ID A0A0J8RKX3_COCIT Unreviewed; 1225 AA.
AC A0A0J8RKX3;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=CIHG_03075 {ECO:0000313|EMBL:KMU85291.1};
OS Coccidioides immitis H538.4.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=396776 {ECO:0000313|EMBL:KMU85291.1, ECO:0000313|Proteomes:UP000054563};
RN [1] {ECO:0000313|Proteomes:UP000054563}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H538.4 {ECO:0000313|Proteomes:UP000054563};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; DS016988; KMU85291.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J8RKX3; -.
DR STRING; 396776.A0A0J8RKX3; -.
DR VEuPathDB; FungiDB:CIHG_03075; -.
DR eggNOG; KOG0922; Eukaryota.
DR Proteomes; UP000054563; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
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 GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
DR CDD; cd17971; DEXHc_DHX8; 1.
DR CDD; cd21691; GH2-like_DHX8; 1.
DR CDD; cd05684; S1_DHX8_helicase; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR044762; DHX8/Prp22_DEXHc.
DR InterPro; IPR049588; DHX8_GH2-like.
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; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR049621; S1_DHX8_helicase.
DR InterPro; IPR003029; S1_domain.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF85; ATP-DEPENDENT RNA HELICASE DHX8; 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 Pfam; PF00575; S1; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 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.
DR PROSITE; PS50126; S1; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000313|EMBL:KMU85291.1};
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:UP000054563}.
FT DOMAIN 258..329
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 571..734
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 752..932
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 80..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1205..1225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 471..498
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 80..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1225 AA; 138033 MW; D6459CEE62C9CEB6 CRC64;
MDDLQSLELL SLVSRVTTEL QNHLGINDKT LAEFVIDQHL KCGGSFKEFK GSLEGMGAEF
PQSLMESIDR LVLAMHPKYK PKQNATDKHS SERENGNGAK INDIEMKAKV FKGLAMPDKA
PQWEDDDYTK PGEILRNDAG ADVLDDTLRC LKGLAAKARG KGDGAKSRKR SRSPSSDDYD
RGTRRREKYR SRSRSRSGER RYRRDEDLAH ERSGTKYGGR NDRYRDDYKD RRGRRGRDDD
DYFRRPPTPE LDERPILYKV YDGRVTGIKD FGAFVNLQGV RGKVDGLVHV SAMQDGARVN
HPSDLVSRAQ PVKVKVVSIQ GPRIGLSMKE VDQVTGRDLV PQRRIASGAN MERLDGTGAD
DRYGNLSSNV HVIEDDDDGK PLRNKKRLNS PERWEIKQLI ASGAVSAADY PDIDEEYHAT
LRGEGDFEEE EDVDIEVKDE EPPFLAGQTK QSLELSPIRV VRAPDGSLNR AAMAGTNLAK
ERRELRQQEA QDKAAEQASH VDLNAQWQDP MIAPDQRKFA SELRTAQKTD AIPEWKRVTQ
SKDVSYGKRT NLTIKQQRES LPVFKFRKQL LEAVHKNQLL IVVGDTGSGK TTQVTQYLAE
AGFANDGMIG CTQPRRVAAV SVAKRVAEEV GCRLGQEVGY TIRFEDCSSP DTKIKYMTDG
ILQREILLDP DLKKYSVIML DEAHERTIAT DVLFGLLKKT IKRRPDLKLI VTSATLDAEK
FSEYFNGCPI FTIPGRTFPV EIMYSREPET DYLDAALVTV MQIHLTEPEG DILLFLTGQE
EIDTSCEILY ERMKSLGPNV PELIILPVYS ALPSEMQSRI FDPAPPGSRK VVIATNIAET
SITIDHIYYV IDPGFVKQNA YDPKLGMDSL VVTPISQAQA KQRAGRAGRT GPGKCFRLYT
EAAFQSEMLP TSIPEIQRQN LSHTILMLKA MGINDLLHFD FMDPPPTNTM LTALEELYAL
SALDDEGLLT RLGRKMADFP MEPALAKVLI ASVDMGCSDE VLSIVAMLSV QNVFYRPKEK
QQQADQKKSK FHDPHGDHLT LLNVYNAWKN SRYSNPWCFE NFIQARQMRR AQDVRQQLVS
IMERYHHKIV SCGRNTIKVR KALCSGFFRN SARKDPQEGY KTLIEGTPVY MHPSSSLFGK
AAEHVIFHTL VLTTKEYMHC TTAIEPKWLV EAAPTFFKVA PTDRLSKRKK AERIQPLHNR
FAGEDDWRLS AQRRQGRGGG GGTWG
//