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Database: UniProt
Entry: A0A067PRF7_9AGAM
LinkDB: A0A067PRF7_9AGAM
Original site: A0A067PRF7_9AGAM 
ID   A0A067PRF7_9AGAM        Unreviewed;      1008 AA.
AC   A0A067PRF7;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Antiviral helicase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=JAAARDRAFT_138149 {ECO:0000313|EMBL:KDQ52896.1};
OS   Jaapia argillacea MUCL 33604.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Jaapiales; Jaapiaceae; Jaapia.
OX   NCBI_TaxID=933084 {ECO:0000313|EMBL:KDQ52896.1, ECO:0000313|Proteomes:UP000027265};
RN   [1] {ECO:0000313|Proteomes:UP000027265}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUCL 33604 {ECO:0000313|Proteomes:UP000027265};
RX   PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA   Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA   Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA   LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA   Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA   Hibbett D.S., Grigoriev I.V.;
RT   "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT   white-rot/brown-rot paradigm for wood decay fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
CC   -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00010140}.
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DR   EMBL; KL197737; KDQ52896.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A067PRF7; -.
DR   STRING; 933084.A0A067PRF7; -.
DR   HOGENOM; CLU_002902_0_1_1; -.
DR   InParanoid; A0A067PRF7; -.
DR   OrthoDB; 1352at2759; -.
DR   Proteomes; UP000027265; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
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:UP000027265}.
FT   DOMAIN          83..239
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          322..526
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          287..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          662..685
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          789..816
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        662..679
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1008 AA;  113880 MW;  ECF319EEABA4B6FE CRC64;
     MASPKPIVVD EVEIEAKREV AASAGLTGAA VESGSRLELK HQVRHQVAVP SGYNYIPIAN
     HIPPAKPARE YKFTLDPFQQ VSVNAIQRNE SVLVSAHTSA GKTVVAEYAI AQCLLNKQRV
     IYTSPIKALS NQKYREMLAE FGDVGLMTGD VTINPSATCL VMTTEILRSM LYRGSEIMRE
     VAWVIFDEIH YMRDKERGVV WEETIILLPH TVRYVFLSAT IPNAMQFAEW ICKSHEQPCH
     IVYTNFRPTP LQHYLFPAGG EGIYLVVNEK GEFREDNFTK AMGMLQDKAG EDPADPKSGK
     GRKGKSKKGG DKKAFDPVGP SDIQKIIKMI MLKNYNPVIV FAFSKRECEA LALAMSKFEF
     NTADEQDLIT NIFNNAMDNL APADRQLPQI SNLLPLLKRG IGIHHGGLLP ILKEVIEILF
     QEGLIKALFA TETFSIGLNM PAKTVVFTAA RKFDGREFRN LSSGEYIQMS GRAGRRGLDD
     RGVVIMMCDE KLEPSAAMNM VKGEADRLDS AFHLGYNMVL NLMKVEGISP EFMLERCFFQ
     FQNSAGVPML EDELRKEEEF KDSIIIPDEA LVAEYYDYRQ QLDQMASDFR DVITHPNYSL
     PFLQPGRLVK VKHQDMDFGW GVIISYQKRV PPKNRPMPQT EEIPPHEQYV LDVLLNCSTG
     SMLPKERNSS STSATPGGVL PCPSGQKGDP LVVPVLLSTI DSISHIRIFL PKDLRQSQAR
     ETVWKSVLEV QKRFPDGIAL LDPVQNMGIK DDKFQMLIKK IDMMEKKMFS SPLHKDPRLP
     EIYTLYSRKQ ERQQRIRALK KRIQATNDVL QMEELKCRKR VLRRLGFTTA DDIVDVKGRV
     ACEISTGDEL LLTELIFNGV FNPLSPEQCA GLLSCFVFTE KSEQVTKLKE ELAAPLRVMQ
     EVARRIAKVS KESKLPIDED EYVSSFKVEL MDAVVQWCRG ASFSDICKLT DQFEGSLIRV
     FRRLQELIRQ MSQAAKVIGN TELQEKFEKA SEMLERPNSV IFCSSLYL
//
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