ID   SUB2_AJECN              Reviewed;         442 AA.
AC   A6R603;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 2.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=ATP-dependent RNA helicase SUB2;
DE            EC=3.6.4.13;
GN   Name=SUB2; ORFNames=HCAG_05061;
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma;
OC   unclassified Histoplasma.
OX   NCBI_TaxID=2059318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
CC   -!- FUNCTION: ATP-binding RNA helicase involved in transcription elongation
CC       and required for the export of mRNA out of the nucleus. SUB2 also plays
CC       a role in pre-mRNA splicing and spliceosome assembly. May be involved
CC       in rDNA and telomeric silencing, and maintenance of genome integrity
CC       (By similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC       family of RNA helicases and controls ATP binding and hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DECD subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDN08562.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH476659; EDN08562.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001539594.1; XM_001539544.1.
DR   AlphaFoldDB; A6R603; -.
DR   SMR; A6R603; -.
DR   STRING; 339724.A6R603; -.
DR   PRIDE; A6R603; -.
DR   EnsemblFungi; EDN08562; EDN08562; HCAG_05061.
DR   GeneID; 5446516; -.
DR   KEGG; aje:HCAG_05061; -.
DR   HOGENOM; CLU_003041_1_0_1; -.
DR   OrthoDB; 779000at2759; -.
DR   Proteomes; UP000009297; Unassembled WGS sequence.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Helicase; Hydrolase; mRNA processing; mRNA splicing;
KW   mRNA transport; Nucleotide-binding; Nucleus; Reference proteome;
KW   RNA-binding; Spliceosome; Transport.
FT   CHAIN           1..442
FT                   /note="ATP-dependent RNA helicase SUB2"
FT                   /id="PRO_0000310221"
FT   DOMAIN          90..265
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          293..438
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           59..87
FT                   /note="Q motif"
FT   MOTIF           212..215
FT                   /note="DECD box"
FT   BINDING         103..110
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   442 AA;  49388 MW;  A3C5AF0A1216F8B3 CRC64;
     MSHEEDLIDY SDEELQATDA AAGTAAAGAN GAAPKKEGDL TVSGARADKK GSYVGIHSTG
     FRDFLLKGEL LRAITDCGFE HPSEVQQVCI PTAILNVDVL CQAKSGLGKT AVFVLTTLHQ
     LEPVPGECSI LVMCHTRELA YQIKNEYARF SKYLPDVKTA VFYGGTPMQK DIELLSSKDT
     YPSIVVGTPG RLNALVRDKK LSLRNIKAFV LDECDKMLDQ IDMRRDVQEI FRATPADKQV
     MMFSATLSQE VRPICKKFMR NPLEVYVDDD TKLTLHGLLQ YYIKLGESEK NRKLNELLDS
     LEFNQVIIFV KSTQRASELD KLLRECNFPS IAVHSGVSQE ERIKRYKEFK EFNKRICVAT
     DVFGRGIDIE RINLAINYDL PADADSYLHR VGRAGRFGTK GLAISFVSSE QDQEVLKDIE
     KRFEVALPEY PQGGVDSSAY MA