNCM KTQTPSHQPI PPPPPEHVSH TMTNRNHGDD DNFLDHTLLN
     SRGFAHTSLS PSSVSMKIED EDTWDITDTS MDDVLCNMTI TAEKNQQEEH MHGDNDCSMF
     GDLDMDMENE PLQDYFLCST ATSDAPSCDL IWADLEQAIY DADKRYHGDG AIQMDTNGND
     DGDIFDLEDT ESIIGHDAQT SFQENATRLP NLIKWINDHV ETIVE
//
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