ID   B6H9G3_PENRW            Unreviewed;       809 AA.
AC   B6H9G3;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=Pc16g10890 {ECO:0000313|EMBL:CAP93759.1}, PCH_Pc16g10890
GN   {ECO:0000313|EMBL:CAP93759.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS   54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP93759.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP93759.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA   van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA   Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
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};
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DR   EMBL; AM920431; CAP93759.1; -; Genomic_DNA.
DR   RefSeq; XP_002561395.1; XM_002561349.1.
DR   AlphaFoldDB; B6H9G3; -.
DR   STRING; 500485.B6H9G3; -.
DR   GeneID; 8303779; -.
DR   KEGG; pcs:Pc16g10890; -.
DR   VEuPathDB; FungiDB:PCH_Pc16g10890; -.
DR   eggNOG; KOG0922; Eukaryota.
DR   HOGENOM; CLU_001832_5_11_1; -.
DR   OMA; KVKVWRH; -.
DR   OrthoDB; 3682876at2759; -.
DR   BioCyc; PCHR:PC16G10890-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c16.
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:UP000000724}.
FT   DOMAIN          134..325
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          376..552
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   COMPBIAS        1..18
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..61
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   809 AA;  89398 MW;  44FD809E122CB6F9 CRC64;
     MPEKVRTVFV DSDDEKIVQN KLSPPSTGEP ERKKKRNKKR KLDESITSTF ADQDEPREIA
     APAKQVETAE SVPRKLPAKV SQTNGLPAAK PYAKSKSKPF TDTKTNFIPL REKAKALLET
     RRKLPVFENA DLIRDLLREQ DVMLLVGETG SGKSTQIPQF LVDEFWCRPV PTQVTRDGKT
     EKKVVGGCIA ITQPRRVAAI SLARRVAEEM GTPLGSHSPA SKVGYSVRFD TSTSPSTRVK
     FLTEGMLLQE MLHDPNLTKY SAIVVDEVHE RGINVDLTLG FLRNLVSGNK EGRGGVPLKV
     VVMSATADME SLTDFFKQGF KQTEPAPKAI QAAEDEADKM DTSTPKDISV CHIKGRQFPV
     KTIYSPAPVH DFVDAALKVI FQIHQKEPMP GDILVFLTGQ ETVEALEHLV NEYAMGMDPS
     LPKILVLPLF AALPQAAQQR VFAPAPPRTR KIVLSTNIAE TSVTVSGVRH VVDCGKAKVK
     QFRTRLGLDS LLVKPISKSA AIQRKGRAGR EAPGQCFRLY TEKDYLALDE TNTPEILRCD
     LSQALLNMKA RGVDDIVGFP FLTRPPREAL EKALLQLLNI NALEDDGKIS PVGLHIAKLP
     LTPTLGRVLL AAAEHGSECL LDVIDIISCL SVENIFLNTT SEEKKEAAEA ARRDLYRREG
     DHLTMLTTVR VYAAEQADRK AWAERHLVSH RAMQSVMDVR KQLRTQCRQA KLLTNEALNN
     TSLHDPSPIL ILQSFLAGFA TNTARLVPDG SYRTIVGNQT VAIHPSSVLY GKKLEAIMYN
     EFVFTNRSYA RGVSAVQMDW VGEALAGKD
//