ID A0A0A1TGL3_9HYPO Unreviewed; 822 AA.
AC A0A0A1TGL3;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=VHEMI05271 {ECO:0000313|EMBL:CEJ89428.1};
OS [Torrubiella] hemipterigena.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC Clavicipitaceae incertae sedis; 'Torrubiella' clade.
OX NCBI_TaxID=1531966 {ECO:0000313|EMBL:CEJ89428.1, ECO:0000313|Proteomes:UP000039046};
RN [1] {ECO:0000313|EMBL:CEJ89428.1, ECO:0000313|Proteomes:UP000039046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Horn F., Habel A., Scharf D.H., Dworschak J., Brakhage A.A., Guthke R.,
RA Hertweck C., Linde J.;
RT "Draft Genome Sequence and Gene Annotation of the Entomopathogenic Fungus
RT Verticillium hemipterigenum.";
RL Genome Announc. 3:e01439-e01414(2015).
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 -!- SIMILARITY: Belongs to the helicase family. RAD25/XPB subfamily.
CC {ECO:0000256|ARBA:ARBA00006637}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CDHN01000002; CEJ89428.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A1TGL3; -.
DR STRING; 1531966.A0A0A1TGL3; -.
DR HOGENOM; CLU_008213_0_0_1; -.
DR OrthoDB; 1360679at2759; -.
DR Proteomes; UP000039046; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IEA:InterPro.
DR CDD; cd18029; DEXHc_XPB; 1.
DR CDD; cd18789; SF2_C_XPB; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR032438; ERCC3_RAD25_C.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001161; XPB/Ssl2.
DR InterPro; IPR032830; XPB/Ssl2_N.
DR NCBIfam; TIGR00603; rad25; 1.
DR PANTHER; PTHR11274:SF0; GENERAL TRANSCRIPTION AND DNA REPAIR FACTOR IIH HELICASE SUBUNIT XPB; 1.
DR PANTHER; PTHR11274; RAD25/XP-B DNA REPAIR HELICASE; 1.
DR Pfam; PF16203; ERCC3_RAD25_C; 1.
DR Pfam; PF13625; Helicase_C_3; 1.
DR Pfam; PF04851; ResIII; 1.
DR PRINTS; PR00851; XRODRMPGMNTB.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:CEJ89428.1};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:CEJ89428.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022806,
KW ECO:0000313|EMBL:CEJ89428.1}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000039046}.
FT DOMAIN 345..508
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 562..716
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..822
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 822 AA; 92221 MW; 4C0DD4C7C01F9D8C CRC64;
MPVKRKASGG VAGGAKAGRS SRVSTPGAAT PREIDSDDEY EEGEEEAVVD EVLERDIDKN
IDQFSLDRYQ RHHDVKEPLP HIFGNNDFSY LDLKKDHQNR PLWIDPQKGR IILESFNPLA
EQAQDFLITI AEPLSRPTFM HEYALTTHSL YAAVSVGLSP ADIINTLERF LKTPLPSEIR
SFINGCTQSY GKVKLVLKNT KYYVESPDPD MLQTLLKNPK IGPLRVHGSE EIVTSAAPKI
GGLVIPGTKS AAGVKQANGQ DGQGIQERDV MAALNDDDDD DQDVTHAFEI ADKDVETVQR
ECLNLGFPVL EEYDFRRDEA NANLDIDLRP GTQIRPYQEK SLSKMFGNGR AKSGLIVLPC
GAGKTLVGIT AACTIKKGVI VLCTSSMSVV QWRNEFLKWS NINPDDIVAF TSDSKGSVFT
GSTGIIVTTY SMVTQSRARS YDAEKMMRFL TGREWGLMLL DEVHVVPANI FRKVTSSIKT
HSKLGLTATL LREDDKISDL NFLIGPKLFE ANWMELSKQG HIARVQCAEV WCPMPTEFYD
EYLRAPSRKK NLLYIMNPRK FQACQYLINY HEARGDKIIV FSDNVYALKA YALKLGKAFI
YGSTGQAERL QVLENFQHNP NVNTLFLSKI GDTSLDLPEA TCLIQISSHY GSRRQEAQRL
GRILRAKRRN DEGFNAFFYS LVSKDTQEMY FSSKRQAFLV DQGYAFKVIT QLANIEKTPG
LAFATASERR ELLQKVLVEN ETMDDEDPTD DLFHSGTMGR TKKRGARRTA GTLGELSGGQ
DMAYIEQNKK LNQSLKKGKG KQDQHKFFKK LRRENARRTA GE
//