ID A0A2J6QLU7_9HELO Unreviewed; 1076 AA.
AC A0A2J6QLU7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Antiviral helicase {ECO:0000313|EMBL:PMD27211.1};
GN ORFNames=NA56DRAFT_676169 {ECO:0000313|EMBL:PMD27211.1};
OS Hyaloscypha hepaticicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha.
OX NCBI_TaxID=2082293 {ECO:0000313|EMBL:PMD27211.1, ECO:0000313|Proteomes:UP000235672};
RN [1] {ECO:0000313|EMBL:PMD27211.1, ECO:0000313|Proteomes:UP000235672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 7357 {ECO:0000313|EMBL:PMD27211.1,
RC ECO:0000313|Proteomes:UP000235672};
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 (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000256|ARBA:ARBA00010140}.
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DR EMBL; KZ613466; PMD27211.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6QLU7; -.
DR STRING; 1745343.A0A2J6QLU7; -.
DR OrthoDB; 1352at2759; -.
DR Proteomes; UP000235672; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0006401; P:RNA catabolic process; IEA:InterPro.
DR CDD; cd18024; DEXHc_Mtr4-like; 1.
DR CDD; cd13154; KOW_Mtr4; 1.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 1.10.3380.30; -; 1.
DR Gene3D; 2.40.30.300; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR048392; MTR4-like_stalk.
DR InterPro; IPR025696; MTR4_beta-barrel.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016438; SKI2-like.
DR InterPro; IPR012961; Ski2/MTR4_C.
DR PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR PANTHER; PTHR12131:SF7; EXOSOME RNA HELICASE MTR4; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF08148; DSHCT; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF21408; MTR4-like_stalk; 1.
DR Pfam; PF13234; MTR4_beta-barrel; 1.
DR PIRSF; PIRSF005198; Antiviral_helicase_SKI2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01142; DSHCT; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
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:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:PMD27211.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000235672}.
FT DOMAIN 159..315
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 396..600
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..63
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1076 AA; 122022 MW; E656D6B333565ACE CRC64;
MDELFDVFDD KPQSEIPEKP KKAKKDKKEK TKKRTANGDV KTDQDGDAEM VDNEQQVAEA
AEEDADVLVE KKDTKRRRRD EEAEPVVTDT FQTEQSREVA ASAGLQGKDD GALVIQHNIQ
HQVSLPPDYD YVPISQHVPP EKPARVWPFE LDPFQKVSIA SIERGESVLV SAHTSAGKTV
VAEYAIAQSL KNNQRVIYTS PIKALSNQKY REFAAEFGDV GLMTGDVTIN PTATCLVMTT
EILRSMLYRG SEIMREVAWV IFDEIHYMRD KSRGVVWEET IILLPDKVRY VFLSATIPNA
MQFAEWITKT HQQPCHIVYT DFRPTPLQHY FFPAGADGIH LIVDEKGNFR EDNFQKAMAT
IEDKKGADPA DIDAKRKGRG PNKRTNKGGN KEGNGDIYKI VRMIMMKHYN PVIVFSFSKR
ECEAYALQMS SMAFNDDSEK AMVTKVFESA IESLSDEDKT LPQIQHILPL LRRGIGVHHS
GLLPILKETI EILFQENLIK VLFATETFSI GLNMPAKTVV FTSVEKFDGT SMRHLTPSEF
VQMSGRAGRR GLDDRGIVIM MINSKMEPAT AKEIVRGEQD KLNSAFYLGY NMILNLMRVE
GISPEFMLEH CFYQFQNTSG VSGLEKELQQ LQLERDSVEI PDEATVKEYY DLRQQLTSYT
KDMRDVINHP NYCLQFMQPG RVVHIKYLDQ DFGWGAVVKF TPRRPAKGQT GEEYTPQQAY
VLDVLLSVSD SSSVGTQAQG DVPAGIRPPA EGEKGKMEVV PVLLSCIEAI GHVRIFLPKD
LHPADQRNNV RKSLEEVKRR FPDGIAVLDP IENMGITDES FKKLLRKIEV LESRLLSNPL
HNSPRLPELY NQYATKMEMG RKIKEKKKSI TAALSIMQLD ELKSRKRVLR RLGFINDQEV
VQLKARVACE ISSTGDGHEL LLSELLFNRF FNELTPEVCA AVLSCFIFEE KSQKAAPLQE
ELGKHFREIQ QQARTIAKVS QESKLEVNEQ AYVASFKSEL MEVVFAWAHG KSFAEICKMT
DVYEGSLIRL FRRLEELLRQ MAQAGKVMGS DELALKFEES LTKIRRDIVA AQSLYL
//
