ID K5WBJ3_PHACS Unreviewed; 689 AA.
AC K5WBJ3;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN ORFNames=PHACADRAFT_27393 {ECO:0000313|EMBL:EKM56590.1};
OS Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS carnosa).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerochaete.
OX NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM56590.1, ECO:0000313|Proteomes:UP000008370};
RN [1] {ECO:0000313|EMBL:EKM56590.1, ECO:0000313|Proteomes:UP000008370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM56590.1,
RC ECO:0000313|Proteomes:UP000008370};
RX PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA Grigoriev I.V., Master E.R.;
RT "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT chrysosporium, to elucidate the genetic basis of the distinct wood types
RT they colonize.";
RL BMC Genomics 13:444-444(2012).
CC -!- FUNCTION: RNA helicase. {ECO:0000256|RuleBase:RU365068}.
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|RuleBase:RU365068};
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC {ECO:0000256|RuleBase:RU365068}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family.
CC {ECO:0000256|RuleBase:RU365068}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH930471; EKM56590.1; -; Genomic_DNA.
DR RefSeq; XP_007394047.1; XM_007393985.1.
DR AlphaFoldDB; K5WBJ3; -.
DR STRING; 650164.K5WBJ3; -.
DR GeneID; 18919500; -.
DR KEGG; pco:PHACADRAFT_27393; -.
DR HOGENOM; CLU_003041_26_6_1; -.
DR InParanoid; K5WBJ3; -.
DR OrthoDB; 276261at2759; -.
DR Proteomes; UP000008370; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd18787; SF2_C_DEAD; 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; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24031:SF384; DEAD-BOX ATP-DEPENDENT RNA HELICASE 31; 1.
DR PANTHER; PTHR24031; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 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, ECO:0000256|RuleBase:RU365068};
KW Helicase {ECO:0000256|RuleBase:RU365068};
KW Hydrolase {ECO:0000256|RuleBase:RU365068};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU365068};
KW Reference proteome {ECO:0000313|Proteomes:UP000008370};
KW RNA-binding {ECO:0000256|RuleBase:RU365068}.
FT DOMAIN 117..323
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 360..539
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 46..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..651
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..680
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 689 AA; 76677 MW; D40065868C015D2B CRC64;
MATPWMRAAL ASSSVLLRAS RPGRVLSKRA ALSSLRLAST AATQSLLTPS RTEVDSEETD
EDGASAVGNH QPKFATLAGK VSAQTLRAIS GIFKIDTMSV VQTVVLPLLP NLAEPYNPQN
KEARDLLVKA RTGTGKTLAF LIPAVEARMK ALDAAGKQAV IDAGLKNDHH IEMRAQRALS
RETAGTLIIS PTRELATQIA NEALRLTTRH EGFEVRLFVG GTSKRMQMRD WMRGRRDIVV
ATPGRMRDLL ENEPEVAKGM KDCKMLILDE ADTLLEMGFR EDIQAITSYI AKTPERQTFL
FSATVSREIQ QIARATLDRN HRFIDCVPVD SSPVHAHVPQ YHTVLPTAAH QIPHILRLLA
HDQLLHPGKS KTIIFLPTTK LTQLFSTFIR ELSSMCLPAG RNTRIYEIHS KRTMESRSKT
SQQFRMDKGN SVLISSDVSA RGVDYPGVTR VIQVGIPSST DQYVHRVGRT GRGRDKVGRA
DLVLLPWEIG FVTWQLTDIP LRPVTVTELT SQVKQLCEEQ NPDAAVVIDD MDAEVKRLMA
KLDPEAIKET LASVLGYYVG KSGELRVQKT VIVEGLKQWT VEACGLSSPP YISDSFLEKL
GMSDGRTKNF GTNRRFSYSS DGPAWQMRGN VEKNRHRMGT ERRESERERR GGGSYGGSSY
GDRPRYDRDD RPRRSYGFDS RPSGRPESF
//
