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Database: UniProt
Entry: C6HHB6_AJECH
LinkDB: C6HHB6_AJECH
Original site: C6HHB6_AJECH 
ID   C6HHB6_AJECH            Unreviewed;      1198 AA.
AC   C6HHB6;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=DEAD/DEAH box helicase {ECO:0000313|EMBL:EER40200.1};
GN   ORFNames=HCDG_05597 {ECO:0000313|EMBL:EER40200.1};
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:EER40200.1, 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; GG692427; EER40200.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6HHB6; -.
DR   STRING; 544712.C6HHB6; -.
DR   VEuPathDB; FungiDB:HCDG_05597; -.
DR   eggNOG; KOG4150; Eukaryota.
DR   HOGENOM; CLU_000809_1_0_1; -.
DR   OMA; GAVHLHQ; -.
DR   Proteomes; UP000002624; Unassembled WGS sequence.
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; cd17923; DEXHc_Hrq1-like; 1.
DR   CDD; cd18797; SF2_C_Hrq; 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; IPR018973; MZB.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR47957; ATP-DEPENDENT HELICASE HRQ1; 1.
DR   PANTHER; PTHR47957:SF3; ATP-DEPENDENT HELICASE HRQ1; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF09369; MZB; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000313|EMBL:EER40200.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002624}.
FT   DOMAIN          400..583
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          623..776
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..68
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1198 AA;  133131 MW;  F8EB27C89C89F4C1 CRC64;
     MNNGLKRKAN ALNDGEHCAT EDGSGYLSRS PELPGEGQRG DVGRVYMSPS ARLPVEVATT
     TTLPTKTHDG PSAAPLQPPK GKRGRRSASS SSRSSSTSSR GRPKKSPATS TPPIPWPEPF
     KLLAQTHRAL NLVYTFCSAR KHFSTTFDNI KAAAEAQTGG RKLSVEDAAR VKVLIPRSVR
     FESVDKGVVD LVGVNEAKGT GKIWRDLEIE GMGHDAEDSE GLNPDGGGDV LIFEFVDGDL
     KKDPQRNSSR RRSKTDDIRV PVYSQKHMVT LIEKRNTKFS DAVDAFLAKC QDEDVDPVEK
     LEADKDMYVP VLPRSGANTP AAMRLPAQIP KERATIAEII ASIREMEWYT DQIVPDGHRV
     FDPQPAVYGD LTFALSQSLV NALYNTRGIT QFYSHQAEAI NNLHDGHNVI VSTSTSSGKS
     LIYQVPMLHE LEQDPHSRGM YIFPTKALAQ DQRRSLKELL GYIEGLEHLL VETFDGDTPM
     ADRNVIREEA RIIFTNPDML HITILPQESS WRTFLKNLKY VVVDELHVYN GLFGSHVAFI
     MRRLRRICAA VGNRHVKFIS CSATVANPEE HMKTIFGIDD VRLTDIDGSP SGRKEFICWN
     TPFRDPGDPS SGRGNSIQES SRLFCQLILR GVRVIAFCRI RKQCELLLAA VRDELKSLDR
     INVSRFVMGY RGGYSPQDRR KIERDMFEGK LLGIVATNAL ELGVDIGSLD AVITHGFPYS
     ISNLRQQSGR AGRRNKDSVS ILVGDSYATD QYYMRNPDEL FTKPNCELQV DLRNELVLEG
     HVQCAAFEMP IKPDEDTEYF GPQLHEFAYT RLTKDSLGFY HCHERFRPHP SKCVAIRDTE
     NNHYAIIDTT NNRNAVIEEI EESRVIFSIY EGGIFFHQGH PYMVKELNTD KRFARVIRVH
     VDWTTQQRDI TDIDPIETEA IRRISSTANT KAFFGAIKIR AIVYGYFKLD KKGRILDAVA
     LDNPPIEILS KGMWLDVPKQ ALDILKTRNL NAAAAIHAAE HAILSLMPTY IISSPGDVRT
     ECKVAVKELG PKHQQAMNQT RSQNVKLPPV PARQRPARLT FYDAKGGSSG SGIAAKAFEF
     VDSLLRRALG RIEACQCTSP QGCIECVCDE RCKEMNVVMS KAGAGVVLKC LLGIEVDVEA
     LPWGEDVLGE RGVASDVVSI QEGKELAGGL ETIVEAMEVS ARPGARARIY GVEGVVEG
//
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