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Database: UniProt
Entry: V5FMJ5_BYSSN
LinkDB: V5FMJ5_BYSSN
Original site: V5FMJ5_BYSSN 
ID   V5FMJ5_BYSSN            Unreviewed;       819 AA.
AC   V5FMJ5;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=PVAR5_7918 {ECO:0000313|EMBL:GAD99209.1};
OS   Byssochlamys spectabilis (strain No. 5 / NBRC 109023) (Paecilomyces
OS   variotii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX   NCBI_TaxID=1356009 {ECO:0000313|EMBL:GAD99209.1, ECO:0000313|Proteomes:UP000018001};
RN   [1] {ECO:0000313|Proteomes:UP000018001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=No. 5 / NBRC 109023 {ECO:0000313|Proteomes:UP000018001};
RX   PubMed=24407650; DOI=10.1128/genomeA.01162-13;
RA   Oka T., Ekino K., Fukuda K., Nomura Y.;
RT   "Draft genome sequence of the formaldehyde-resistant fungus Byssochlamys
RT   spectabilis No. 5 (anamorph Paecilomyces variotii No. 5) (NBRC109023).";
RL   Genome Announc. 2:E0116213-E0116213(2014).
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=3.6.4.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00001556};
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:GAD99209.1}.
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DR   EMBL; BAUL01000285; GAD99209.1; -; Genomic_DNA.
DR   AlphaFoldDB; V5FMJ5; -.
DR   eggNOG; KOG0922; Eukaryota.
DR   HOGENOM; CLU_001832_5_11_1; -.
DR   InParanoid; V5FMJ5; -.
DR   OrthoDB; 3682876at2759; -.
DR   Proteomes; UP000018001; Unassembled WGS sequence.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd17917; DEXHc_RHA-like; 1.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR048333; HA2_WH.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF118; ATP-DEPENDENT RNA HELICASE DHX33; 1.
DR   Pfam; PF21010; HA2_C; 1.
DR   Pfam; PF04408; HA2_N; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018001}.
FT   DOMAIN          139..331
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          386..562
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          330..355
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..85
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..115
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        330..345
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   819 AA;  90648 MW;  266BEFFAD8BA6225 CRC64;
     MPEKVHTRFE DSDDDAGKAT VRPQKKEQAA AADPVVTEPR EKKNKKRKRE ETAEVKPNTQ
     RVVIRDGEKP RAVSPAQEGE QKRNVKEASN GFNSQKKHQS KDQKMIRQGK PSSSLREKAR
     ALYEIRKKLP IFPHADEIRQ RLKKDDVMLL VGETGSGKST QIPQFLVDES WCRPKTVKVT
     AEDGKQKDVN VGGCIAITQP RRVAAISLAR RVADEMGTPL GSSSPGSRVG YSVRFDTSTS
     PSTKVKYLTE GMLLQEMLHD PWLTKYSAVL VDEVHERGVN VDLVLGFLRN IVSGKKEGRG
     GIPLKVLAMS ATADMESLLS FFQEGFDNAQ RAETDSTNAS DSAPNDQDSK ADEKQRQVAV
     CHIKGRQFPV KTIYTPDPVH DFVDAALKVI FQIHCKEPMP GDILVFLTGQ ETVEALEYLV
     NDYAIGMDPA LPKVQVLPLF AALPQAAQQR VFQPAPPRTR KIILATNIAE TSVTISGIRF
     VVDCGKAKMK QFRTRLGLDS LLVKPISKSA AIQRKGRAGR EAPGQCYRLY TEKDYLALQE
     TNTPEILRCD LSQAILTMKA RGVDDIVGFP FLTRPSREAL EKALLQLFNI QALEESGKIS
     SIGLQIAKLP LTAPLGRVLL AAAQNGPNCL LDVIDIISAL SVENIFLNTT SEEKKEEAEK
     ARRDLFRREG DHLTMLATVQ AYAAENTDRK AWAERHMVSH RAMQSVMDVR KQLTTQCRQA
     KLLPDANACA SLANNQPDPV LILKSFLTGF ATNTARIIPD GSYRTIVGNQ TVAIHPSSVL
     FGKKVEAIMY NEFVFTNRSY ARGVSAVQMD WVGEVLAGQ
//
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