ID A0A2B7XJD9_9EURO Unreviewed; 1467 AA.
AC A0A2B7XJD9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=ATP-dependent RNA helicase DHX29 {ECO:0008006|Google:ProtNLM};
GN ORFNames=GX51_00940 {ECO:0000313|EMBL:PGH08883.1};
OS Blastomyces parvus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=2060905 {ECO:0000313|EMBL:PGH08883.1, ECO:0000313|Proteomes:UP000224080};
RN [1] {ECO:0000313|EMBL:PGH08883.1, ECO:0000313|Proteomes:UP000224080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH130 {ECO:0000313|EMBL:PGH08883.1,
RC ECO:0000313|Proteomes:UP000224080};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PGH08883.1}.
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DR EMBL; PDNC01000007; PGH08883.1; -; Genomic_DNA.
DR STRING; 2060905.A0A2B7XJD9; -.
DR OrthoDB; 1095660at2759; -.
DR Proteomes; UP000224080; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; 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; 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; IPR011545; DEAD/DEAH_box_helicase_dom.
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:SF197; DEPENDENT RNA HELICASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G07950)-RELATED; 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; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000224080}.
FT DOMAIN 682..853
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 942..1107
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 338..365
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 15..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1467 AA; 165022 MW; B127376678FA2FC2 CRC64;
MAPNRKKKKP ASNPARGFTT VSVPSKLKAT ESSTSLSSAN APTQPQSELQ PPTESPSTTS
VGVQPQPELQ QLSPDKLQKH LEDAELQLLV EKYGVKCKSD SSRQVLKLET EKRILRTQAS
HLNVTDWLSP EILNEIMEKE KLEMKKSSEQ TSRPEMEEAQ IHTEEEELSI KLWTLRQSLK
GLGFTQQNID AALKATLQLY FNDPTASKDI VWGLDPALEW LGMNCDEKDL PLYDKSSSKL
SKIATEDAST FEKSNTSSTP STTGYNTPSD ARSKPRETQA KSTLSLSSPS SDESDSDPDS
LVPKYIELRT QLYTEQPDVF NQTNKRQRKG ISPLTLANDQ ASSNIARLKK KLAKIENDVL
FDRDQAENIW QIKLSELREH TAKFLQNAVA REPRPETPPI ELKDTQVQDA SDALIETILS
DSNENDDLLG GLFATDLEGP SASVSNTEAN DNTVVRSRDF GKPTGMNPRR VLEEGCRARD
SGCKISYKAI SATPFSHRKE IEIRWSKAQD IPPHVPLSDI SYRGDSHFIC AAMTSLSTPS
ALEAESYISM VALFAIFSHS QKESKIYMKL PAAWRELWDE FVHAKKEYDD EVDKGILKDI
QRLVQEQMST LEEDVVLLEN FRKRNSGVNS PVPRGDTRSK QTTRTQEQLQ DLWVQRSSTS
SFTSMESSRK ALPIWQFKDQ ILDTLAANQA IIICSETGSG KSTQIPSFIL EKELLSGHDC
KIYVTEPRRI SAMSLAKRVS EELGEDKNAV GTNRSLVGYA IRLESKISSS TRLIFATTGV
VVRMLERPKD FQDITHLVLD EVHERTIDSD FLLIILRRLM QERPDLKLVL MSATVDAKRF
SNYLHGAPIL DIPGRTFPVE VKYLEDAIEV TKHRPNSDGL SALTDDSDDA LDDAPQKPIE
DLASSLAGYS RQTRETVTGF DEYRLDYKLI VTLLSAIATK NEFKQYSKAI LIFMPGMAEI
RRLNDEILSE PLFNKGDWIV HALHSSIATE DQEKAFLIPP TSVRKIVIAT NIAETGITIP
DITAVIDTGK EKVMRFDERR QLSRLVESFI ARANAKQRRG RAGRVQSGLC FHLFTKFRHD
QLLSEQQTPE ILRLSLQDLV LRVKICNLGE VEQTLSEAID PPSPKNIRRA IEALKEVKAL
TNAENLTPLG RQLAKLPLDV FLGKLIIYGA FFRCLDSAVS IAAILSSKSP FITAVGSSTQ
RELAKLAFKR GNSDLLTIYN AYLAWKRHRS TPGMSEYAFC RKNYLSPQTL LNIEDVKMQL
LVSIVDAGLL SLDRAEQESL ARSRFTGRQR QFFTVPKRVD VNSENDLIVN SVIAWSFYPK
LLIREGKGWR NVANNQTVSL HPTSVNKRPD STVKWLSFYH IMQARSRYLN AHETSPVEDF
AVALLCGDVE FKLYAGIISI DGSRIRFSVK DWKSMLALKA LTTGIRNVLS FTIRNPRKEL
TASQQGWVDL WQQVFTEARE RELRRSG
//
