ID A6R4P4_AJECN Unreviewed; 968 AA.
AC A6R4P4;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=HCAG_04602 {ECO:0000313|EMBL:EDN08092.1};
OS Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN08092.1, ECO:0000313|Proteomes:UP000009297};
RN [1] {ECO:0000313|Proteomes:UP000009297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
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 -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC PRP16 sub-subfamily. {ECO:0000256|ARBA:ARBA00038040}.
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; CH476658; EDN08092.1; -; Genomic_DNA.
DR AlphaFoldDB; A6R4P4; -.
DR STRING; 339724.A6R4P4; -.
DR VEuPathDB; FungiDB:HCAG_04602; -.
DR HOGENOM; CLU_001832_6_1_1; -.
DR OMA; VDVMFHR; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000009297; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
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; IPR011545; DEAD/DEAH_box_helicase_dom.
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:SF91; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE PRP16; 1.
DR Pfam; PF00270; DEAD; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000313|EMBL:EDN08092.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000009297}.
FT DOMAIN 309..472
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 494..669
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 914..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 914..941
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 968 AA; 108114 MW; 149E5AB9D5A9F628 CRC64;
MAREGSPKRR KLDSDRLTPT SSSQPSRHLY APRSRLQTNR DDKLVSTSRA STPRGIRNGD
STPHQEAFQG PESLVDIEDT LALDRDWYTG DELGHTFGDE THNPFGGADS TWADQQREAA
LSERKNNKRI SARAAQKQKD VDAWETNRML TSGVAQRREY DADFDDDEES TRVHLLVHDL
RPPFLDGRTV FTKQLDPVSA VRDPQSDMAV FSRKGSKVVR EKRAQKERQK QAQDATKMAG
TALGNLMGIK EDDGDSAAAI PAEEEGQHKG SKFAEHLKKS EGASAFSKSK SLKEQREYLP
AFAVREELLR VIRDNQVVIV VGQTGSGKTT QLTQFLYEDG YAKLGMIGCT QPRRVAAMSV
AKRVSEEMEV KLGGLVGYAI RFEDCTSNET AIKYMTDGVL LRESLVQPDL DKYSCIIMDE
AHERALNTDV LMGLIKKVLA RRRDLKLIVT SATMNAERFS KFYGGAPEFF IPGRTFPVDI
QYSRSPCEDY VDSAVKQVLA IHVSQGPGDI LVFMTGQEDI EVTCEIIAER LALLNDPPKI
SILPIYSQMP ADLQAKIFDR APPGVRKVIV ATNIAETSLT VDGIMYVVDA GFSKLKVYNP
RMGMDTLQIT PISQANASQR AGRAGRTGPG KAYHLFTELA FKNELYIQTI PEIQRTNLSN
TVLLLKSLGV KDLLDFDFMD PPPQDTITTS LFDLWALGAI DNLGDLTPMG RRMSAFPMDP
SLAKLLISAS EEYDCSEEML TIVSMLSVPG VFYRPKERQE ESDAAREKFF VPESDHLTLL
HVYTQWKSNG YSDACCGTDW DVIRKCICSG YYHQAARVKG IGEYINLRTS VTIQLHPTSA
LYGLGYLPDY VVYHELILTS KEYMSTVTSV DPRWLADLGG VFYSIKEKGY SARERRVTEH
EFNRRMEIEA QMAADRERAA EQKRKAAEED TLRRKQDAEG SSAHVGMKPV VKLPVRKPGS
YVPAGALH
//
