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Database: UniProt
Entry: C6HT40_AJECH
LinkDB: C6HT40_AJECH
Original site: C6HT40_AJECH 
ID   C6HT40_AJECH            Unreviewed;      1130 AA.
AC   C6HT40;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=HCDG_09371 {ECO:0000313|EMBL:EER36487.1};
OS   Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=544712 {ECO:0000313|EMBL:EER36487.1, ECO:0000313|Proteomes:UP000002624};
RN   [1] {ECO:0000313|Proteomes:UP000002624}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
RA   Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA   Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M.,
RA   Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA   Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA   Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA   Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA   Nusbaum C., Birren B.W.;
RT   "The genome sequence of Ajellomyces capsulatus strain H143.";
RL   Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GG692440; EER36487.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6HT40; -.
DR   STRING; 544712.C6HT40; -.
DR   VEuPathDB; FungiDB:HCDG_09371; -.
DR   eggNOG; KOG0923; Eukaryota.
DR   HOGENOM; CLU_001832_7_0_1; -.
DR   OMA; HITLMNV; -.
DR   Proteomes; UP000002624; 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:SF83; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE DHX16; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000313|EMBL:EER36487.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002624}.
FT   DOMAIN          492..656
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          678..854
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          105..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..164
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        193..216
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..283
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1130 AA;  127857 MW;  85940CBA560F7E48 CRC64;
     MDIRTYISDS LLRLTGASDA TVIDYILATT SSAKSAGSLH EKLGPFLDGD EGDIHSFCAE
     LWKRVRGGSS AEDGGKKTSK EKGGDGLKKR YKLVDMEEED VDVNAGLAPL QSTEAGKLRR
     KVKENGESGE SRDRDDDSRR KRAHRDARGE RKRGREGDHD RDGRHRSKKV RRRDDRDFED
     QWGDEDIPED EAEMHDERLQ DEGYQHEERE PRQHSRSPRS SSPSSDIDPE TKAERARQRD
     LKERDEFAKR LAKKDESKSK KIVEDRSSTK DSQAARRRAL ADDAAARSAA MPDLRLRSRQ
     EYLKKREAER LALLRKQVAE ETAELRENPN LTRREKEEFA KNREVLRLAE ERLRIDDYRD
     GYALPEDYIT EKGKIDRKRK EEALYKRYVD RDEHGHERFI TEHEEWENEQ TAKAKAQIQR
     AEFVDEGDYE YVFDDAQKIN FIMDSKLEGD RKPLTKDQLL FQQKLDAAEQ KAASIEETRK
     SLPIYRFREE IIRAVADHQV IIIVGETGSG KTTQIPQYLH EAGYTKGGMK IGCTQPRRVA
     AMSVAARVAE EMGVKVGNEV GYAIRFEDAT SDKTVLKYMT DGMLLRELLT EPDLGGYSAL
     MIDEAHERTV STDIACGLLK DIAKARPDLK LLISSATIDA QKFQKYFDDA PIFNIPGRRY
     PVDIHYTSQP EANYLAAAIT TVFHIHISQG AGDVLVFLTG QEEIEAAEQS IQETARKLGS
     KIPELIICPI YANLPSELQA KIFEPTPPGA RKVVLATNIA ETSLTIDGIV YVIDPGFVKE
     NVFNPRTGME SLVVTPCSRA SAGQRAGRAG RVGPGKCFRL YTKWAFYNEL EENTTPEIQR
     TNLNGVVLML KSLGIDQLLD FDFMDPPPAE TLIRALEQLY ALGALNDHGD LTKVGRQMAE
     FPTDPMLARA ILAADKYGCV EEVLSIIAML GEASALFFRP KDKKIHADSA RARFTIKDGG
     DHFSLLNVWN QWVDSDFSYV WARENFLQQR SLTRARDVRD QLAKLCDRVE VTITSAGSNN
     LAPIQKAITA GFFPNAARLQ RGGDSYRTVK NGQTVYLHPS STLFEVNPKW VIYYELVLTS
     KEYMRSNMPL QPEWLVEVAP HYHKKKDLET LGIDRKVPKG QGATGEKSKI
//
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