ID A0A2J6SQ18_9HELO Unreviewed; 834 AA.
AC A0A2J6SQ18;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=K444DRAFT_656202 {ECO:0000313|EMBL:PMD52851.1};
OS Hyaloscypha bicolor E.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha; Hyaloscypha bicolor.
OX NCBI_TaxID=1095630 {ECO:0000313|EMBL:PMD52851.1, ECO:0000313|Proteomes:UP000235371};
RN [1] {ECO:0000313|EMBL:PMD52851.1, ECO:0000313|Proteomes:UP000235371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E {ECO:0000313|EMBL:PMD52851.1,
RC ECO:0000313|Proteomes:UP000235371};
RG DOE Joint Genome Institute;
RA Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA Martin F., Perotto S.;
RT "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL Submitted (APR-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 -!- SIMILARITY: Belongs to the helicase family. RAD25/XPB subfamily.
CC {ECO:0000256|ARBA:ARBA00006637}.
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DR EMBL; KZ613895; PMD52851.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6SQ18; -.
DR STRING; 1095630.A0A2J6SQ18; -.
DR InParanoid; A0A2J6SQ18; -.
DR OrthoDB; 1360679at2759; -.
DR Proteomes; UP000235371; 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:PMD52851.1};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:PMD52851.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022806,
KW ECO:0000313|EMBL:PMD52851.1}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000235371}.
FT DOMAIN 354..516
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 570..724
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..834
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 834 AA; 94289 MW; 7A50AF2F3818B77A CRC64;
MPVKRKASST VKGAEKTRKD SVASTPGPAT PRSIGSSDEY ESSDVTESDD EAAKRVKTAL
DIKEYKSKKV TSAVKSRDSA SHHFGEHDFS YLSLKPDHDN RPLWIDPQKG RIILESFSPL
ATHAQDFLTT VAEPASRPAF LHEYKLTPHS LYAAVSVGLD PKDIINVLDR LSKIPVPENI
RNFITSCTQS YGKVKLVLKN TKHYLESSDP EMLQRLLKDE VIGPLRVQGA EDITTTSAPK
MGALVIPGTK NAAGVQQAAA DQRKQPQEGE NANQEDIFAT LNEEDDDDDD ADAVHAFEIV
DEGVEHIQKR CLELGLPVLE EYDFRNDDAN ANLDIDLKPT AQIRHYQEKS LSKMFGNGRA
KSGLIVLPCG AGKTLVGITA ACTIKKGVII LCTSSMSVVQ WRQEFLKWSN INPNDIAVFT
SDNKEKFTGN TGIIVTTYNM VAQKGKRSYD SQKMMDFLQG REWGLMILDE VHVAPAHMFR
RVVSVIKTHS KLGLTATLLR EDDKISDLNF LIGPKLYEAN WMELAEQGHI ARVQCAEVWC
PMTTEFYQEY LHQTSKKQAL LWIMNPRKFQ ACQFLIDYHE KRGDKIIVFS DNVYALQVYA
QKLKKVFIFG ETSNSERLRI LENFQHNENI NTLFLSKIGD TSLDLPEATC LIQISSHFGS
RRQEAQRLGR ILRAKRRNDE GFNAFFYSLV SKDTQEMVYS SKRQAFLVDQ GYAFKVITHL
QGIEHLPDLS FTTPAERREL LQNVMIHNAS EDASKDYEDV DDLFHRIDGG RKKKKKGARR
TAGTLSELAG GQDMAYVEQN KSRNKELKKK KESNPFFKKV QREQQKRRLA RDDE
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