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Database: UniProt
Entry: A0A0J8RKX3_COCIT
LinkDB: A0A0J8RKX3_COCIT
Original site: A0A0J8RKX3_COCIT 
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
//
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