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Database: UniProt
Entry: A0A2C5YZQ3_9HYPO
LinkDB: A0A2C5YZQ3_9HYPO
Original site: A0A2C5YZQ3_9HYPO 
ID   A0A2C5YZQ3_9HYPO        Unreviewed;      1091 AA.
AC   A0A2C5YZQ3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=ATP-dependent RNA helicase DOB1 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CDD80_4111 {ECO:0000313|EMBL:PHH72990.1};
OS   Ophiocordyceps camponoti-rufipedis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX   NCBI_TaxID=2004952 {ECO:0000313|EMBL:PHH72990.1, ECO:0000313|Proteomes:UP000226431};
RN   [1] {ECO:0000313|EMBL:PHH72990.1, ECO:0000313|Proteomes:UP000226431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Map16 {ECO:0000313|EMBL:PHH72990.1,
RC   ECO:0000313|Proteomes:UP000226431};
RA   De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT   "Ant-infecting Ophiocordyceps genomes reveal a high diversity of potential
RT   behavioral manipulation genes and a possible major role for enterotoxins.";
RL   Submitted (JUN-2017) 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:PHH72990.1}.
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DR   EMBL; NJES01000377; PHH72990.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C5YZQ3; -.
DR   STRING; 2004952.A0A2C5YZQ3; -.
DR   OrthoDB; 1352at2759; -.
DR   Proteomes; UP000226431; 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};
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:UP000226431}.
FT   DOMAIN          166..322
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          402..606
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          375..396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          747..768
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..37
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..73
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..91
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1091 AA;  123099 MW;  4995FFEE603CDE42 CRC64;
     MDEMFDVFEG KAGPQSDSDG ERAKSRDKSK KRKADEAING AAASSSAPRE TVDVEMGDAT
     ESSNDDDSDE ESDTPSQQDK KRRKKEDGVG PVMTDAFKTE QSREVAAAKT LLPQDASLVL
     SHNIQHQVAL PPDLDYEYVP LSEHKSPDEP ARTWSFKLDP FQSLSVASIE RDESVLVSAH
     TSAGKTVVAE YAIAQCLKRN QRVIYTSPIK ALSNQKFRDF DGIFGDVGLM TGDVTINPTA
     SCLVMTTEIL RSMLYRGSEI MREVAWVVFD EIHYMRDKTR GVVWEETIIL LPDKVRYVFL
     SATIPNAFQF AEWIAKIHHQ ACHVVYTDFR PTPLQNYFYP TGGKGARIVV DEKGIFNEKN
     FNSVMEEVEE LKGSASADPN ARMKGKGKNK KINKGGADPG SPIYKIIKMT IKNNFNPVIV
     FNFSKRECED IAKKLSGLDF NDDSEKAMVR KVFESAIEQL SEQDRELPTL QYILPLLEKG
     IGVHHSGLLP LLKETIEILF QESLIKVLVA TETFSIGLNM PAKTVVFTQV TKWDGTAVRA
     ITSSEYVQMS GRAGRRGIDA RGIVLMMVDD KLEPSVAKQI VTGQQDKLNS AFHLGYNMIL
     NLLRIEAISP EYMLEKCFHQ FQNAASVPTL EKDLMALQQE RDDMSIPDEA TIKDYYQIRQ
     QLNTFTRDMR AVIQHPQYSL DFLQPGRLVQ IYNPKQSPDN VGGGVDFGWG VILNHSPRKG
     PRMGEPQYSA QESYMIEVLL PISASSKEIG PSQPAGEMPP GLSPATSEQD TIHEVVPCLL
     SCVKAISQIR IFMPKDGLKA GEDKEQAYKS LTEVKRRFPD GVPILDPIEN MDIADESFKK
     LMRKIEVLES RLLANPLHMS PLLPSLWDQY HNKMQIAEKI KEKKKTMAKA HSISQLEELK
     SRKRVLRRLG FINDSEVVQL KARVACEISS TEGHELLLSE LLFDRFFNEL PPDKCAAVLS
     CFVCEEKLET QALKEELQKP FREIQAKARI VAKVAQEAKL DMNPEEYALS FKWQLMETVY
     RWAQGRSFLE ISKMTKMYEG SLIRVFRRLE ELLRQMAQAA KVMGNDDLVK KFEECLQKVR
     RDIVAAQSLF L
//
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