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Database: UniProt
Entry: A0A1Y2CRX2_9FUNG
LinkDB: A0A1Y2CRX2_9FUNG
Original site: A0A1Y2CRX2_9FUNG 
ID   A0A1Y2CRX2_9FUNG        Unreviewed;      1041 AA.
AC   A0A1Y2CRX2;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Antiviral helicase {ECO:0000313|EMBL:ORY49800.1};
GN   ORFNames=BCR33DRAFT_781343 {ECO:0000313|EMBL:ORY49800.1};
OS   Rhizoclosmatium globosum.
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Chytridiomycetes; Chytridiales;
OC   Chytriomycetaceae; Rhizoclosmatium.
OX   NCBI_TaxID=329046 {ECO:0000313|EMBL:ORY49800.1, ECO:0000313|Proteomes:UP000193642};
RN   [1] {ECO:0000313|EMBL:ORY49800.1, ECO:0000313|Proteomes:UP000193642}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEL800 {ECO:0000313|EMBL:ORY49800.1,
RC   ECO:0000313|Proteomes:UP000193642};
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   -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00010140}.
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:ORY49800.1}.
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DR   EMBL; MCGO01000008; ORY49800.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2CRX2; -.
DR   STRING; 329046.A0A1Y2CRX2; -.
DR   OrthoDB; 1352at2759; -.
DR   Proteomes; UP000193642; 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; cd18795; SF2_C_Ski2; 1.
DR   Gene3D; 1.10.3380.30; -; 2.
DR   Gene3D; 1.20.1500.20; -; 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:SF8; HELICASE SKI2W; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF08148; DSHCT; 2.
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; 3.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01142; DSHCT; 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:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:ORY49800.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193642}.
FT   DOMAIN          184..296
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          395..595
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          91..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          344..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..111
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1041 AA;  114994 MW;  827A9B22B0F77315 CRC64;
     MRSTWTNFEF GFGWTQTVPP GFDRGLSLKV LYCLFLLTDV PVLTFETSPS DTDQVPAYAH
     ETVLNIQDIL GSTGDDFGLF DAPTIQVELV TPETQREQPT DESKDTEQSS LTADLDDLIP
     TKEVVPVVAT KAAKPKKEAL KEWAYVVDVN QPFPDFYEKV PELAHKFSSP RTHPRKNRSG
     RIAIALAQKH MTRAIYTSPI KALSNQKFRD FKDPSCLIMT TEILRSMLYR GADLIRDVEF
     VIFDEVHYVN DAERGVVWEE VIIMLPAHIT LILLSATVPN TREFADWVGR TKKRDIFVIS
     TQKRPVPLEH HLYVEKEIYK VVGAEKKFLS AGWEGGAVAA AAGRGGRGGA VARGGGRGGG
     AAGGANRGGG GGGGGGSGGN NSFSRDVADR NMYVNIISLL KKKSLLPVIV FSFSKRKCEE
     YANALVNLDL TSGSGEKSEI HVFIERSLAR LKGTDKQLPQ VLRIRDLLSR GIAVHHGGLL
     PIIKEMVEIL FTRGLVKVLF ATETFAMGVN APARAVVFSS TRKHDGRNFR ELLPGEYTQM
     SGRAGRRGLD DTGVVIIACS DEVPEPTMLN QMLLGVPTKL ESQFRLTYTM ILNLLRVEAL
     KVEEMIKRSF SENTAQKMLP EQQSMYDESA KALSNLQKLS CSICTDIGPF YDASSKVVLL
     GHQLREKIMR SPLGSKVAVP GRVIIVNSGF FRNVVGVILK PGIVPPVSAS HETARREATA
     DGRAFIVLAV VENMGSGANP YAGVDLSPMP VTRVSLPAAS RQAFEVIAVP YSDMSVITKH
     VIKIDQDQIL ESKLSAEATR VGQLLVSLAE EMAQESRIPE NDWSKIRELE FQEKEKEKNA
     LLAKLSSFQC SKCPDLVEHY GIIHNERQLE VQLAELAHNI SDQNLELLPD YHQRIEGRVA
     CEINTADELI LTELILENFL ADYEPAEIGI EEIKNIAIKV HSVQKMCGLD VGGPEDAIAG
     LKFGLVEVVY EWARGMSFKE ITELTDVLEG SIVRCIVRLD ETCREVRGAS RIIGDSNLHR
     KMEEAAESIR RDIVFAASLY F
//
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